COMPOSITIONS AND METHODS FOR THE THERAPY AND DIAGNOSIS OF ACNE VULGARIS

Abstract: Compositions and methods for the therapy and diagnosis of acne vulgaris and other related conditions are disclosed. Compositions may comprise one or more <i>Propionibacterium acnes</i> proteins, immunogenic portions thereof, or polynucleotides that encode such portions. Alternatively, a therapeutic composition may comprise an antibody that binds a <i>Propionibacterium acnes</i> protein, antigen presenting cell that expresses a <i>Propionibacterium acnes</i> protein, or a T cell that is specific for cells expressing such a protein. Such compositions may be used, for example, for the prevention and/or treatment of acne.

Description: COMPOSITIONS AND METHODS FOR THE THERAPY AND DIAGNOSIS OF ACNE VULGARIS TECHNICAL FIELD The present invention relates generally to therapy and diagnosis of acne, particularly those forms of acne that are caused in whole or in part by the organism Propiombacterium acnes or a related organism. The invention is more specifically related to Propiombacterium acnes polynucleotides, polypeptides, antibodies and other compositions for the prevention, treatment and/or diagnosis of acne. BACKGROUND OF THE INVENTION Members of the genera Propiombacterium comprise a group of anaerobic non-spore-forming gram-positive rods that are the predominant member of anaerobic flora from co junctiveal cultures of adults and children. Propionibacteria have been implicated in a number of human conditions, including SAPHO syndrome (synovitis, acne, pustulosis, hypertosis, and osteomyelitis), uveitis and endophthalamitis. The organism has also been shown to be pathogenic in infections of bone, joints and the central nervous system. Several lines of evidence support a particularly important role for Propiombacterium acnes in the inflammatory lesions associated with the skin disorder acne vulgaris. Acne vulgaris is a disease of the pilosebaceous follicle that results in inflammatory and non-inflammatory clinical lesions. In most patients, there is a mixture of non-inflammatory comedones and inflammatory papules, pustules and nodules. Correlations have been observed between the severity of inflammatory acne and the level of circulating antibodies to P. acnes. There are several mechanisms by which Propiombacterium acnes is currently thought to lead to disruption of the follicular epithelium and subsequent inflammatory reactions in the surrounding dermis. In addition to its ability to stimulate both the classical and alternative complement pathways, Propiombacterium acnes also has been reported to produce small molecular weight, serum-independent neutrophil chemotactic factors that can attract neutrophils through the epithelial wall to Propiombacterium acnes within the sebaceous follicle lumen. Ingestion of Propiombacterium acnes by neutrophils in the presence of antibody specific for Propiombacterium acnes results in the release of hydrolases that may contribute to the disruption of the follicular wall. Along with neutrophil infiltration of the sebaceous follicular epithelium, lymphocyte accumulation and infiltration have been described as early events in pathophysiology of inflammatory acne. In spite of considerable research into therapies for acne vulgaris, and other conditions associated with Propionobacterium, there remains a need for alternative approaches for their effective treatment. Accordingly, there is a need in the art for improved methods for the prophylactic and/or therapeutic treatment of acne. The present invention fulfills these needs and further provides other related advantages. SUMMARY OF THE INVENTION Briefly stated, the present invention provides compositions and methods for the diagnosis and therapy of skin and other disorders, such as acne vulgaris, that are at least partly caused or contributed to in mammals by Propiombacterium acnes and other related organisms. In one aspect, the present invention provides polypeptides comprising at least a portion of a Propiombacterium acnes protein, or a fragment or variant thereof. Certain portions and other variants are immunogenic, such that the ability of the variant to react with antigen-specific antisera is not substantially diminished. Within certain embodiments, the polypeptide comprises a sequence that is encoded by a polynucleotide sequence selected from the group consisting of: (a) sequences recited in SEQ ID NOs: 1-299; (b) variants and biological functional equivalents of a sequence recited in SEQ ID NOs: 1-299; and (c) complements of a sequence of (a) or (b). In specific embodiments, the polypeptides of the present invention comprise at least a portion of a Propiombacterium acnes protein that includes an amino acid sequence selected from the group consisting of SEQ ID NOs: 300-29,212 and variants and derivatives thereof. Moreover, the present invention provides polynucleotides that encode a polypeptide as described above, or portions thereof (such as a portion encoding at least 15, 25, 35, 45, 55, etc., contiguous amino acid residues of a Propiombacterium acnes protein), as well as expression vectors comprising such polynucleotides and host cells transformed or transfected with such expression vectors. P. acnes polypeptides have been identified herein by a variety of experimental and bioinformatic approaches. For example, in one aspect, the present invention provides P. acnes transferase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 927, 1051, 2084, 2525, 2767, 2891, 3255, 3443, 4287, 5495, 5751, 6133, 6186, 10674, 12113, 12316, 12334, 12347, 12610, 12868, 14234, 14307, 14769, 16001, 16403, 17869, 18690, 20108, 20783, 21258, 22948, 24326, 24787, 25803, 26333, 27012, 27019, 27138, 27141, 27307, 28925, 29085 and 29204. The mvention further provides P. acnes enterotoxin polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 23419. The invention further provides P. acnes lipoprotein-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 6740, 12271, 15138, 16073, 19399, 19447, 21711, 24622, 26161 and 28123. The invention further provides P. acnes membrane-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 1469, 1909, 2482, 2676, 2905, 3081, 3151, 3773, 4114, 4725, 5864, 6515, 7380, 7425, 7576, 7710, 8042, 8324, 8370, 9100, 9782, 10658, 13122, 13897, 15890, 16337, 16713, 17093, 17631, 19021, 19085, 19108, 19154, 19407, 20132, 20207, 20382, 20395, 20512, 21074, 22771, 23809, 24355, 24770, 24800, 24826, 26504, 26798, 27079, 27470, 27475 and 29132. The invention further provides R. acnes permease-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 9383, 9430, 11564, 12052, 12110, 12261, 14484, 14820, 15476, 21154, 21180, 21983, 22019, 22456, 24300, 26784 and 27769. The invention further provides P. acnes protease/proteinase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 10003, 10107, 10197, 17403, 18436, 21368,1585, 2909, 3071, 8768, 10789, 11032, 11033 and 12785. The invention further provides P. acnes protein A-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 23820. The invention further provides P. acnes secreted polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 3609, 4118, 6124, 8003, 10273, 11816, 14351, 14514, 16142, 17629, 21155, 22996, 23418 and 24185. The invention further provides P. acnes dismutase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 3608. The invention further provides R acnes adhesin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 17237. The invention further provides P. acnes transporter-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 3979, 4157, 4686, 5329, 6589, 6709, 6896, 7028, 7564, 8125, 8126, 8170, 8541, 9004, 9383, 9430, 11564, 11565, 11624, 11682, 12346, 12429, 12563, 12718, 14103, 14484, 14742, 15884, 16279, 16327, 17306, 17307, 18134, 18177, 18245, 19157, 19191, 19359, 19566, 19581, 20311, 20479, 20923, 20926, 21153, 21172, 22819, 23880, 23891, 25720, 26021, 26025, 26281, 26490, 26700, 26784, 26977, 27523, 28116, 28250 and 28385. The invention further provides P. acnes haemolysin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 7017. The invention further provides R acnes penicillin binding-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 10657, 16595 and 25267. The invention further provides R acnes sialidase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 6710, 16380, 26503 and 27212. The invention further provides P. acnes siderophore-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 6887. The invention further provides P. acnes lipase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 13402. The invention further provides R acnes enterobactin receptor-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 5334 and 11075. The invention further provides isolated cohemolysin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 15127, 25540, 6706, 23076, 8751 and 27533. The invention further provides isolated polypeptides, such as those identified herein as described in Examples 6 and 7, comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 20036, 19872, 6373, 8769, 5991, 19299, 5011, 12317, 11062, 4958, 6923, 11989, 24369, 21491, 7887, 10447, 3070, 7878, 25103, 6868, 9121, 24474, 12029, 20955, 16555, 15237, 20973, 20475, 15259, 6427, 4967, 20100, 10141, 15657, 3608, 16608, 21710, 25380, 4853, 25957, 9071, 3659, 13512, 3697, 7384, 24722, 10674, 1282, 1209, 6501, 3691, 12347, 21762, 15197, 1165, 23091, 6428, 5429, 24758, 3590, 3723, 9106, 12217, 7270, 2913, 1187, 1585, 16537, 24679, 26397, 26691, 7397, 6695, 6892, 19926, 4754, 26692, 15670, 3652, 20510, 3449, 20070, 19245, 20108, 19427, 10564, 10678, 21172, 21780, 3334, 6338, 5379, 11580, 15693, 9994, 24973, 20684, 7865, 16573, 11864, 12324, 20439, 1230, 14278, 3412, 12317, 5991, 6923, 10741, 5373, 19299, 383, 1284, 12228, 26402, 4673, 7887, 9004, 384, 25103, 6373, 12029, 20036, 16555, 17521, 20476, 15237, 24581, 3659, 14031, 9071, 4958, 15259, 12904, 5440, 23560, 3697, 3608, 25957, 7384, 24722, 15863, 8135, 20585, 3691, 12217, 16439, 1645, 5514, 21710, 24895, 4853, 23420, 5437, 1278, 16992, 12126, 20934, 20475, 17970, 20955, 3070, 6564, 9069, 12666, 7864, 18692, 2453, 1209, 20973, 7419, 15197, 23591, 20100, 23065, 6337, 10989, 1585, 17841 and 6868. The invention further provides, for example, isolated polypeptides comprising at least an immunogenic fragment of a polypeptide encoded by a DNA molecule identified by serological expression cloning, as described herein, such as a polypeptide sequence selected from the group consisting of SEQ ID NOs: 25131, 25133, 25135, 25163, 25164, 25165, 25166, 25167, 25168, 25169, 25192, 25193, 25215, 25216, 25217, 25218, 7729, 25957, 6884, 7653, 7668, 20966, 20984, 21002, 905, 906, 1008, 5541, 25957, 5527, 5541, 25086, 25088, 25089, 25090, 25103, 25130, 25131, 25133, 25135, 25163, 25164, 25165, 25166, 25167, 25168, 25169, 25192, 25193, 25215, 25216, 25217, 25218, 25922, 25938, 25957, 5527, 5541, 25088, 25089, 25090, 25103, 25131, 25133, 25135, 25163, 25164, 25165, 25166, 25167, 25215, 25216, 25217, 25089, 25103, 25135, 25164, 25165, 25166, 25216, 6695, 5527 and 5541. The invention further provides polypeptide compositions encoded by any one ofthe DNA sequences set forth in SEQ ID NOs: 1-299. For example, the invention provides polypeptides encoded by SEQ ID NO: 1 such as those selected from the group consisting of SEQ ID NOs: 318, 319, 337, 340, 348, 351, 364, 365, 366, 369, 373, 374, 382, 383, 384, 398, 418, 427, 428, 429, 431, 443, 444, 470, 486 and 28650. The invention further provides polypeptides encoded by SEQ ID NO: 2 such as those selected from the group consisting of SEQ ID NOs: 493, 504, 506, 513, 518, 524, 547, 559, 572, 578, 589, 593, 600, 617, 620, 624, 632, 642, 644, 665, 666, 692, 701, 709, 710, 716, 727, 736, 737, 771, 786, 787, 789, 790, 791, 792, 805, 807, 808 and 812. The invention further provides polypeptides encoded by SEQ ID NO: 3 such as those selected from the group consisting of SEQ ID NOs: 814, 853, 873, 878, 885, 898, 899, 905, 906, 917, 921, 927, 928, 930, 970, 975, 993, 995, 997, 1007, 1008, 1012, 1026 and 28654. The invention further provides polypeptides encoded by SEQ ID NO: 4 such as those selected from the group consisting of SEQ ID NOs: 1049, 1051, 1054, 1056, 1081, 1123 and 28657. The invention further provides polypeptides encoded by SEQ ID NO: 5 such as those selected from the group consisting of SEQ ID NOs: 1127, 1133, 1137, 1138, 1153, 1159, 1161, 1162, 1163, 1165, 1167, 1168, 1171, 1172, 1181, 1187, 1196, 1203, 1209, 1212, 1215, 1225, 1229, 1230, 1231, 1235, 1251, 1252, 1269, 1270, 1274, 1275, 1277, 1278, 1282, 1284, 1285, 1289, 1290, 1292, 1293, 1294, 1295, 1297, 1300, 1318, 1323, 1324, 1332, 1334, 1335, 1338, 1339, 1340, 1341, 1343, 1358, 1359, 1375, 1376, 1377, 1378, 1379, 1383, 1385, 1389, 1390, 1391, 1393, 1394, 1396, 1411, 1412, 1421,1422, 1425 and 28660. The invention further provides polypeptides encoded by SEQ ID NO: 6 such as those selected from the group consisting of SEQ ID NOs: 1434, 1437, 1442, 1444, 1445, 1446, 1447, 1449, 1452, 1460, 1463, 1469, 1483, 1488, 1489, 1490, 1491, 1508, 1522, 1523, 1524, 1535, 1550, 1567, 1575, 1585, 1586, 1588, 1595, 1596, 1599, 1603, 1607, 1608, 1611, 1616, 1624, 1626, 1627, 1632, 1635, 1636, 1637, 1645, 1646, 1652 and 28661. The invention further provides polypeptides encoded by SEQ ID NO: 7 such as those selected from the group consisting of SEQ ID NOs: 1670, 1674, 1708, 1714, 1716, 1731, 1734, 1744, 1754, 1756, 1767, 1776, 1779, 1780, 1795, 1800, 1827, 1832, 1841 and 1845. The invention further provides polypeptides encoded by SEQ ID NO: 8 such as those selected from the group consisting of SEQ ID NOs: 1871, 1884, 1895, 1906, 1907, 1909, 1938, 1941, 1952, 1955, 1957, 1968, 1971, 1973, 1979, 1980, 1998, 2004, 2005, 2020, 2025, 2028, 2035, 2036, 2040, 2044, 2084, 2088, 2114, 2127, 2137, 2150, 2153, 2158, 2164, 2180, 2190, 2192, 2198, 2203, 2215, 2218, 2228, 2230, 2231, 2240, 2243, 2246, 2258, 2259, 2260, 2265 and 2278. The invention further provides polypeptides encoded by SEQ ID NO: 9 such as those selected from the group consisting of SEQ ID NOs: 2288, 2292, 2299, 2300, 2303, 2305, 2306, 2310, 2311, 2315, 2316, 2324, 2326, 2329, 2344, 2346, 2357, 2378, 2379, 2388, 2398, 2402, 2403, 2405, 2410, 2412, 2414, 2417, 2420, 2425, 2427, 2447, 2453, 2457, 2458, 2460, 2461, 2462, 2469, 2474, 2482, 2483, 2487, 2492, 2494, 2497, 2506, 2507 and 28666. The invention further provides polypeptides encoded by SEQ ID NO: 10 such as those selected from the group consisting of SEQ ID NOs: 2512, 2518, 2522, 2525, 2535, 2544, 2548, 2549, 2553, 2576, 2577, 2578, 2586, 2604, 2617, 2618, 2632, 2648, 2657, 2666, 2672, 2676, 2682, 2685, 2703, 2713, 2724, 2742, 2743, 2745, 2748, 2752, 2755, 2760, 2767, 2769, 2784, 2790, 2798, 2799, 2800, 2801, 2802, 2813, 2824, 2825, 2826, 2827, 2828, 2830, 2845, 2850, 2880, 2891, 2894, 2905, 2907, 2909, 2913, 2925, 2926, 2927, 2937, 2940, 2942, 2952, 2956, 2978, 2984, 2986, 2987, 2988, 2989, 2997, 3004, 3013, 3018, 3038, 3039, 3051, 3060, 3061, 3070, 3071, 3073, 3075, 3076, 3079, 3081, 3091, 3098, 3112, 3114, 3118, 3119, 3121, 3128, 3138, 3151, 3155, 3160, 3176, 3178, 3179, 3181, 3188, 3195, 3197, 3204 and 28668. The invention further provides polypeptides encoded by SEQ ID NO: 11 such as those selected from the group consisting of SEQ ID NOs: 3217, 3222, 3235, 3255, 3261, 3267, 3272, 3287, 3289, 3296, 3297, 3301, 3302, 3313, 3314, 3315, 3317, 3319, 3320, 3327, 3331, 3334, 3342, 3349, 3369, 3370, 3371, 3373, 3375, 3381, 3382, 3390, 3402, 3403, 3418, 3422, 3425, 3429, 3437, 3441, 3442, 3443, 3449, 3451, 3454, 3455, 3457, 3458, 3471, 3483, 3489, 3499, 3522, 3523, 3525, 3528 and 3536. The invention further provides polypeptides encoded by SEQ ID NO: 12 such as those selected from the group consisting of SEQ ID NOs: 3539, 3544, 3549, 3551, 3552, 3555, 3558, 3559, 3560, 3572, 3584, 3585, 3586, 3587, 3589, 3591, 3593, 3594, 3608, 3609, 3625, 3626, 3627, 3632, 3635, 3652, 3658, 3659, 3661, 3666, 3682, 3683, 3687, 3690, 3691, 3697, 3701, 3708, 3721, 3722, 3723, 3731, 3736 and 28674. The invention further provides polypeptides encoded by SEQ ID NO: 13 such as those selected from the group consisting of SEQ ID NOs: 3755, 3759, 3763, 3764, 3767, 3773, 3776, 3783, 3799, 3807, 3808, 3809, 3815, 3816, 3817, 3821, 3828, 3831, 3835, 3837, 3838, 3849, 3866, 3875, 3889, 3904, 3909, 3916, 3917, 3918, 3923, 3925, 3945, 3947, 3955, 3956, 3969, 3979, 3988, 4004, 4023, 4024, 4060, 4073, 4080, 4096, 4101, 4102, 4103, 4111, 4114, 4118, 4122, 4134, 4135, 4143, 4149 and 4152. The invention further provides polypeptides encoded by SEQ ID NO: 14 such as those selected from the group consisting of SEQ ID NOs: 4157, 4169, 4171, 4174, 4179, 4188, 4189, 4198, 4207, 4211, 4213, 4220, 4224, 4227, 4240, 4247, 4249, 4258, 4261, 4262, 4265, 4274, 4275, 4278, 4287, 4306, 4307, 4308, 4309, 4310, 4311, 4328, 4333, 4336, 4339, 4345, 4346, 4350 and 4351. The invention further provides polypeptides encoded by SEQ ID NO: 15 such as those selected from the group consisting of SEQ ID NOs: 4362, 4365, 4370, 4373, 4378, 4380, 4386, 4389, 4393, 4394, 4407, 4408, 4417, 4418, 4428, 4435, 4437, 4438, 4439, 4442, 4450, 4454, 4458, 4460, 4462, 4466, 4474, 4495, 4496, 4510, 4511, 4522, 4529, 4531, 4533, 4536, 4539, 4545, 4552, 4553, 4570, 4577, 4581, 4587, 4591, 4594, 4599, 4605, 4612, 4616, 4617, 4618, 4620, 4622, 4630, 4634, 4640, 4643, 4646, 4651, 4659, 4666, 4673, 4678 and 28680. The invention further provides polypeptides encoded by SEQ ID NO: 16 such as those selected from the group consisting of SEQ ID NOs: 4686, 4687, 4694, 4723, 4725, 4742, 4745, 4749, 4754, 4757, 4763, 4766, 4767, 4771, 4772, 4789, 4792, 4825, 4832, 4834, 4847, 4853, 4857, 4866, 4871, 4873, 4875, 4877, 4879, 4887, 4888, 4890, 4897, 4907, 4938, 4945, 4947, 4948, 4950, 4951, 4952, 4958, 4966, 4967, 4968, 4975, 4977, 4978, 4986, 4988, 4996, 5001, 5006, 5008, 5009, 5011, 5017, 5021, 5022, 5025, 5035, 5037, 5038, 5040, 5053, 5054, 5056, 5057, 5062, 5068, 5079, 5111, 5120, 5124, 5125, 5134, 5141, 5142, 5143, 5144, 5149, 5156, 5157, 5160, 5163, 5167, 5179, 5180, 5181, 5184, 5185, 5186, 5187, 5189, 5201, 5218, 5247, 5259, 5269, 5270, 5271, 5281, 5282, 5283, 5286, 5292, 5293, 5302, 5303, 5304, 5306, 5311, 5318, 5319, 5320, 5321, 5323, 5326, 5328, 5329, 5332, 5334, 5338, 5341 and 5347. The invention further provides polypeptides encoded by SEQ ID NO: 17 such as those selected from the group consisting of SEQ ID NOs: 5354, 5356, 5358, 5373, 5379, 5389, 5396, 5397, 5399, 5417, 5429, 5437, 5438, 5440, 5441, 5446, 5452, 5463, 5478, 5493, 5495, 5503, 5511, 5512, 5514, 5519, 5520, 5523, 5527, 5541, 5544, 5559, 5568, 5577, 5585, 5586, 5593, 5606, 5607, 5613, 5614, 5639, 5648, 5655, 5662, 5664, 5671, 5673, 5675, 5678, 5716, 5737, 5738, 5747, 5751, 5756, 5758, 5759 and 28685. The invention further provides polypeptides encoded by SEQ ID NO: 18 such as those selected from the group consisting of SEQ ID NOs: 5770, 5773, 5774, 5776, 5783, 5789, 5810, 5811, 5823, 5834, 5844, 5847, 5852, 5855, 5858, 5860, 5861, 5863, 5864, 5865, 5867, 5868, 5872, 5884, 5886, 5895, 5900 and 28687. The invention further provides polypeptides encoded by SEQ ID NO: 19 such as those selected from the group consisting of SEQ ID NOs: 5922, 5928, 5932, 5975, 5991, 5993, 6001, 6032, 6034, 6042, 6055, 6061, 6084, 6089, 6104, 6108, 6109, 6122, 6124, 6129, 6132, 6133, 6137, 6140, 6152, 6153, 6154, 6164, 6174, 6185, 6186, 6198, 6202 and 6213. The invention further provides polypeptides encoded by SEQ ID NO: 20 such as those selected from the group consisting of SEQ ID NOs: 6225, 6245, 6248, 6252, 6259, 6268, 6270, 6278, 6279, 6280, 6288, 6301, 6302, 6304, 6318, 6321, 6322, 6327, 6331, 6337, 6338, 6342, 6346, 6360, 6361, 6362, 6367, 6373, 6404, 6417, 6427, 6428, 6429, 6432, 6448, 6455, 6482, 6483, 6484, 6496, 6500, 6501, 6505, 6507, 6508, 6511, 6515, 6573, 6576, 6580, 6589, 6597, 6598, 6599, 6607, 6610, 6618, 6639, 6643, 6658, 6666, 6684, 6695, 6698, 6702, 6706, 6709 and 6710. The mvention further provides polypeptides encoded by SEQ ID NO: 21 such as those selected from the group consisting of SEQ ID NOs: 6711, 6712, 6722, 6731, 6732, 6740, 6741, 6756, 6773, 6782, 6784, 6794, 6795, 6796, 6849, 6852, 6868, 6870, 6875, 6877, 6879, 6881, 6884, 6887, 6889, 6890, 6892, 6893, 6894, 6896, 6908, 6916, 6923 and 28692. The invention further provides polypeptides encoded by SEQ ID NO: 22 such as those selected from the group consisting of SEQ ID NOs: 6927, 6929, 6930, 6931, 6955, 6956, 6957, 6958, 6961, 6962, 6970, 6985, 6996, 6998, 7010, 7016, 7017, 7018, 7026, 7028, 7035 and 7037. The invention further provides polypeptides encoded by SEQ ID NO: 23 such as those selected from the group consisting of SEQ ID NOs: 7040, 7054, 7060, 7066, 7071, 7075, 7084, 7085, 7091, 7092, 7093, 7100, 7102, 7108, 7112 and 7117. The invention further provides polypeptides encoded by SEQ ID NO: 24 such as those selected from the group consisting of SEQ ID NOs: 7125, 7130, 7131, 7132, 7152, 7163, 7164, 7168, 7174, 7176, 7177, 7197, 7209, 7210, 7211, 7212, 7224, 7225, 7258, 7259, 7260, 7261, 7270, 7272, 7274, 7277, 7287, 7292, 7294, 7297, 7309, 7310, 7316, 7318, 7338, 7345, 7352, 7356 and 28697. The invention further provides polypeptides encoded by SEQ ID NO: 25 such as those selected from the group consisting of SEQ ID NOs: 7380, 7381, 7383, 7384, 7386, 7388, 7390, 7394, 7397, 7406, 7412, 7419, 7421, 7422, 7425, 7426, 7438, 7448, 7452, 7466, 7468, 7469, 7474, 7478, 7482, 7488, 7489, 7490, 7491, 7502, 7504 and 28698. The invention further provides polypeptides encoded by SEQ ID NO: 26 such as those selected from the group consisting of SEQ ID NOs: 7511, 7564, 7576, 7578, 7601 and 28701. The invention further provides polypeptides encoded by SEQ ID NO: 27 such as those selected from the group consisting of SEQ ID NOs: 7605, 7606, 7607, 7622, 7623, 7632, 7635, 7636, 7641, 7648, 7653, 7661, 7662, 7663, 7668, 7673, 7674, 7683 and 7689. The invention further provides polypeptides encoded by SEQ ID NO: 28 such as those selected from the group consisting of SEQ ID NOs: 7699 and 7710. The invention further provides polypeptides encoded by SEQ ID NO: 29 such as those selected from the group consisting of SEQ ID NOs: 7721, 7725, 7729, 7731, 7739, 7741, 7742, 7752, 7764, 7765, 7767, 7772, 7781, 7787, 7788, 7789, 7793, 7794, 7801, 7803, 7806, 7807, 7822, 7828, 7829, 7831, 7832, 7839, 7841, 7859, 7865, 7878, 7879, 7882, 7883, 7887, 7889, 7891, 7894, 7895, 7897 and 7898. The invention further provides polypeptides encoded by SEQ ID NO: 30 such as those selected from the group consisting of SEQ ID NOs: 7900, 7914, 7915, 7920, 7922, 7925, 7929, 7932, 7942, 7967, 7968, 7970, 7981, 7990, 7991, 7996, 8003, 8014, 8015, 8023, 8024, 8036, 8037, 8039, 8040, 8041, 8042, 8047, 8055, 8066, 8067, 8075, 8104, 8108, 8118, 8120, 8121, 8122, 8125, 8126, 8127, 8153, 8163 and 8170. The invention further provides polypeptides encoded by SEQ ID NO: 31 such as those selected from the group consisting of SEQ ID NOs: 8188, 8208, 8214, 8215, 8218, 8229, 8239, 8242, 8244, 8246, 8249, 8253, 8263, 8279, 8280, 8282, 8289, 8290, 8292, 8298 and 8302. The invention further provides polypeptides encoded by SEQ ID NO: 32 such as those selected from the group consisting of SEQ ID NOs: 8312, 8318, 8321, 8322, 8323, 8324, 8326, 8329, 8333, 8336, 8340, 8343, 8344, 8370, 8371, 8401, 8402, 8406, 8411, 8417, 8424, 8425, 8429, 8434 and 8435. The invention further provides polypeptides encoded by SEQ ID NO: 33 such as those selected from the group consisting of SEQ ID NOs: 8448, 8460, 8461, 8488, 8507, 8509, 8527, 8541, 8546, 8556, 8567, 8575, 8589, 8605, 8627, 8628, 8647 and 8658. The invention further provides polypeptides encoded by SEQ ID NO: 34 such as those selected from the group consisting of SEQ ID NOs: 8685, 8686, 8705, 8731, 8736, 8745, 8747, 8748, 8749, 8751, 8757, 8764, 8768, 8780, 8782, 8783, 8787, 8793, 8794, 8795, 8796, 8805, 8806, 8813, 8818, 8820, 8828, 8861, 8876, 8877, 8878, 8879, 8880, 8883, 8890, 8908, 8912, 8933, 8938, 8949, 8968, 8969, 8976, 8993, 8994, 8995, 8996 and 9004 The invention further provides polypeptides encoded by SEQ ID NO: 35 such as those selected from the group consisting of SEQ ID NOs: 9017, 9018, 9019, 9020, 9021, 9022, 9023, 9024, 9025, 9026, 9027, 9028, 9029, 9030, 9031, 9032, 9033, 9034, 9035, 9036, 9037, 9038, 9040 and 9041. The invention further provides polypeptides encoded by SEQ ID NO: 36 such as those selected from the group consisting of SEQ ID NOs: 9044, 9048, 9052, 9061, 9065, 9069, 9071, 9076, 9077, 9092, 9095, 9097, 9100, 9101, 9105, 9106, 9113, 9114, 9116, 9121, 9122, 9123, 9124, 9129, 9152, 9155, 9169, 9172, 9173, 9174, 9182, 9186, 9187, 9188, 9189, 9190, 9192, 9193, 9194, 9195, 9196, 9197, 9198, 9200, 9201, 9203, 9205, 9207, 9232, 9246, 9247, 9248, 9251, 9254, 9255, 9267, 9272, 9288, 9296, 9298, 9299, 9301, 9311 and 9312. The invention further provides polypeptides encoded by SEQ ID NO: 37 such as those selected from the group consisting of SEQ ID NOs: 9337, 9338, 9340, 9342, 9353, 9356, 9364, 9365, 9367, 9383, 9385, 9392, 9409, 9411, 9414, 9415, 9420, 9430, 9434, 9438, 9451, 9452, 9464, 9471, 9472, 9476, 9483, 9484, 9485, 9506, 9536, 9537, 9548, 9549, 9556, 9557, 9560, 9587, 9589, 9590, 9611, 9612, 9621, 9639, 9652, 9654, 9657, 9664, 9667, 9674 and 9679. The invention further provides polypeptides encoded by SEQ ID NO: 38 such as those selected from the group consisting of SEQ ID NOs: 9685, 9689, 9691, 9698, 9715, 9716, 9717, 9718, 9722, 9725, 9755, 9770, 9772, 9773, 9776, 9780, 9781, 9782, 9787, 9795, 9798, 9803, 9814, 9824, 9842, 9851, 9855, 9856, 9858, 9861, 9862, 9866, 9867, 9883, 9897, 9902, 9906, 9941, 9949, 9955, 9956, 9957, 9960, 9994, 9997, 9998, 10002, 10003, 10021, 10038, 10105, 10107, 10110, 10123, 10129, 10131, 10141, 10161, 10192, 10197, 10199, 10202, 10218, 10219, 10220, 10221 and 28714. The invention further provides polypeptides encoded by SEQ ID NO: 39 such as those selected from the group consisting ofSEQ ID NOs: 10226, 10229, 10250, 10254, 10258, 10261, 10273, 10306, 10309, 10315, 10336, 10339, 10341, 10350 and 28715. The invention further provides polypeptides encoded by SEQ ID NO: 40 such as those selected from the group consisting ofSEQ ID NOs: 10356, 10358, 10377, 10389, 10396, 10437, 10439, 10447, 10459, 10467, 10473, 10487, 10489, 10534, 10535, 10540, 10541, 10547, 10548, 10552, 10558, 10564, 10581, 10600, 10601, 10616, 10629, 10637, 10645, 10657, 10658, 10674, 10678, 10681, 10683, 10684, 10686, 10687, 10692, 10698, 10700, 10708, 10723, 10741, 10744, 10747, 10785, 10789, 10799, 10802, 10803, 10807, 10808, 10809, 10812, 10825, 10830, 10837, 10845, 10853, 10865, 10870, 10886, 10895, 10910, 10922, 10923, 10924, 10927, 10928, 10929, 10930, 10931, 10933, 10934, 10935, 10945, 10965, 10971, 10988, 10989, 11007, 11010, 11032, 11033, 11048, 11049, 11052, 11053, 11066, 11067, 11071, 11075 and 28717. The invention further provides polypeptides encoded by SEQ ID NO: 41 such as those selected from the group consisting of SEQ ID NOs: 11091, 11092, 11093, 11094, 11098, 11099, 11107, 11108, 11110, 11113, 11122, 11138, 11145, 11146, 11148, 11154, 11168, 11172, 11174, 11195, 11199, 11202, 11212, 11218, 11222, 11223, 11224, 11225, 11236, 11249, 11250, 11258, 11261, 11273, 11275, 11277, 11284, 11285, 11286, 11303, 11314, 11319 and 11342. The invention further provides polypeptides encoded by SEQ ID NO: 42 such as those selected from the group consisting of SEQ ID NOs: 11391 and 28723. The invention further provides polypeptides encoded by SEQ ID NO: 43 such as those selected from the group consisting of SEQ ID NOs: 11399, 11401, 11417, 11427, 11430, 11439, 11441, 11453, 11457, 11460, 11462, 11463, 11464, 11469, 11470, 11475, 11476, 11490, 11491, 11503, 11526, 11530, 11537, 11550, 11560, 11564, 11565, 11571, 11572, 11577, 11580, 11582, 11583, 11585, 11599, 11613, 11624, 11641, 11646, 11648, 11655, 11658, 11661, 11667, 11682 and 28724. The invention further provides polypeptides encoded by SEQ ID NO: 44 such as those selected from the group consisting of SEQ ID NOs: 11707, 11716, 11719, 11724, 11747, 11749, 11756, 11771, 11776, 11782, 11783, 11788, 11796, 11800, 11806, 11809, 11811, 11814, 11816, 11825, 11834, 11838, 11849, 11855, 11856, 11858, 11863, 11864, 11878, 11883, 11890, 11899, 11900, 11907, 11914, 11920, 11930, 11931, 11935, 11937, 11938, 11959, 11960, 11961, 11962, 11973, 11974, 11976, 11979, 11984, 11989, 11991, 11997, 11998, 12002, 12004, 12006, 12013, 12029, 12035, 12036, 12037, 12038, 12039, 12040, 12043, 12047, 12051, 12052, 12057, 12060, 12068, 12072, 12083, 12084, 12093, 12094, 12102, 12103, 12104, 12107, 12110, 12111, 12113, 12123, 12126, 12137, 12149, 12169, 12175, 12192, 12197, 12210, 12217, 12221, 12228, 12233, 12251, 12252, 12261, 12262, 12271, 12294 and 12307. The invention further provides polypeptides encoded by SEQ ID NO: 45 such as those selected from the group consisting of SEQ ID NOs: 12310, 12314, 12316, 12317, 12319, 12320, 12322, 12324, 12330, 12331, 12334, 12341, 12342, 12343, 12346, 12347, 12357, 12374, 12377, 12378, 12379, 12385, 12395, 12405, 12410, 12411, 12413, 12414, 28726 and 28727. The invention further provides polypeptides encoded by SEQ ID NO: 46 such as those selected from the group consisting ofSEQ ID NOs: 12418, 12420, 12429, 12440, 12441, 12442, 12447, 12448, 12453, 12456, 12460, 12481, 12487, 12501, 12503, 12524, 12528, 12533, 12534, 12535, 12546, 12558, 12563, 12574, 12576, 12586, 12587, 12588, 12589, 12590, 12600, 12609, 12610, 12611, 12626, 12645, 12647, 12649, 12650, 12654, 12659, 12667, 12668, 12669, 12670, 12674, 12675, 12686, 12718, 12739, 12740, 12741, 12749, 12750, 12751, 12752, 12755, 12756, 12766, 12773, 12785, 12809, 12816, 12819, 12820, 12827, 12828, 12830, 12831, 12833 and 12850. The invention further provides polypeptides encoded by SEQ ID NO: 47 such as those selected from the group consisting ofSEQ ID NOs: 12861, 12862, 12866, 12868, 12871, 12875, 12879, 12887, 12890, 12897, 12902, 12904, 12907, 12913, 12914, 12916, 12917, 12920, 12921, 12926, 12941, 12945, 12948, 12962, 12976, 12978, 12979, 12981, 12983, 12992, 13002, 13006, 13011, 13016, 13023, 13026, 13029, 13031, 13032, 13034, 13036, 13038, 13039, 13040, 13054, 13056, 13062, 13063, 13066, 13069, 13085, 13086 and 13088. The invention further provides polypeptides encoded by SEQ ID NO: 48 such as those selected from the group consisting of SEQ ID NOs: 13093, 13097, 13115, 13119, 13122, 13124, 13130, 13131, 13134, 13139, 13152, 13156, 13161, 13165, 13171, 13173, 13184, 13185, 13187, 13200, 13201, 13206, 13214, 13232, 13243, 13248, 13273, 13277, 13284, 13297, 13301, 13312, 13318, 13321, 13324, 13326, 13328, 13332, 13340, 13342, 13348, 13349, 13352, 13356, 13358, 13383, 13385, 13386, 13394, 13396, 13402, 13413, 13417, 13424, 13428, 13430, 13437, 13438, 13440, 13451, 13455, 13475, 13476, 13489 and 28732. The invention further provides polypeptides encoded by SEQ ID NO: 49 such as those selected from the group consisting ofSEQ ID NOs: 13494, 13496, 13500, 13502, 13505, 13506, 13507, 13512, 13517, 13524, 13526, 13527, 13528, 13529, 13538, 13547, 13550, 13552, 13557, 13580, 13593, 13594, 13609, 13617, 13618, 13641, 13646 and 13647. The mvention further provides polypeptides encoded by SEQ ID NO: 50 such as those selected from the group consisting ofSEQ ID NOs: 13661, 13667, 13673, 13684, 13690, 13691, 13700, 13718, 13732 and 13797. The invention further provides polypeptides encoded by SEQ ID NO: 51 such as those selected from the group consisting of SEQ ID NOs: 13830, 13841, 13861, 13863, 13865, 13866, 13877, 13878, 13879, 13880 and 13893. The invention further provides polypeptides encoded by SEQ ID NO: 52 such as those selected from the group consisting of SEQ ID NOs: 13897, 13905, 13915, 13952, 13961, 13967, 14001, 14031, 14041, 14042, 14062, 14064, 14068, 14094, 14101 and 14103. The invention further provides polypeptides encoded by SEQ ID NO: 53 such as those selected from the group consisting of SEQ ID NOs: 14120, 14124, 14126, 14143, 14151, 14152, 14168, 14169, 14173, 14181, 14188, 14189, 14195, 14209, 14214, 14215, 14216, 14222, 14229, 14233, 14234, 14236, 14242, 14247, 14249, 14261, 14268, 14277, 14279, 14287, 14301, 14306, 14307, 14308, 14312, 14313, 14321, 14322, 14323, 14324, 14331, 14336, 14338, 14339, 14346, 14349, 14351, 14353, 14365, 14368, 14369, 14370, 14374, 14376, 14378, 14379 and 14380. The invention further provides polypeptides encoded by SEQ ID NO: 54 such as those selected from the group consisting of SEQ ID NOs: 14398, 14408, 14411, 14429, 14456, 14458, 14464, 14471, 14480, 14482, 14484, 14485, 14503, 14509, 14514, 14518, 14520, 14521, 14545 and 28741. The invention further provides polypeptides encoded by SEQ ID NO: 55 such as those selected from the group consisting of SEQ ID NOs: 14552, 14557, 14558, 14575, 14577, 14579, 14580, 14589, 14592, 14593, 14595, 14602, 14603, 14606, 14608, 14618, 14625, 14637, 14638, 14641, 14644, 14647, 14652, 14653, 14656, 14659, 14661, 14671, 14672, 14675, 14676, 14699, 14702, 14707, 14708, 14709, 14712, 14720, 14721 and 28744. The invention further provides polypeptides encoded by SEQ ID NO: 56 such as those selected from the group consisting of SEQ ID NOs: 14742, 14745, 14751, 14752, 14764, 14769, 14789, 14796 and 14798. The invention further provides polypeptides encoded by SEQ ID NO: 57 such as those selected from the group consisting of SEQ ID NOs: 14819, 14820, 14833, 14834, 14836, 14837, 14838, 14849, 14870, 14872, 14876, 14877, 14885, 14898, 14912, 14913, 14923, 14924, 14933, 14935, 14972, 14973, 14991, 14992, 14993, 14994, 14998, 15002, 15036, 15043, 15047, 15049, 15050, 15065, 15080, 15085, 15090, 15094, 15095, 15096, 15101, 15106, 15113, 15127, 15138, 15147, 15149, 15170, 15172, 15192, 15193, 15197, 15198, 15215, 15217, 15218 and 28748. The invention further provides polypeptides encoded by SEQ ID NO: 58 such as those selected from the group consisting of SEQ ID NOs: 15237, 15250, 15255, 15259, 15265, 15272, 15278, 15286, 15288, 15298, 15302, 15303, 15305, 15311, 15312, 15318, 15319, 15322, 15323, 15324, 15325, 15335, 15336, 15338, 15339, 15350 and 15371. The invention further provides polypeptides encoded by SEQ ID NO: 59 such as those selected from the group consisting of SEQ ID NOs: 15385, 15386, 15410, 15411, 15413, 15421, 15422, 15423, 15424, 15425, 15437, 15441, 15455, 15458, 15470, 15472, 15476, 15479, 15486, 15487, 15488, 15490, 15496, 15497, 15500, 15502, 15507, 15508, 15518, 15519, 15525, 15531, 15541, 15544, 15549, 15560, 15561, 15563, 15567, 15570, 15573, 15598, 15614, 15620, 15622, 15624, 15627, 15629, 15633, 15635, 15643, 15646, 15647, 15652, 15653, 15657, 15670, 15685, 15687, 15689 and 15693. The invention further provides polypeptides encoded by SEQ ID NO: 60 such as those selected from the group consisting ofSEQ ID NOs: 15695, 15697, 15706, 15724, 15728 and 15742 The invention further provides polypeptides encoded by SEQ ID NO: 61 such as those selected from the group consisting ofSEQ ID NOs: 15757, 15769, 15795, 15796, 15808, 15816, 15819, 15821, 15837, 15844, 15845, 15849, 15851, 15853, 15875, 15876, 15884, 15888, 15890, 15896, 15915, 15916, 15917, 15918, 15931, 15935, 15938, 15948, 15949, 15960, 15964, 15965, 15966, 15970, 15982, 15987, 15989, 15990, 15991, 15992, 15993, 15994, 15997, 16001, 16002, 16003, 16015, 16018, 16026, 16029, 16045, 16050, 16052, 16053, 16068, 16069, 16073, 16078, 16079, 16080, 16088, 16109, 16111 and 16119. The invention further provides polypeptides encoded by SEQ ID NO: 62 such as those selected from the group consisting ofSEQ ID NOs: 16131, 16134, 16138, 16141, 16142, 16145, 16146, 16155, 16168, 16176, 16187, 16189, 16190, 16192, 16195, 16210, 16219, 16225, 16232, 16234, 16238, 16241, 16242, 16248, 16256 and 16258. The invention further provides polypeptides encoded by SEQ ID NO: 63 such as those selected from the group consisting of SEQ ID NOs: 16265, 16272, 16274, 16279, 16285, 16297, 16299, 16312, 16315, 16316, 16327, 16328, 16337, 16352, 16353, 16354, 16355, 16356, 16357, 16371, 16372, 16378, 16379, 16380, 16392, 16399, 16400, 16403, 16424, 16426, 16439, 16442, 16447, 16448, 16453, 16471, 16483, 16492 and 16498. The invention further provides polypeptides encoded by SEQ ID NO: 64 such as those selected from the group consisting ofSEQ ID NOs: 16501, 16502, 16504, 16536, 16537, 16546, 16547, 16555, 16566, 16573, 16590, 16592, 16593, 16594, 16595, 16601, 16602, 16608, 16616, 16619, 16629, 16649, 16659, 16688, 16691, 16693, 16694, 16695, 16712, 16713, 16736, 16744, 16745, 16749, 16787 and 16788. The invention further provides polypeptides encoded by SEQ ID NO: 65 such as those selected from the group consisting ofSEQ ID NOs: 16805, 16808, 16811, 16812, 16816, 16817, 16842, 16843, 16845, 16850 and 16865. The invention further provides polypeptides encoded by SEQ ID NO: 66 such as those selected from the group consisting ofSEQ ID NOs: 16881, 16888, 16891, 16901, 16902, 16910, 16920, 16924, 16932, 16935, 16962, 16967, 16971, 16982, 16989, 16990, 16992, 16993 and 28767. The invention further provides polypeptides encoded by SEQ ID NO: 67 such as those selected from the group consisting of SEQ ID NOs: 17001, 17006, 17011, 17020, 17022, 17029, 17037, 17039, 17044, 17049, 17050, 17055, 17057, 17058, 17064, 17073, 17080, 17093, 17097, 17098, 17099, 17102, 17113 and 17116. The invention further provides polypeptides encoded by SEQ ID NO: 68 such as those selected from the group consisting of SEQ ID NOs: 17120, 17121, 17134, 17135, 17145, 17148, 17163, 17169, 17170, 17171, 17189, 17190, 17191, 17192, 17193, 17194, 17200, 17210, 17212, 17226, 17229, 17237, 17257, 17259, 17284, 17287, 17294, 17295, 17298, 17306, 17307, 17311, 17317, 17319, 17328, 17329, 17330, 17331, 17332, 17348, 17351, 17372, 17377, 17380, 17388, 17395, 17396, 17403, 17407, 17430, 17436, 17440, 17454, 17455, 17463, 17469, 17480, 17482, 17497, 17514 and 17521. The invention further provides polypeptides encoded by SEQ ID NO: 69 such as those selected from the group consisting of SEQ ID NOs: 17526, 17527, 17537, 17560, 17561 and 28771. The invention further provides polypeptides encoded by SEQ ID NO: 70 such as those selected from the group consisting of SEQ ID NOs: 17584, 17597, 17613, 17629 and 17631. The invention further provides polypeptides encoded by SEQ ID NO: 71 such as those selected from the group consisting of SEQ ID NOs: 17665, 17681, 17685, 17691, 17703 and 17706. The invention further provides polypeptides encoded by SEQ ID NO: 72 such as those selected from the group consisting of SEQ ID NOs: 17711, 17713, 17734, 17738, 17739, 17744, 17745, 17748, 17749, 17754, 17757, 17759, 17776, 17778, 17782, 17798, 17806, 17814, 17815, 17819, 17820, 17821, 17822, 17823, 17841, 17850, 17858, 28773 and 28774. The invention further provides polypeptides encoded by SEQ ID NO: 73 such as those selected from the group consisting of SEQ ID NOs: 17860, 17869, 17870, 17874, 17883, 17884, 17887, 17888, 17919, 17931, 17935, 17940, 17946, 17959, 17960, 17962, 17970, 17975, 17987, 17993, 18009, 18024, 18033, 18036, 18053, 18055, 18068 and 28775. The invention further provides polypeptides encoded by SEQ ID NO: 74 such as those selected from the group consisting of SEQ ID NOs: 18080, 18083, 18086, 18089, 18123, 18124, 18134, 18142, 18149, 18160, 18161, 18164, 18166, 18177, 18189, 18199, 18200, 18202, 18220, 18221, 18222, 18235, 18245, 18248 and 18249. The invention further provides polypeptides encoded by SEQ ID NO: 75 such as those selected from the group consisting of SEQ ID NOs: 18270, 18276, 18284, 18287, 18296, 18297, 18298, 18299, 18300, 18307, 18311, 18312, 18314, 18319, 18320, 18322, 18323, 18324, 18326, 18328, 18329, 18330, 18331, 18337, 18359, 18360, 18367, 18380, 18388, 18397, 18412, 18413, 18416, 18420, 18421 and 28781. The invention further provides polypeptides encoded by SEQ ID NO: 76 such as those selected from the group consisting of SEQ ID NOs: 18422, 18423, 18430, 18432, 18433, 18434, 18436, 18437, 18438, 18439, 18440, 18446, 18454, 18460, 18471, 18472, 18473, 18474, 18480, 18483 and 18484. The invention further provides polypeptides encoded by SEQ ID NO: 77 such as those selected from the group consisting of SEQ ID NOs: 18491, 18492, 18493, 18495, 18497, 18500, 18513, 18514, 18517, 18521, 18525, 18526 and 18532. The invention further provides polypeptides encoded by SEQ ID NO: 78 such as those selected from the group consisting of SEQ ID NOs: 18544, 18553, 18557, 18560, 18562, 18563, 18578, 18582, 18587, 18591, 18594, 18595, 18599, 18610, 18616, 18624, 18637, 18646, 18649, 18654, 18656, 18663, 18671, 18672, 18680, 18681, 18688, 18689, 18690, 18692, 18695, 18698, 18699, 28785 and 28786. The invention further provides polypeptides encoded by SEQ ID NO: 79 such as those selected from the group consisting of SEQ ID NOs: 18716, 18735, 18737, 18749 and 18757. The invention further provides polypeptides encoded by SEQ ID NO: 80 such as those selected from the group consisting of SEQ ID NOs: 18778, 18790, 18799, 18803, 18816, 18829, 18833, 18834, 18837, 18847, 18868, 18871, 18879, 18888, 18893, 18895, 18897, 18909, 18921, 18927, 18928, 18931 and 18938. The invention further provides polypeptides encoded by SEQ ID NO: 81 such as those selected from the group consisting of SEQ ID NOs: 18979, 18986, 19021, 19023, 19026, 19028, 19030, 19034 and 19036. The invention further provides polypeptides encoded by SEQ ID NO: 82 such as those selected from the group consisting of SEQ ID NOs: 19053, 19060, 19063, 19067, 19072, 19080, 19085, 19090, 19091, 19105 and 19108. The invention further provides polypeptides encoded by SEQ ID NO: 83 such as those selected from the group consisting of SEQ ID NOs: 19119, 19133, 19134, 19135, 19136, 19137, 19138, 19139, 19141, 19142, 19143, 19144, 19149, 19154, 19157, 19158, 19159, 19177, 19178, 19179, 19180, 19183, 19184, 19191, 19199, 19200, 19204, 19205, 19208, 19212, 19213, 19218, 19244, 19245, 19246, 19248, 19249, 19258, 19261, 19273, 19277, 19287, 19288, 19298 and 19299. The invention further provides polypeptides encoded by SEQ ID NO: 84 such as those selected from the group consisting of SEQ ID NOs: 19300, 19330, 19331, 19344, 19345, 19350, 19353, 19359, 19367, 19368, 19370, 19391, 19399, 19400, 19401, 19407, 19422, 19424, 19427, 19447, 19448, 19449 and 28794. The invention further provides polypeptides encoded by SEQ ID NO: 85 such as those selected from the group consisting of SEQ ID NOs: 19456, 19460, 19487, 19499, 19500, 19501, 19519, 19521, 19526, 19533, 19535, 19542, 19553, 19566, 19567, 19573, 19577, 19581, 19586, 19589, 19595 and 28796. The invention further provides polypeptides encoded by SEQ ID NO: 86 such as those selected from the group consisting of SEQ ID NOs: 19600, 19605, 19607, 19608, 19609, 19610, 19611, 19612, 19631, 19634, 19641, 19642, 19644, 19646, 19648, 19649, 19651, 19660, 19663, 19668, 19670, 19676, 19682, 19683, 19684, 19687 and 19705. The mvention further provides polypeptides encoded by SEQ ID NO: 87 such as those selected from the group consisting of SEQ ID NOs: 19734, 19743 and 19757. The invention further provides polypeptides encoded by SEQ ID NO: 88 such as those selected from the group consisting of SEQ ID NOs: 19771, 19772, 19773, 19775, 19780, 19782, 19788, 19805, 19809, 19810, 19813, 19820, 19843, 19844, 19854, 19855, 19856, 19863, 19864, 19865, 19872, 19883, 28800 and 28801. The invention further provides polypeptides encoded by SEQ ID NO: 89 such as those selected from the group consisting of SEQ ID NOs: 19886, 19891, 19896, 19898, 19903, 19926, 19930, 19933, 19940, 19941, 19945, 19961, 19965, 19967, 19968, 19970, 19972, 19977, 19979 and 19981. The invention further provides polypeptides encoded by SEQ ID NO: 90 such as those selected from the group consisting of SEQ ID NOs: 20005, 20013 and 28806. The invention further provides polypeptides encoded by SEQ ID NO: 91 such as those selected from the group consisting of SEQ ID NOs: 20029, 20036, 20041, 20046, 20048, 20052, 20057, 20068, 20069, 20070, 20092, 20100, 20106, 20108, 20113, 20116, 20119, 20129, 20132, 20133, 20147, 20163, 20164, 20165, 20166, 20174, 20177, 20186, 20193, 20194, 20197, 20198, 20199, 20201, 20202, 20204, 20207, 20208, 20213, 20214, 20221, 20229, 28807 and 28809. The invention further provides polypeptides encoded by SEQ ID NO: 92 such as those selected from the group consisting of SEQ ID NOs: 20262. The invention further provides polypeptides encoded by SEQ ID NO: 93 such as those selected from the group consisting of SEQ ID NOs: 28812. The invention further provides polypeptides encoded by SEQ ID NO: 94 such as those selected from the group consisting of SEQ ID NOs: 20284, 20286, 20287, 20288, 20289, 20290, 20292, 20293, 20294, 20296, 20297, 20298, 20299, 20300 and 28814. The invention further provides polypeptides encoded by SEQ ID NO: 95 such as those selected from the group consisting of SEQ ID NOs: 20311. The invention further provides polypeptides encoded by SEQ ID NO: 96 such as those selected from the group consisting of SEQ ID NOs: 20329, 20332, 20333, 20334, 20357, 20360, 20369, 20370, 20372, 20382, 20385, 20386, 20391, 20392, 20393, 20395, 20399, 20400, 20401, 20411, 20412, 20414, 20415, 20422, 20425, 20442, 20458, 20463, 20474, 20475, 20476, 20479, 20480, 20485, 20494, 20510, 20512, 20517, 20525, 20528, 20530 and 20542. The invention further provides polypeptides encoded by SEQ ID NO: 97 such as those selected from the group consisting of SEQ ID NOs: 20562, 20564, 20565, 20573, 20577, 20585, 20590, 20608, 20609, 20611, 20616, 20617, 20618, 20620, 20630, 20635, 20638, 20658, 20669, 20671, 20683, 20684, 28820 and 28822. The invention further provides polypeptides encoded by SEQ ID NO: 98 such as those selected from the group consisting of SEQ ID NOs: 20703, 20704, 20705, 20714, 20715, 20733 and 20734. The invention further provides polypeptides encoded by SEQ ID NO: 99 such as those selected from the group consisting of SEQ ID NOs: 20742, 20756, 20759, 20764, 20766, 20774, 20776, 20783, 20799, 20800, 28826 and 28827. The invention further provides polypeptides encoded by SEQ ID NO: 100 such as those selected from the group consisting of SEQ ID NOs: 20806, 20832, 20836, 20854, 20855, 20856, 20877, 20882, 20897, 20913, 20923, 20925, 20926, 20935, 20943, 20949 and 20951. The invention further provides polypeptides encoded by SEQ ID NO: 101 such as those selected from the group consisting of SEQ ID NOs: 20952, 20955, 20963, 20966, 20973, 20975, 20984, 20987, 21002, 21018, 21049 and 21054. The invention further provides polypeptides encoded by SEQ ID NO: 102 such as those selected from the group consisting of SEQ ID NOs: 21065, 21070, 21074, 21079, 21085, 21089, 21092, 21093, 21112, 21126, 21129, 21132, 21135, 21137, 21146, 21153, 21154, 21155, 21172, 21180, 21185, 21190, 21198, 21202, 21217, 21221, 21222, 21229 and 28830. The invention further provides polypeptides encoded by SEQ ID NO: 103 such as those selected from the group consisting of SEQ ID NOs: 21241, 21250, 21256, 21258, 21259, 21264, 21265, 21266, 21267, 21271, 21287, 21300, 21315, 21333, 21348, 21349, 21350, 21355, 21359, 21363, 21368, 21372, 21387, 21399, 21402, 21405, 21428, 21435, 21446, 21447, 21449, 21453, 21466, 21477, 21483, 21485, 21486, 21489, 21490, 21493 and 21495. The invention further provides polypeptides encoded by SEQ ID NO: 104 such as those selected from the group consisting of SEQ ID NOs: 21504, 21511, 21519, 21522, 21526, 21528, 21529, 21531, 21532, 21533, 21539, 21543, 21544, 21567, 21568, 21570, 21573, 21574, 21575, 21579, 21584, 21587, 21597, 21598, 21608, 21615, 21619, 21620, 21634, 21641, 21643, 21649, 21650, 21655, 21658, 21659, 21663, 21670, 21671, 21674, 21675, 21680, 21691, 21693, 21695, 21703, 21705, 21707, 21708, 21710, 21711, 21740, 21743, 21749, 21762, 21765, 21774, 21778, 21780, 21788, 28834 and 28835. The invention further provides polypeptides encoded by SEQ ID NO: 105 such as those selected from the group consisting of SEQ ID NOs: 21789, 21791, 21803, 21806, 21808, 21827 and 21831. The invention further provides polypeptides encoded by SEQ ID NO: 106 such as those selected from the group consisting of SEQ ID NOs: 21845, 21850 and 21856. The invention further provides polypeptides encoded by SEQ ID NO 107 such as those selected from the group consisting of SEQ ID NOs: 21861, 21872 21875, 21894, 21897, 21908, 21910, 21913, 21923, 21926, 21978, 21979, 21983 21997, 22003, 22014, 22019, 22020, 22027, 22042, 22054, 22062, 22063, 22064 22065, 22071, 22072, 28844 and 28845. The invention further provides polypeptides encoded by SEQ ID NO 108 such as those selected from the group consisting of SEQ ID NOs: 22084, 22085 22086, 22090, 22093, 22098, 22107, 22108, 22119, 22124, 22125, 22127, 22139 ; 22146, 22148, 22152, 22153, 22157, 22163, 22164, 22165, 22167, 22168, 22177 22185, 22188, 22189, 22196, 22211, 22218, 22219, 22227, 22233, 22239, 22247 22256, 22265, 22269, 22270, 22289, 22290, 22292, 22298, 22300, 22309, 22311 22312, 22318, 22323, 22324 and 22328. The invention further provides polypeptides encoded by SEQ ID NO: 109 such as those selected from the group consisting of SEQ ID NOs: 22329, 22337, 22342, 22343, 22347, 22350, 22355, 22363 and 28852. The invention further provides polypeptides encoded by SEQ ID NO: 110 such as those selected from the group consisting of SEQ ID NOs: 22369, 22379, 22381, 22393, 22394, 22395, 22396, 22406, 22427, 22444, 22454, 22456 and 22462. The invention further provides polypeptides encoded by SEQ ID NO: 111 such as those selected from the group consisting of SEQ ID NOs: 22481, 22515, 22519, 22523, 22534, 22543, 22547, 22551, 22563, 22581, 22586, 22590, 22595, 22596, 22597, 22615, 22616, 22619, 22622, 22629, 22630 and 28857. The invention further provides polypeptides encoded by SEQ ID NO: 112 such as those selected from the group consisting of SEQ ID NOs: 22659, 22660, 22669, 22670, 22675, 22676, 22677, 22678 and 22684. The invention further provides polypeptides encoded by SEQ ID NO: 113 such as those selected from the group consisting of SEQ ID NOs: 22693, 22706, 22712, 22719, 22726, 22738, 22747, 22748, 22752, 22771, 22775, 22784, 22790, 22804 and 28861. The invention further provides polypeptides encoded by SEQ ID NO: 114 such as those selected from the group consisting of SEQ ID NOs: 22809, 22819, 22821, 22837, 22838, 22842, 22846 and 22872. The invention further provides polypeptides encoded by SEQ ID NO: 115 such as those selected from the group consisting of SEQ ID NOs: 22879, 22882, 22886, 22906, 22907, 22910, 22920, 22922, 22937, 22938, 22939, 22948, 22958, 22976, 22977, 22984, 22987, 22988, 22989, 22990, 22991, 22996, 23001, 23013, 23017, 23021, 23034, 23038, 23039, 23044, 23046, 23063, 23065, 23074, 23075, 23076, 23079, 23082, 23084, 23090, 23091, 23092 and 23093. The invention further provides polypeptides encoded by SEQ ID NO: 116 such as those selected from the group consisting of SEQ ID NOs: 23096, 23098, 23101, 23106, 23112, 23114, 23115, 23116, 23118, 23125, 23127, 23130, 23136, 23138, 23140, 23144, 23151, 23164, 23168, 23170 and 28871. The invention further provides polypeptides encoded by SEQ ID NO: 117 such as those selected from the group consisting of SEQ ID NOs: 23186, 23187, 23189, 23190, 23194, 23195, 23202, 23203, 23209, 23213 and 28873. The invention further provides polypeptides encoded by SEQ ID NO 118 such as those selected from the group consisting of SEQ ID NOs: 23215, 23219. 23222, 23225, 23233, 23238, 23246, 23253, 23256, 23260, 23264, 23269, 23275 23279, 23291, 23304, 23322, 23326, 23328, 23335, 23336, 23344, 23367, 23368 23369, 23370, 23379, 23382, 23383, 23384, 23388 and 28874. The invention further provides polypeptides encoded by SEQ ID NO 119 such as those selected from the group consisting of SEQ ID NOs: 23418, 23419 23420, 23437, 23441, 23442, 23443, 23444, 23448, 23449 and 23452. The invention further provides polypeptides encoded by SEQ ID NO 120 such as those selected from the group consisting of SEQ ID NOs: 23481, 23484 23485, 23489, 23513, 23518, 23532, 23533, 23535, 23538, 23543, 23549, 23558 23561, 23567, 23571, 23577, 23582, 23586, 23587 and 23591. The invention further provides polypeptides encoded by SEQ ID NO 121 such as those selected from the group consisting of SEQ ID NOs: 23610, 23613 23614, 23616, 23618, 23624, 23635, 23647, 23651, 23657, 23658, 23664, 23682 : 23683, 23685, 23687, 23706, 23707, 23708, 23709, 23711, 23719, 23722 and 28882. The invention further provides polypeptides encoded by SEQ ID NO 122 such as those selected from the group consisting of SEQ ID NOs: 23729, 23741 23745, 23750, 23763, 23768, 23770, 23790, 23791, 23792, 23796, 23799, 23805 23806, 23809 and 23817. The invention further provides polypeptides encoded by SEQ ID NO 123 such as those selected from the group consisting of SEQ ID NOs: 23847, 23857 23864, 23871, 23880, 23886, 23891 and 23907. The invention further provides polypeptides encoded by SEQ ID NO 124 such as those selected from the group consisting of SEQ ID NOs: 23911, 23913 23925, 23926, 23927, 23928, 23931, 23932, 23934, 23937, 23938, 23941, 23943 23944, 23945, 23950, 23951, 23954, 23956, 23957, 23959, 23972, 23999, 24011 24018, 24022, 24024, 24027, 24032, 24034 and 28887. The invention further provides polypeptides encoded by SEQ ID NO 125 such as those selected from the group consisting of SEQ ID NOs: 24047, 24051, 24055, 24097, 24099, 24107, 24113, 24114, 24118, 24128, 24146, 24154, 24180, 24181, 24185 and 24211. The invention further provides polypeptides encoded by SEQ ID NO: 126 such as those selected from the group consisting of SEQ ID NOs: 24227, 24231, 24244, 24246, 24248, 24262, 24271, 24273, 24275, 24279, 24284 and 28892. The mvention further provides polypeptides encoded by SEQ ID NO: 127 such as those selected from the group consisting of SEQ ID NOs: 24293, 24294, 24300, 24303, 24317, 24319, 24326, 24327, 24331, 24341, 24342, 24351, 24352, 24355, 24361, 24398, 24399, 24406, 24420, 24431, 24433, 24434, 24435, 24442, 24450, 24456, 24459, 24463, 24465, 24473, 24474, 24482, 24487, 24499, 24514 and 24515. The invention further provides polypeptides encoded by SEQ ID NO: 128 such as those selected from the group consisting of SEQ ID NOs: 24528, 24534, 24543, 24545, 24566, 24587, 24588, 24589, 24590, 24597, 24602, 24605, 24606, 24609, 24612, 24619, 24620, 24621, 24622, 24623, 24626, 24629, 24630, 24639, 24640, 24641, 24652, 24663, 24665, 24667, 24673, 24676, 24679, 24684, 24685, 24687, 24696, 24698, 24704, 24705, 24709, 24715, 24716, 24721, 24722, 24728, 24730, 24739, 24742, 24743, 24745, 24749, 28897 and 28900. The invention further provides polypeptides encoded by SEQ ID NO: 129 such as those selected from the group consisting of SEQ ID NOs: 24755, 24758, 24761, 24770, 24778, 24779, 24780, 24787, 24788, 24791, 24800, 24801, 24821, 24824, 24825, 24826, 24829, 24840, 24850, 24851, 24861, 24879, 24895, 24903, 24907, 24913, 24936, 24937, 24950, 24952, 24955 and 24957. The invention further provides polypeptides encoded by SEQ ID NO: 130 such as those selected from the group consisting of SEQ ID NOs: 24961, 24967, 24968, 24969, 24973, 24981, 24984, 24986, 24987, 24992, 24993, 24995, 25004, 28903 and 28904. The mvention further provides polypeptides encoded by SEQ ID NO: 131 such as those selected from the group consisting of SEQ ID NOs: 25024, 25029, 25038, 25045, 25067 and 25076. The invention further provides polypeptides encoded by SEQ ID NO: 132 such as those selected from the group consisting of SEQ ID NOs: 25082, 25085, 25086, 25088, 25089, 25090, 25094, 25096, 25102, 25103, 25112, 25129, 25130, 25131, 25133, 25135, 25139, 25150, 25160, 25163, 25164, 25165, 25166, 25167, 25168, 25169, 25174, 25178, 25187, 25192, 25193, 25194, 25195, 25197, 25208, 25215, 25216, 25217 and 25218. The invention further provides polypeptides encoded by SEQ ID NO: 133 such as those selected from the group consisting of SEQ ID NOs: 25229, 25237, 25239, 25246, 25267, 25271, 25274, 25275, 25283 and 28908. The invention further provides polypeptides encoded by SEQ ID NO: 134 such as those selected from the group consisting of SEQ ID NOs: 25288, 25304, 25309, 25313, 25315, 25320, 25339, 25340, 25346, 25354, 25355, 25356, 28911 and 28912. The invention further provides polypeptides encoded by SEQ ID NO: 135 such as those selected from the group consisting of SEQ ID NOs: 25365, 25367, 25378, 25379, 25380, 25385, 25387, 25404, 25410 and 25417. The invention further provides polypeptides encoded by SEQ ID NO: 136 such as those selected from the group consisting of SEQ ID NOs: 25442, 25445, 25456, 25458, 25474, 25475, 25479, 25480, 25490 and 25516. The invention further provides polypeptides encoded by SEQ ID NO: 137 such as those selected from the group consisting of SEQ ID NOs: 25535, 25539, 25540, 25546, 25550, 25553, 25562, 25578, 25584 and 25590. The invention further provides polypeptides encoded by SEQ ID NO: 138 such as those selected from the group consisting of SEQ ID NOs: 25602, 25603, 25611, 25613, 25620, 25621, 25622, 25629 and 28920. The invention further provides polypeptides encoded by SEQ ID NO: 139 such as those selected from the group consisting of SEQ ID NOs: 25644 and 25671. The invention further provides polypeptides encoded by SEQ ID NO: 140 such as those selected from the group consisting of SEQ ID NOs: 25684, 25685, 25687, 25692, 25700, 25706, 25715, 25720, 25737, 25738, 25742, 25745, 25746, 25760, 25764, 25766, 25777 and 25780. The invention further provides polypeptides encoded by SEQ ID NO: 141 such as those selected from the group consisting of SEQ ID NOs: 25784, 25788, 25791, 25803, 25804, 25807, 25812, 25815, 25828, 25830 and 25832. The invention further provides polypeptides encoded by SEQ ID NO: 142 such as those selected from the group consisting of SEQ ID NOs: 25853. The mvention further provides polypeptides encoded by SEQ ID NO: 143 such as those selected from the group consisting of SEQ ID NOs: 25862, 25873, 25874, 25877, 25884, 25896 and 28925. The invention further provides polypeptides encoded by SEQ ID NO: 144 such as those selected from the group consisting of SEQ ID NOs: 25906, 25911, 25913 and 28927. The invention further provides polypeptides encoded by SEQ ID NO: 145 such as those selected from the group consisting of SEQ ID NOs: 25916, 25917, 25918, 25922, 25929, 25938, 25952, 25957, 25960 and 25963. The mvention further provides polypeptides encoded by SEQ ID NO: 147 such as those selected from the group consisting of SEQ ID NOs: 25987, 25990, 25994, 25997, 25998, 26005, 26006, 26011, 26012, 26016, 28932 and 28933. The invention further provides polypeptides encoded by SEQ ID NO: 148 such as those selected from the group consisting of SEQ ID NOs: 26021, 26025, 26036 and 26037. The invention further provides polypeptides encoded by SEQ ID NO: 149 such as those selected from the group consisting of SEQ ID NOs: 26044, 26061, 26067, 26071, 26090, 26099 and 28940. The invention further provides polypeptides encoded by SEQ ID NO: 150 such as those selected from the group consisting of SEQ ID NOs: 26122, 26140, 26141, 26143, 26149, 26156, 26157, 26161, 26163, 26171, 26175 and 28941. The invention further provides polypeptides encoded by SEQ ID NO: 151 such as those selected from the group consisting of SEQ ID NOs: 26181, 26195, 26196, 26200, 26207, 26214, 26216, 26221, 26232, 28943 and 28945. The invention further provides polypeptides encoded by SEQ ID NO: 152 such as those selected from the group consisting of SEQ ID NOs: 26247. The invention further provides polypeptides encoded by SEQ ID NO: 153 such as those selected from the group consisting of SEQ ID NOs: 26281, 26284 and 28950. The invention further provides polypeptides encoded by SEQ ID NO: 154 such as those selected from the group consisting of SEQ ID NOs: 26287 and 28953. The invention further provides polypeptides encoded by SEQ ID NO: 155 such as those selected from the group consisting of SEQ ID NOs: 26321, 26333, 26337 and 28955. The invention further provides polypeptides encoded by SEQ ID NO: 156 such as those selected from the group consisting of SEQ ID NOs: 26370, 26380, 26388, 26390, 26392, 26397 and 28956. The invention further provides polypeptides encoded by SEQ ID NO: 157 such as those selected from the group consisting of SEQ ID NOs: 26436, 26437 and 26442. The invention further provides polypeptides encoded by SEQ ID NO: 158 such as those selected from the group consisting of SEQ ID NOs: 26490, 26503 and 26504. The mvention further provides polypeptides encoded by SEQ ID NO: 159 such as those selected from the group consisting of SEQ ID NOs: 28962. The invention further provides polypeptides encoded by SEQ ID NO: 160 such as those selected from the group consisting of SEQ ID NOs: 26532. The invention further provides polypeptides encoded by SEQ ID NO: 161 such as those selected from the group consisting of SEQ ID NOs: 26549, 26555 and 28965. The invention further provides polypeptides encoded by SEQ ID NO: 162 such as those selected from the group consisting of SEQ ID NOs: 26567 and 26586. The invention further provides polypeptides encoded by SEQ ID NO: 163 such as those selected from the group consisting of SEQ ID NOs: 26598, 26605 and 28969. The invention further provides polypeptides encoded by SEQ ID NO: 164 such as those selected from the group consisting of SEQ ID NOs: 26618, 26619, 26621, 26625, 26629 and 28970. The invention further provides polypeptides encoded by SEQ ID NO: 165 such as those selected from the group consisting of SEQ ID NOs: 26658 and 26659. The invention further provides polypeptides encoded by SEQ ID NO: 166 such as those selected from the group consisting of SEQ ID NOs: 26691, 26692 and 28976. The invention further provides polypeptides encoded by SEQ ID NO: 167 such as those selected from the group consisting of SEQ ID NOs: 26693, 26700 and 26703. The invention further provides polypeptides encoded by SEQ ID NO: 168 such as those selected from the group consisting of SEQ ID NOs: 26726. The invention further provides polypeptides encoded by SEQ ID NO: 169 such as those selected from the group consisting of SEQ ID NOs: 26738. The invention further provides polypeptides encoded by SEQ ID NO: 171 such as those selected from the group consisting of SEQ ID NOs: 28986. The invention further provides polypeptides encoded by SEQ ID NO: 172 such as those selected from the group consisting of SEQ ID NOs: 26770 and 26773. The invention further provides polypeptides encoded by SEQ ID NO: 173 such as those selected from the group consisting of SEQ ID NOs: 26776 and 26784. The invention further provides polypeptides encoded by SEQ ID NO: 174 such as those selected from the group consisting of SEQ ID NOs: 26793. The' invention further provides polypeptides encoded by SEQ ID NO: 175 such as those selected from the group consisting of SEQ ID NOs: 26798 and 28991. The invention further provides polypeptides encoded by SEQ ID NO: 176 such as those selected from the group consisting of SEQ ID NOs: 26816, 26817, 26819 and 28992. The invention further provides polypeptides encoded by SEQ ID NO: 178 such as those selected from the group consisting of SEQ ID NOs: 26852. The invention further provides polypeptides encoded by SEQ ID NO: 179 such as those selected from the group consisting of SEQ ID NOs: 26880, 28997 and 28998. The invention further provides polypeptides encoded by SEQ ID NO: 180 such as those selected from the group consisting of SEQ ID NOs: 26894. The invention further provides polypeptides encoded by SEQ ID NO: 181 such as those selected from the group consisting of SEQ ID NOs: 26900 and. 26909. The invention further provides polypeptides encoded by SEQ ID NO: 182 such as those selected from the group consisting of SEQ ID NOs: 26915. The invention further provides polypeptides encoded by SEQ ID NO: 183 such as those selected from the group consisting of SEQ ID NOs: 26937 and 29004. The invention further provides polypeptides encoded by SEQ ID NO: 184 such as those selected from the group consisting of SEQ ID NOs: 26945. The invention further provides polypeptides encoded by SEQ ID NO: 185 such as those selected from the group consisting of SEQ ID NOs: 26949 and 26962. The invention further provides polypeptides encoded by SEQ ID NO: 186 such as those selected from the group consisting of SEQ ID NOs: 26966, 26971 and 26975. The invention further provides polypeptides encoded by SEQ ID NO: 187 such as those selected from the group consisting of SEQ ID NOs: 26977, 26980, 26984, 26985 and 26986. The invention further provides polypeptides encoded by SEQ ID NO: 188 such as those selected from the group consisting of SEQ ID NOs: 26995, 26996, 26998 and 29012. The invention further provides polypeptides encoded by SEQ ID NO: 189 such as those selected from the group consisting of SEQ ID NOs: 27001, 27005, 27009, 27012 and 27019. The invention further provides polypeptides encoded by SEQ ID NO: 190 such as those selected from the group consisting of SEQ ID NOs: 27023, 27029, 27030, 27031, 27036, 27037, 27050, 27051 and 29014. The invention further provides polypeptides encoded by SEQ ID NO: 192 such as those selected from the group consisting of SEQ ID NOs: 27070 and 27072. The invention further provides polypeptides encoded by SEQ ID NO: 193 such as those selected from the group consisting of SEQ ID NOs: 27079 and 27084. The invention further provides polypeptides encoded by SEQ ID NO: 194 such as those selected from the group consisting of SEQ ID NOs: 27090 and 29024. The invention further provides polypeptides encoded by SEQ ID NO: 196 such as those selected from the group consisting of SEQ ID NOs: 27116, 27118, 27122, 27124, 27126, 27127, 27131, 27134, 27135, 27137, 27138, 27141 and 29027. The invention further provides polypeptides encoded by SEQ ID NO: 197 such as those selected from the group consisting of SEQ ID NOs: 27152, 27153, 27154 and 29030. The invention further provides polypeptides encoded by SEQ ID NO: 198 such as those selected from the group consisting of SEQ ID NOs: 27155, 27163 and 27165. The invention further provides polypeptides encoded by SEQ ID NO: 199 such as those selected from the group consisting of SEQ ID NOs: 27167, 27168, 27171, 27172, 27175 and 29035. The invention further provides polypeptides encoded by SEQ ID NO: 200 such as those selected from the group consisting of SEQ ID NOs: 27190. The invention further provides polypeptides encoded by SEQ ID NO: 201 such as those selected from the group consisting of SEQ ID NOs: 27199, 27205 and 29040. The invention further provides polypeptides encoded by SEQ ID NO: 202 such as those selected from the group consisting of SEQ ID NOs: 27212 and 27218. The invention further provides polypeptides encoded by SEQ ID NO: 204 such as those selected from the group consisting of SEQ ID NOs: 29041. The invention further provides polypeptides encoded by SEQ ID NO: 205 such as those selected from the group consisting of SEQ ID NOs: 27270 and 27271. The invention further provides polypeptides encoded by SEQ ID NO: 206 such as those selected from the group consisting of SEQ ID NOs: 27283 and 29043. The invention further provides polypeptides encoded by SEQ ID NO: 207 such as those selected from the group consisting of SEQ ID NOs: 27307 and 29044. The invention further provides polypeptides encoded by SEQ ID NO: 208 such as those selected from the group consisting of SEQ ID NOs: 27315 and 27319. The invention further provides polypeptides encoded by SEQ ID NO: 209 such as those selected from the group consisting of SEQ ID NOs: 27328 and 29047. The invention further provides polypeptides encoded by SEQ ID NO: 210 such as those selected from the group consisting of SEQ ID NOs: 29048 and 29049. The invention further provides polypeptides encoded by SEQ ID NO: 212 such as those selected from the group consisting of SEQ ID NOs: 27366. The invention further provides polypeptides encoded by SEQ ID NO: 213 such as those selected from the group consisting of SEQ ID NOs: 27375 and 29053. The invention further provides polypeptides encoded by SEQ ID NO: 214 such as those selected from the group consisting of SEQ ID NOs: 27398 and 29056. The invention further provides polypeptides encoded by SEQ ID NO: 215 such as those selected from the group consisting of SEQ ID NOs: 27399. The invention further provides polypeptides encoded by SEQ ID NO: 217 such as those selected from the group consisting of SEQ ID NOs: 27419, 27431, 27434, 27438, 29060 and 29062. The invention further provides polypeptides encoded by SEQ ID NO: 218 such as those selected from the group consisting of SEQ ID NOs: 27446. The invention further provides polypeptides encoded by SEQ ID NO: 219 such as those selected from the group consisting of SEQ ID NOs: 27449 and 27461. The invention further provides polypeptides encoded by SEQ ID NO: 220 such as those selected from the group consisting of SEQ ID NOs: 27470, 27475 and 29069. The invention further provides polypeptides encoded by SEQ ID NO: 221 such as those selected from the group consisting of SEQ ID NOs: 27485, 27486 and 29071. The invention further provides polypeptides encoded by SEQ ID NO: 222 such as those selected from the group consisting of SEQ ID NOs: 27497 and 29076. The invention further provides polypeptides encoded by SEQ ID NO: 223 such as those selected from the group consisting of SEQ ID NOs: 27503, 27508, 27523 and 27525. The invention further provides polypeptides encoded by SEQ ID NO: 224 such as those selected from the group consisting of SEQ ID NOs: 27527, 27533 and 27541. The invention further provides polypeptides encoded by SEQ ID NO: 225 such as those selected from the group consisting of SEQ ID NOs: 27550, 27558, 27561, 29082 and 29083. The invention further provides polypeptides encoded by SEQ ID NO: 226 such as those selected from the group consisting of SEQ ID NOs: 27578, 27580, 27582, 27584, 27585, 27586 and 27590. The invention further provides polypeptides encoded by SEQ ID NO: 227 such as those selected from the group consisting of SEQ ID NOs: 27598, 27601, 27602, 27605 and 29085. The invention further provides polypeptides encoded by SEQ ID NO: 228 such as those selected from the group consisting of SEQ ID NOs: 27607, 27610 and 29087. The invention further provides polypeptides encoded by SEQ ID NO: 229 such as those selected from the group consisting of SEQ ID NOs: 27640 and 29089. The invention further provides polypeptides encoded by SEQ ID NO: 230 such as those selected from the group consisting of SEQ ID NOs: 27656 and 27657. The invention further provides polypeptides encoded by SEQ ID NO: 231 such as those selected from the group consisting of SEQ ID NOs: 27665 and 29092. The invention further provides polypeptides encoded by SEQ ID NO: 232 such as those selected from the group consisting of SEQ ID NOs: 27687. The invention further provides polypeptides encoded by SEQ ID NO: 233 such as those selected from the group consisting of SEQ ID NOs: 27692, 27698, 27701, 27704 and 27709. The invention further provides polypeptides encoded by SEQ ID NO: 234 such as those selected from the group consisting of SEQ ID NOs: 27712 and 27720. The invention further provides polypeptides encoded by SEQ ID NO: 235 such as those selected from the group consisting of SEQ ID NOs: 27738, 27746 and 29098. The invention further provides polypeptides encoded by SEQ ID NO: 236 such as those selected from the group consisting of SEQ ID NOs: 27759 and 29099. The invention further provides polypeptides encoded by SEQ ID NO: 237 such as those selected from the group consisting of SEQ ID NOs: 27767, 27769, 27770 and 29101. The invention further provides polypeptides encoded by SEQ ID NO: 238 such as those selected from the group consisting of SEQ ID NOs: 29102. The invention further provides polypeptides encoded by SEQ ID NO: 239 such as those selected from the group consisting of SEQ ID NOs: 27800, 27807 and 29105. The invention further provides polypeptides encoded by SEQ ID NO: 240 such as those selected from the group consisting of SEQ ID NOs: 27819. The invention further provides polypeptides encoded by SEQ ID NO: 241 such as those selected from the group consisting of SEQ ID NOs: 27836. The invention further provides polypeptides encoded by SEQ ID NO: 242 such as those selected from the group consisting of SEQ ID NOs: 27848. The invention further provides polypeptides encoded by SEQ ID NO: 243 such as those selected from the group consisting of SEQ ID NOs: 27857, 27870, 27879, 29112, 29114 and 29115. The invention further provides polypeptides encoded by SEQ ID NO: 244 such as those selected from the group consisting of SEQ ID NOs: 27885 and 27887. The invention further provides polypeptides encoded by SEQ ID NO: 245 such as those selected from the group consisting of SEQ ID NOs: 27906, 27908 and 29118. The invention further provides polypeptides encoded by SEQ ID NO: 246 such as those selected from the group consisting of SEQ ID NOs: 27911, 27921 and 27926. The invention further provides polypeptides encoded by SEQ ID NO: 247 such as those selected from the group consisting of SEQ ID NOs: 27927, 27928 and 27935. The invention further provides polypeptides encoded by SEQ ID NO: 248 such as those selected from the group consisting of SEQ ID NOs: 27938 and 27940. The invention further provides polypeptides encoded by SEQ ID NO: 249 such as those selected from the group consisting of SEQ ID NOs: 27943, 27944, 27952, 27953 and 29124. The invention further provides polypeptides encoded by SEQ ID NO: 250 such as those selected from the group consisting of SEQ ID NOs: 27957, 27958, 27964 and 27966. The invention further provides polypeptides encoded by SEQ ID NO: 251 such as those selected from the group consisting of SEQ ID NOs: 27980. The invention further provides polypeptides encoded by SEQ ID NO: 252 such as those selected from the group consisting of SEQ ID NOs: 27986 and 27991. The invention further provides polypeptides encoded by SEQ ID NO: 253 such as those selected from the group consisting of SEQ ID NOs: 29129. The invention further provides polypeptides encoded by SEQ ID NO: 254 such as those selected from the group consisting of SEQ ID NOs: 28021 and 29132. The invention further provides polypeptides encoded by SEQ ID NO: 255 such as those selected from the group consisting of SEQ ID NOs: 28032, 28033 and 28042. The invention further provides polypeptides encoded by SEQ ID NO: 256 such as those selected from the group consisting of SEQ ID NOs: 28051. The invention further provides polypeptides encoded by SEQ ID NO: 257 such as those selected from the group consisting of SEQ ID NOs: 28067 and 28079. The invention further provides polypeptides encoded by SEQ ID NO: 258 such as those selected from the group consisting of SEQ ID NOs: 28087. The invention further provides polypeptides encoded by SEQ ID NO: 259 such as those selected from the group consisting of SEQ ID NOs: 28100 and 29139. The invention further provides polypeptides encoded by SEQ ID NO: 260 such as those selected from the group consisting of SEQ ID NOs: 28116, 28119 and 28121. The invention further provides polypeptides encoded by SEQ ID NO: 261 such as those selected from the group consisting of SEQ ID NOs: 28123 and 29144. The invention further provides polypeptides encoded by SEQ ID NO: 262 such as those selected from the group consisting of SEQ ID NOs: 28132. The invention further provides polypeptides encoded by SEQ ID NO: 263 such as those selected from the group consisting of SEQ ID NOs: 28143, 28146 and 29149. The invention further provides polypeptides encoded by SEQ ID NO: 264 such as those selected from the group consisting of SEQ ID NOs: 28161 and 29150. The invention further provides polypeptides encoded by SEQ ID NO: 265 such as those selected from the group consisting of SEQ ID NOs: 28166, 28169 and 28175. The invention further provides polypeptides encoded by SEQ ID NO: 266 such as those selected from the group consisting of SEQ ID NOs: 28177 and 28179. The invention further provides polypeptides encoded by SEQ ID NO: 267 such as those selected from the group consisting of SEQ ID NOs: 28187, 28199 and 28203. The invention further provides polypeptides encoded by SEQ ID NO: 268 such as those selected from the group consisting of SEQ ID NOs: 28207 and 28221. The invention further provides polypeptides encoded by SEQ ID NO: 269 such as those selected from the group consisting of SEQ ID NOs: 28230. The invention further provides polypeptides encoded by SEQ ID NO: 270 such as those selected from the group consisting of SEQ ID NOs: 28248, 28250 and 29166. The invention further provides polypeptides encoded by SEQ ID NO: 271 such as those selected from the group consisting of SEQ ID NOs: 28253, 28263 and 28265. The invention further provides polypeptides encoded by SEQ ID NO: 272 such as those selected from the group consisting of SEQ ID NOs: 28269 and 28274. The invention further provides polypeptides encoded by SEQ ID NO: 273 such as those selected from the group consisting of SEQ ID NOs: 28282, 28290 and 28291. The invention further provides polypeptides encoded by SEQ ID NO: 274 such as those selected from the group consisting of SEQ ID NOs: 28295, 28300, 28302, 28305, 28312 and 28316. The invention further provides polypeptides encoded by SEQ ID NO: 275 such as those selected from the group consisting of SEQ ID NOs: 28328. The invention further provides polypeptides encoded by SEQ ID NO: 276 such as those selected from the group consisting of SEQ ID NOs: 28334, 28339, 28342, 28346, 29174 and 29175. The invention further provides polypeptides encoded by SEQ ID NO: 277 such as those selected from the group consisting of SEQ ID NOs: 28357, 28358 and 28361. The invention further provides polypeptides encoded by SEQ ID NO: 279 such as those selected from the group consisting of SEQ ID NOs: 28385 and 28387. The invention further provides polypeptides encoded by SEQ ID NO: 280 such as those selected from the group consisting of SEQ ID NOs: 28394, 28396, 29182 and 29184. The invention further provides polypeptides encoded by SEQ ID NO:- 281 such as those selected from the group consisting of SEQ ID NOs: 28410. The invention further provides polypeptides encoded by SEQ ID NO: 282 such as those selected from the group consisting of SEQ ID NOs: 28424, 28432 and 28434. The invention further provides polypeptides encoded by SEQ ID NO: 283 such as those selected from the group consisting of SEQ ID NOs: 28439, 28440 and 28446. The invention further provides polypeptides encoded by SEQ ID NO: 284 such as those selected from the group consisting of SEQ ID NOs: 28452, 28454 and 28461. The invention further provides polypeptides encoded by SEQ ID NO: 285 such as those selected from the group consisting of SEQ ID NOs: 28474, 28476, 28477 and 29191. The invention further provides polypeptides encoded by SEQ ID NO: 286 such as those selected from the group consisting of SEQ ID NOs: 28490, 29192 and 29193. The invention further provides polypeptides encoded by SEQ ID NO: 287 such as those selected from the group consisting of SEQ ID NOs: 28497. The invention further provides polypeptides encoded by SEQ ID NO: 288 such as those selected from the group consisting of SEQ ID NOs: 28503, 28509, 28512 and 28513. The invention further provides polypeptides encoded by SEQ ID NO: 289 such as those selected from the group consisting of SEQ ID NOs: 28523 and 28526. The invention further provides polypeptides encoded by SEQ ID NO: 290 such as those selected from the group consisting of SEQ ID NOs: 29198. The invention further provides polypeptides encoded by SEQ ID NO: 291 such as those selected from the group consisting of SEQ ID NOs: 28544, 28547 and 28558. The invention further provides polypeptides encoded by SEQ ID NO: 292 such as those selected from the group consisting of SEQ ID NOs: 28560, 28564 and 29201. The invention further provides polypeptides encoded by SEQ ID NO: 294 such as those selected from the group consisting of SEQ ID NOs: 28584 and 28586. The invention further provides polypeptides encoded by SEQ ID NO: 295 such as those selected from the group consisting of SEQ ID NOs: 28588, 28589, 28593, 28594, 28597 and 28598. The invention further provides polypeptides encoded by SEQ ID NO: 296 such as those selected from the group consisting of SEQ ID NOs: 28604. The invention further provides polypeptides encoded by SEQ ID NO: 297 such as those selected from the group consisting of SEQ ID NOs: 28612 and 29204. The invention further provides polypeptides encoded by SEQ ID NO: 298 such as those selected from the group consisting of SEQ ID NOs: 29207. The invention further provides polypeptides encoded by SEQ ID NO: 299 such as those selected from the group consisting of SEQ ID NOs: 28644. Within other aspects, the present invention provides pharmaceutical compositions comprising a polypeptide or polynucleotide as described above and a physiologically acceptable carrier. Within a related aspect of the present invention, vaccines for prophylactic or therapeutic use are provided. Such vaccines comprise a polypeptide or polynucleotide as described above and an immunostimulant. The present invention further provides pharmaceutical compositions that comprise: (a) an antibody or antigen-binding fragment thereof that specifically binds to a Propiombacterium acnes protein; and (b) a physiologically acceptable carrier. Within further aspects, the present invention provides pharmaceutical compositions comprising: (a) an antigen presenting cell that expresses a polypeptide as described above and (b) a pharmaceutically acceptable carrier or excipient. Antigen presenting cells include dendritic cells, macrophages, monocytes, fibroblasts and B cells. Within related aspects, vaccines are provided that comprise: (a) an antigen presenting cell that expresses a polypeptide as described above and (b) an immunostimulant. The present invention further provides, in other aspects, fusion proteins that comprise at least one polypeptide as described above, as well as polynucleotides encoding such fusion proteins. Within related aspects, pharmaceutical compositions comprising a fusion protein, or a polynucleotide encoding a fusion protein, in combination with a physiologically acceptable carrier are provided. Vaccines are further provided, within other aspects, that comprise a fusion protein, or a polynucleotide encoding a fusion protein, in combination with an immunostimulant. Within further aspects, the present invention provides methods for the treatment of acne in a patient, comprising administering to a patient a pharmaceutical composition or vaccine as recited above. The patient may be afflicted with acne, in which case the methods provide treatment for the disease, or patient considered at risk for acne may be treated prophylactically. Methods are further provided, within other aspects, for stimulating and/or expanding T cells specific for a Propiombacterium acnes protein, comprising contacting T cells with one or more of: (i) a polypeptide as described above; (ii) a polynucleotide encoding such a polypeptide; and/or (iii) an antigen presenting cell that expresses such a polypeptide; under conditions and for a time sufficient to permit the stimulation and/or expansion of T cells. Isolated T cell populations comprising T cells prepared as described above are also provided. Within further aspects, the present invention provides methods for inhibiting the development or progression of acne in a patient, comprising administering to a patient an effective amount of a T cell population as described above. The present invention further provides methods for the treatment of acne in a patient, comprising the steps of: (a) incubating CD4 + and/or CD8 + T cells isolated from a patient with one or more of: (i) a polypeptide comprising at least an immunogenic portion of a Propiombacterium acnes protein; (ii) a polynucleotide encoding such a polypeptide; and (iii) an antigen-presenting cell that expresses such a polypeptide; and (b) administering to the patient an effective amount ofthe proliferated T cells, and thereby inhibiting the development or progression of acne in the patient. Proliferated cells may, but need not, be cloned prior to administration to the patient. Within further aspects, the present invention provides methods for determining the presence or absence of Propiombacterium acnes in a patient, comprising: (a) contacting a biological sample obtained from a patient with a binding agent that binds to a polypeptide as recited above; (b) detecting in the sample an amount of polypeptide that binds to the binding agent; and (c) comparing the amount of polypeptide with a predetermined cut-off value, and therefrom determining the presence or absence of the organism in the patient. Within preferred embodiments, the binding agent is an antibody, more preferably a monoclonal antibody. The present invention also provides, within other aspects, methods for monitoring the progression of acne in a patient. Such methods comprise the steps of: (a) contacting a biological sample obtained from a patient at a first point in time with a binding agent that binds to a polypeptide as recited above; (b) detecting in the sample an amount of polypeptide that binds to the binding agent; (c) repeating steps (a) and (b) using a biological sample obtained from the patient at a subsequent point in time; and (d) comparing the amount of polypeptide detected in step (c) with the amount detected in step (b). The present invention further provides, within other aspects, methods for determining the presence or absence of a Propiombacterium acnes in a patient, comprising the steps of: (a) contacting a biological sample obtained from a patient with an oligonucleotide that hybridizes to a polynucleotide that encodes a Propiombacterium acnes protein; (b) detecting in the sample a level of a polynucleotide, preferably mRNA, that hybridizes to the oligonucleotide; and (c) comparing the level of polynucleotide that hybridizes to the oligonucleotide with a predetermined cut-off value, and therefrom determining the presence or absence ofthe organism in the patient. Within certain embodiments, the amount of mRNA is detected via polymerase chain reaction using, for example, at least one oligonucleotide primer that hybridizes to a polynucleotide encoding a polypeptide as recited above, or a complement of such a polynucleotide. Within other embodiments, the amount of mRNA is detected using a hybridization technique, employing an oligonucleotide probe that hybridizes to a polynucleotide that encodes a polypeptide as recited above, or a complement of such a polynucleotide. In related aspects, methods are provided for monitoring the progression of acne in a patient, comprising the steps of: (a) contacting a biological sample obtained from a patient with an oligonucleotide that hybridizes to a polynucleotide that encodes a Propiombacterium acnes protein; (b) detecting in the sample an amount of a polynucleotide that hybridizes to the oligonucleotide; (c) repeating steps (a) and (b) using a biological sample obtained from the patient at a subsequent point in time; and (d) comparing the amount of polynucleotide detected in step (c) with the amount detected in step (b). Within further aspects, the present invention provides antibodies, such as monoclonal antibodies, that bind to a polypeptide as described above, as well as diagnostic kits comprising such antibodies. Diagnostic kits comprising one or more oligonucleotide probes or primers as described above are also provided. These and other aspects of the present invention will become apparent upon reference to the following detailed description and attached drawings. All references disclosed herein are hereby incorporated by reference in their entirety as if each was incorporated individually. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 is an immunoblot demonstrating that sera from individuals with severe cases of facial acnes react with several dominant species having sizes about 18 — 28 kDa; 35-40 kDa; -50 kDa; -70 kDa; -lOOkDa, as well as several low molecular weight species below 18kDa. Figure 2 is a gel showing the molecular weights of two proteins found in clinical isolates, referred to as ZI and ZII. Figure 3 shows the amino sequences of the predicted ORF of P. acnes sequence ID#15127. The underlined residue (M) at position +29 (start), indicate the probable initiator methionine of the full length protein. The remaining underlined sequences indicate residues identified by N-terminal (non-italicized) and mass spec (MS) (italicized) sequencing of ZI & II. The predicted full length protein is 30.4 kDa (313 amino acid residues) while those of ZI & II are -27.7- (257 amino acid residues) and 24-kDa (222 amino acid residues) respectively in agreememt with their observed mobilities. DETAILED DESCRIPTION OF THE INVENTION As noted above, the present invention is generally directed to compositions and methods for using the compositions, for example in the therapy and diagnosis of acne, particularly those forms of acne in whole or in part caused by the organism Propiombacterium acnes. Certain illustrative compositions described herein include Propiombacterium acnes polypeptides, polynucleotides encoding such polypeptides, binding agents such as antibodies, antigen presenting cells (APCs) and/or immune system cells (e.g., T cells). Certain preferred Propiombacterium acnes polypeptides include those that react detectably (within an immunoassay, such as an ELISA or Western blot) with antisera of a patient afflicted with acne. The practice of the present invention will employ, unless indicated specifically to the contrary, conventional methods of virology, immunology, microbiology, molecular biology and recombinant DNA techniques within the skill of the art, many of which are described below for the purpose of illustration. Such techniques are explained fully in the literature. See, e.g., Sambrook, et al. Molecular Cloning: A Laboratory Manual (2nd Edition, 1989); Maniatis et al. Molecular Cloning: A Laboratory Manual (1982); DNA Cloning: A Practical Approach, vol. I & II (D. Glover, ed.); Oligonucleotide Synthesis (N. Gait, ed., 1984); Nucleic Acid Hybridization (B. Hames & S. Higgins, eds., 1985); Transcription and Translation (B. Hames & S. Higgins, eds., 1984); Animal Cell Culture (R. Freshney, ed., 1986); Perbal, A Practical Guide to Molecular Cloning (1984). All publications, patents and patent applications cited herein, whether supra or infra, are hereby incorporated by reference in their entirety. As used in this specification and the appended claims, the singular forms "a," "an" and "the" include plural references unless the content clearly dictates otherwise. Therefore, in accordance with the above, and as described further herein, the present invention provides illustrative polynucleotide compositions having sequences set forth in SEQ ID NOs: 1-299, illustrative polypeptide compositions having amino acid sequences set forth in SEQ ID NOs: 300-29,212, antibody compositions capable of binding such polypeptides, and numerous additional embodiments employing these and other compositions, for example in the detection, diagnosis and/or therapy of acne in humans. POLYNUCLEOTIDE COMPOSITIONS As used herein, the terms "DNA segment" and "polynucleotide" refer to a DNA molecule that has been isolated free of total genomic DNA of a particular species. Therefore, a DNA segment encoding a polypeptide refers to a DNA segment that contains one or more coding sequences yet is substantially isolated away from, or purified free from, total genomic DNA of the species from which the DNA segment is obtained. Included within the terms "DNA segment" and "polynucleotide" are DNA segments and smaller fragments of such segments, and also recombinant vectors, including, for example, plasmids, cosmids, phagemids, phage, viruses, and the like. As will be understood by those skilled in the art, the DNA segments of this invention can include genomic sequences, extra-genomic and plasmid-encoded sequences and smaller engineered gene segments that express, or may be adapted to express, proteins, polypeptides, peptides and the like. Such segments may be naturally isolated, or modified synthetically by the hand of man. "Isolated," as used herein, means that a polynucleotide is substantially away from other coding sequences, and that the DNA segment does not contain large portions of unrelated coding DNA, such as large chromosomal fragments or other functional genes or polypeptide coding regions. Of course, this refers to the DNA segment as originally isolated, and does not exclude genes or coding regions later added to the segment by the hand of man. As will be recognized by the skilled artisan, polynucleotides may be single-stranded (coding or antisense) or double-stranded, and may be DNA (genomic, cDNA or synthetic) or RNA molecules. RNA molecules include HnRNA molecules, which contain introns and correspond to a DNA molecule in a one-to-one manner, and mRNA molecules, which do not contain introns. Additional coding or non-coding sequences may, but need not, be present within a polynucleotide of the present invention, and a polynucleotide may, but need not, be linked to other molecules and/or support materials. Polynucleotides may comprise a native sequence (i.e., an endogenous sequence that encodes a Propiombacterium acnes protein or a portion thereof) or may comprise a variant or a biological or antigenic functional equivalent of such a sequence. Polynucleotide variants may contain one or more substitutions, additions, deletions and/or insertions, as further described below, preferably such that the immunogenicity of the encoded polypeptide is not diminished, relative to a native Propiombacterium acnes protein. The effect on the immunogenicity of the encoded polypeptide may generally be assessed as described herein. The term "variants" also encompasses homologous genes of xenogenic origin. When comparing polynucleotide or polypeptide sequences, two sequences are said to be "identical" if the sequence of nucleotides or amino acids in the two sequences is the same when aligned for maximum correspondence, as described below. Comparisons between two sequences are typically performed by comparing the sequences over a comparison window to identify and compare local regions of sequence similarity.* A "comparison window" as used herein, refers to a segment of at least about 20 contiguous positions, usually 30 to about 75, 40 to about 50, in which a sequence may be compared to a reference sequence of the same number of contiguous positions after the two sequences, are optimally aligned. Optimal alignment of sequences for comparison may be conducted using the Megalign program in the Lasergene suite of bioinfbrmatics software (DNASTAR, Inc., Madison, WI), using default parameters. This program embodies several alignment schemes described in the following references: Dayhoff, M.O. (1978) A model of evolutionary change in proteins - Matrices for detecting distant relationships. In Dayhoff, M.O. (ed.) Atlas of Protein Sequence and Structure, National Biomedical Research Foundation, Washington DC Vol. 5, Suppl. 3, pp. 345-358; Hein J. (1990) Unified Approach to Alignment and Phylogenes pp. 626-645 Methods in Enzymology vol. 183, Academic Press, Inc., San Diego, CA; Higgins, D.G. and Sharp, P.M. (1989) CABIOS 5:151-153; Myers, E.W. and Muller W (1988) CABIOS 4:11-11; Robinson, E.D. (1971) Comb. Theor 11:105; Santou, N. Nes, M. (1987) Mol. Biol. Evol. 4:406-425; Sneath, P.H.A. and Sokal, R.R. (1973) Numerical Taxonomy — the Principles and Practice of Numerical Taxonomy, Freeman Press, San Francisco, CA; Wilbur, W.J. and Lipman, D.J. (1983) Proc. Natl. Acad, Sci. USA 80:126-130. Alternatively, optimal alignment of sequences for comparison may be conducted by the local identity algorithm of Smith and Waterman (1981) Add. APL. Math 2:482, by the identity alignment algorithm of Needleman and Wunsch (1970) J. Mol. Biol. 48:443, by the search for similarity methods of Pearson and Lipman (1988) Proc. Natl. Acad. Sci. (U.S.A.) 85: 2444, by computerized implementations of these algorithms (GAP, BESTFIT, BLAST, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group (GCG), 575 Science Dr., Madison, WI), or by inspection. One preferred example of algorithms that are suitable for determining percent sequence identity and sequence similarity are the BLAST and BLAST 2.0 algorithms, which are described in Altschul et al. (1977) Nuc. Acids Res. 25:3389-3402 and Altschul et al. (1990) J. Mol. Biol. 215:403-410, respectively. BLAST and BLAST 2.0 can be used, for example with the parameters described herein, to determine percent sequence identity for the polynucleotides and polypeptides of the invention. Software for performing BLAST analyses is publicly available through the National Center for Biotechnology Information (http ://www.ncbi .nlm.nih. gov - In one illustrative example, cumulative scores can be calculated using, for nucleotide sequences, the parameters M (reward score for a pair of matching residues; always >0) and N (penalty score for mismatching residues; always <0). For amino acid sequences, a scoring matrix can be used to calculate the cumulative score. Extension ofthe word hits in each direction are halted when: the cumulative alignment score falls off by the quantity X from its maximum achieved value; the cumulative score goes to zero or below, due to the accumulation of one or more negative-scoring residue alignments; or the end of either sequence is reached. The BLAST algorithm parameters W, T and X determine the sensitivity and speed of the alignment. The BLASTN program (for nucleotide sequences) uses as defaults a word length (W) of 11, and expectation (E) of 10, and the BLOSUM62 scoring matrix (see Henikoff and Henikoff (1989) Proc. Natl. Acad. Sci. USA 89:10915) alignments, (B) of 50, expectation (E) of 10, M=5, N=-4 and a comparison of both strands. Preferably, the "percentage of sequence identity" is determined by comparing two optimally aligned sequences over a window of comparison of at least 20 positions, wherein the portion of the polynucleotide or polypeptide sequence in the comparison window may comprise additions or deletions (i.e., gaps) of 20 percent or less, usually 5 to 15 percent, or 10 to 12 percent, as compared to the reference sequences (which does not comprise additions or deletions) for optimal alignment ofthe two sequences. The percentage is calculated by determining the number of positions at which the identical nucleic acid bases or amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the reference sequence (i.e., the window size) and multiplying the results by 100 to yield the percentage of sequence identity. Therefore, the present invention encompasses polynucleotide and polypeptide sequences having substantial identity to the sequences disclosed herein, for example those comprising at least 50% or more sequence identity, preferably at least 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% or higher, sequence identity compared to a polynucleotide or polypeptide sequence of this invention using the methods described herein, (e.g., BLAST analysis using standard parameters, as described below). One skilled in this art will recognize that these values can be appropriately adjusted to determine corresponding identity of proteins encoded by two nucleotide sequences by taking into account codon degeneracy, amino acid similarity, reading frame positioning and the like. In additional embodiments, the present invention provides isolated polynucleotides and polypeptides comprising various lengths of contiguous stretches of sequence identical to or complementary to one or more of the sequences disclosed herein. For example, polynucleotides are provided by this invention, preferably polynucleotides encoding R acnes polypeptides, that comprise at least about 15, 20, 30, 40, 50, 75, 100, 150, 200, 300, 400, 500 or 1000 or more contiguous nucleotides of one or more of the sequences disclosed herein as well as all intermediate lengths therebetween. It will be readily understood that "intermediate lengths", in this context, means any length between the quoted values, such as 16, 17, 18, 19, etc.; 21, 22, 23, etc.; 30, 31, 32, etc.; 50, 51, 52, 53, etc.; 100, 101, 102, 103, etc.; 150, 151, 152, 153, etc.; including all integers through the 200-500; 500-1,000, and the like. The polynucleotides of the present invention, or fragments thereof, regardless of the length of the coding sequence itself, may be combined with other DNA sequences, such as promoters, polyadenylation signals, additional restriction enzyme sites, multiple cloning sites, other coding segments, and the like, such that their overall length may vary considerably. It is therefore contemplated that a nucleic acid fragment of almost any length may be employed, with the total length preferably being limited by the ease of preparation and use in the intended recombinant DNA protocol. For example, illustrative DNA segments with total lengths of about 10,000, about 5000, about 3000, about 2,000, about 1,000, about 500, about 200, about 100, about 50 base pairs in length, and the like, (including all intermediate lengths) are contemplated to be useful in many implementations of this invention. In another embodiment of the invention, polynucleotide compositions are provided that are capable of hybridizing under moderate to high stringency conditions to a polynucleotide sequence provided herein, or a fragment thereof, or a complementary sequence thereof. Hybridization techniques are well known in the art of molecular biology. For purposes of illustration, suitable moderately stringent conditions for testing the hybridization of a polynucleotide of this invention with other polynucleotides include prewashing in a solution of 5 X SSC, 0.5% SDS, 1.0 mM EDTA (pH 8.0); hybridizing at 50°C-60°C, 5 X SSC, overnight; followed by washing twice at 65°C for 20 minutes with each of 2X, 0.5X and 0.2X SSC containing 0.1% SDS. One skilled in the art will understand that the stringency of hybridization can be readily manipulated, such as by altering the salt content of the hybridization solution and/or the temperature at which the hybridization is performed. For example, in another embodiment, suitable highly stringent hybridization conditions include those described above, with the exception that the temperature of hybridization is increased, e.g. , to 60-65°C or 65-70°C. In certain preferred embodiments, the polynucleotides described above, e.g., polynucleotide variants, fragments and hybridizing sequences, encode polypeptides that are immunologically cross-reactive with a polypeptide sequence specifically set forth herein. In other preferred embodiments, such polynucleotides encode polypeptides that have a level of immunogenic activity of at least about 50%, preferably at least about 70%, and more preferably at least about 90% of that for a polypeptide sequence specifically set forth herein. Moreover, it will be appreciated by those of ordinary skill in the art that, as a result of the degeneracy of the genetic code, there are many nucleotide sequences that encode a polypeptide as described herein. Some of these polynucleotides bear minimal homology to the nucleotide sequence of any native gene. Nonetheless, polynucleotides that vary due to differences in codon usage are specifically contemplated by the present invention. Further, alleles of the genes comprising the polynucleotide sequences provided herein are within the scope ofthe present invention. Alleles are endogenous genes that are altered as a result of one or more mutations, such as deletions, additions and/or substitutions of nucleotides. The resulting mRNA and protein may, but need not, have an altered structure or function. Alleles may be identified using standard techniques (such as hybridization, amplification and/or database sequence comparison). PROBES AND PRIMERS In other embodiments of the present invention, the polynucleotide sequences provided herein can be advantageously used as probes or primers for nucleic acid hybridization. As such, it is contemplated that nucleic acid segments that comprise a sequence region of at least about a 15 nucleotide long contiguous sequence that has the same sequence as, or is complementary to, a 15 nucleotide long contiguous sequence disclosed herein will find particular utility. Longer contiguous identical or complementary sequences, e.g., those of about 20, 30, 40, 50, 100, 200, 500, 1000 (including all intermediate lengths) and even up to full length sequences will also be of use in certain embodiments. The ability of such nucleic acid probes to specifically hybridize to a sequence of interest will enable them to be of use in detecting the presence of complementary sequences in a given sample. However, other uses are also envisioned, such as the use of the sequence information for the preparation of mutant species primers, or primers for use in preparing other genetic constructions. Polynucleotide molecules having sequence regions consisting of contiguous nucleotide stretches of 10-14, 15-20, 30, 50, or even of 100-200 nucleotides or so (including intermediate lengths as well), identical or complementary to SEQ ID NOs: 1-299, are particularly contemplated as hybridization probes for use in, e.g., Southern and Northern blotting. This would allow a gene product, or fragment thereof, to be analyzed, both in diverse cell types and also in various bacterial cells. The total size of fragment, as well as the size of the complementary stretch(es), will ultimately depend on the intended use or application of the particular nucleic acid segment. Smaller fragments will generally find use in hybridization embodiments, wherein the length of the contiguous complementary region may be varied, such as between about 15 and about 100 nucleotides, but larger contiguous complementarity stretches may be used, according to the length complementary sequences one wishes to detect. The use of a hybridization probe of about 15-25 nucleotides in length allows the formation of a duplex molecule that is both stable and selective. Molecules having contiguous complementary sequences over stretches greater than 15 bases in length are generally preferred, though, in order to increase stability and selectivity of the hybrid, and thereby improve the quality and degree of specific hybrid molecules obtained. One will generally prefer to design nucleic acid molecules having gene- complementary stretches of 15 to 25 contiguous nucleotides, or even longer where desired. Hybridization probes may be selected from any portion of any of the sequences disclosed herein. All that is required is to review the sequence set forth in SEQ ID NOs: 1-299, or to any continuous portion of the sequence, from about 15-25 nucleotides in length up to and including the full length sequence, that one wishes to utilize as a probe or primer. The choice of probe and primer sequences may be governed by various factors, such as, by way of example only, one may wish to employ primers from towards the termini ofthe total sequence. Small polynucleotide segments or fragments may be readily prepared by, for example, directly synthesizing the fragment by chemical means, as is commonly practiced using an automated oligonucleotide synthesizer. Also, fragments may be obtained by application of nucleic acid reproduction technology, such as the PCR™ technology of U. S. Patent 4,683,202 (incorporated herein by reference), by introducing selected sequences into recombinant vectors for recombinant production, and by other recombinant DNA techniques generally known to those of skill in the art of molecular biology. The nucleotide sequences of the invention may be used for their ability to selectively form duplex molecules with complementary stretches ofthe entire gene or gene fragments of interest. Depending on the application envisioned, one will typically desire to employ varying conditions of hybridization to achieve varying degrees of selectivity of probe towards target sequence. For applications requiring high selectivity, one will typically desire to employ relatively stringent conditions to form the hybrids, e.g., one will select relatively low salt and/or high temperature conditions, such as provided by a salt concentration of from about 0.02 M to about 0.15 M salt at temperatures of from about 50°C to about 70°C. Such selective conditions tolerate little, if any, mismatch between the probe and the template or target strand, and would be particularly suitable for isolating related sequences. Of course, for some applications, for example, where one desires to prepare mutants employing a mutant primer strand hybridized to an underlying template, less stringent (reduced stringency) hybridization conditions will typically be needed in order to allow formation ofthe heteroduplex. In these circumstances, one may desire to employ salt conditions such as those of from about 0.15 M to about 0.9 M salt, at temperatures ranging from about 20°C to about 55°C. Cross-hybridizing species can thereby be readily identified as positively hybridizing signals with respect to control hybridizations. In any case, it is generally appreciated that conditions can be rendered more stringent by the addition of increasing amounts of formamide, which serves to destabilize the hybrid duplex in the same manner as increased temperature. Thus, hybridization conditions can be readily manipulated, and thus will generally be a method of choice depending on the desired results. POLYNUCLEOTIDE IDENTIFICATION AND CHARACTERIZATION Polynucleotides may be identified, prepared and/or manipulated using any of a variety of well established techniques. For example, a polynucleotide may be identified, as described in more detail below, by screening a microarray of Propiombacterium acnes cDNAs. Such screens may be performed, for example, using a Synteni microarray (Palo Alto, CA) according to the manufacturer's instructions (and essentially as described by Schena et al., Proc. Natl. Acad. Sci. USA °5:10614-10619, 1996 and Heller et al, Proc. Natl. Acad. Sci. USA *^:2150-2155, 1997). Alternatively, polynucleotides may be amplified from cDNA prepared from cells expressing the proteins described herein, such as cells containing Propiombacterium crozes-derived DNA. Such polynucleotides may be amplified via polymerase chain reaction (PCR). For this approach, sequence-specific primers may be designed based on the sequences provided herein, and may be purchased or synthesized. An amplified portion of a polynucleotide ofthe present invention may be used to isolate a full length gene from a suitable library (e.g., a Propiombacterium acnes cDNA library) using well known techniques. Within such techniques, a library (cDNA or genomic) is screened using one or more polynucleotide probes or primers suitable for amplification. Preferably, a library is size-selected to include larger molecules. Random primed libraries may also be preferred for identifying 5' and upstream regions of genes. Genomic libraries are preferred for obtaining introns and extending 5' sequences. For hybridization techniques, a partial sequence may be labeled (e.g., by nick-translation or end-labeling with 32 P) using well known techniques. A bacterial or bacteriophage library is then generally screened by hybridizing filters containing denatured bacterial colonies (or lawns containing phage plaques) with the labeled probe (see Sambrook et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratories, Cold Spring Harbor, NY, 1989). Hybridizing colonies or plaques are selected and expanded, and the DNA is isolated for further analysis. cDNA clones may be analyzed to determine the amount of additional sequence by, for example, PCR using a primer from the partial sequence and a primer from the vector. Restriction maps and partial sequences may be generated to identify one or more overlapping clones. The complete sequence may then be determined using standard techniques, which may involve generating a series of deletion clones. The resulting overlapping sequences can then assembled into a single contiguous sequence. A full length cDNA molecule can be generated by ligating suitable fragments, using well known techniques. Alternatively, there are numerous amplification techniques for obtaining a full length coding sequence from a partial cDNA sequence. Within such techniques, amplification is generally performed via PCR. Any of a variety of commercially available kits may be used to perform the amplification step. Primers may be designed using, for example, software well known in the art. For many applications, primers are preferably 22-30 nucleotides in length, have a GC content of at least 50% and anneal to the target sequence at temperatures of about 68°C to 72°C. The amplified region may be sequenced as described above, and overlapping sequences assembled into a contiguous sequence. One such amplification technique is inverse PCR (see Triglia et al., Nucl Acids Res. 16:8186, 1988), which uses restriction enzymes to generate a fragment in the known region ofthe gene. The fragment is then circularized by intramolecular ligation and used as a template for PCR with divergent primers derived from the known region. Within an alternative approach, sequences adjacent to a partial sequence may be retrieved by amplification with a primer to a linker sequence and a primer specific to a known region. The amplified sequences are typically subjected to a second round of amplification with the same linker primer and a second primer specific to the known region. A variation on this procedure, which employs two primers that initiate extension in opposite directions from the known sequence, is described in WO 96/38591. Another such technique is known as "rapid amplification of cDNA ends" or RACE. This technique involves the use of an internal primer and an external primer, which hybridizes to a polyA region or vector sequence, to identify sequences that are 5' and 3 ' of a known sequence. Additional techniques include capture PCR (Lagerstrom et al., PCR Methods Applic. 7:111-19, 1991) and walking PCR (Parker et al., Nucl. Acids. Res. 79:3055-60, 1991). Other methods employing amplification may also be employed to obtain a full length cDNA sequence. In certain instances, it is possible to obtain a full length cDNA sequence by analysis of sequences provided in an expressed sequence tag (EST) database, such as that available from GenBank. Searches for overlapping ESTs may generally be performed using well known programs (e.g., NCBI BLAST searches), and such ESTs may be used to generate a contiguous full length sequence. Full length DNA sequences may also be obtained by analysis of genomic fragments. POLYNUCLEOTIDE EXPRESSION IN HOST CELLS In other embodiments of the invention, polynucleotide sequences or fragments thereof which encode polypeptides of the invention, or fusion proteins or functional equivalents thereof, may be used in recombinant DNA molecules to direct expression of a polypeptide in appropriate host cells. Due to the inherent degeneracy of the genetic code, other DNA sequences that encode substantially the same or a functionally equivalent amino acid sequence may be produced and these sequences may be used to clone and express a given polypeptide. As will be understood by those of skill in the art, it may be advantageous in some instances to produce polypeptide-encoding nucleotide sequences possessing non-naturally occurring codons. For example, codons preferred by a particular prokaryotic or eukaryotic host can be selected to increase the rate of protein expression or to produce a recombinant RNA transcript having desirable properties, such as a half- life which is longer than that of a transcript generated from the naturally occurring sequence. Moreover, the polynucleotide sequences of the present invention can be engineered using methods generally known in the art in order to alter polypeptide encoding sequences for a variety of reasons, including but not limited to, alterations which modify the cloning, processing, and/or expression of the gene product. For example, DNA shuffling by random fragmentation and PCR reassembly of gene fragments and synthetic oligonucleotides may be used to engineer the nucleotide sequences. In addition, site-directed mutagenesis may be used to insert new restriction sites, alter glycosylation patterns, change codon preference, produce splice variants, or introduce mutations, and so forth. In another embodiment of the invention, natural, modified, or recombinant nucleic acid sequences may be ligated to a heterologous sequence to encode a fusion protein. For example, to screen peptide libraries for inhibitors of polypeptide activity, it may be useful to encode a chimeric protein that can be recognized by a commercially available antibody. A fusion protein may also be engineered to contain a cleavage site located between the polypeptide-encoding sequence and the heterologous protein sequence, so that the polypeptide may be cleaved and purified away from the heterologous moiety. Sequences encoding a desired polypeptide may be synthesized, in whole or in part, using chemical methods well known in the art (see Caruthers, M. H. et al. (1980) Nucl. Acids Res. Symp. Ser. 215-223, Horn, T. et al. (1980) Nucl. Acids Res. Symp. Ser. 225-232). Alternatively, the protein itself may be produced using chemical methods to synthesize the amino acid sequence of a polypeptide, or a portion thereof. For example, peptide synthesis can be performed using various solid-phase techniques (Roberge, J. Y et al. (1995) Science 269:202-204) and automated synthesis may be achieved, for example, using the ABI 431 A Peptide Synthesizer (Perkin Elmer). A newly synthesized peptide may be substantially purified by preparative high performance liquid chromatography, for example (e.g., Creighton, T. (1983) Proteins, Structures and Molecular Principles, WH Freeman and Co., New York, N.Y), or other comparable techniques available in the art. The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g., the Edman degradation procedure). Additionally, the amino acid sequence of a polypeptide, or any part thereof, may be altered during direct synthesis and/or combined using chemical methods with sequences from other proteins, or any part thereof, to produce a variant polypeptide. In order to express a desired polypeptide, the nucleotide sequences encoding the polypeptide, or functional equivalents, may be inserted into appropriate expression vector, i.e., a vector which contains the necessary elements for the transcription and translation ofthe inserted coding sequence. Methods which are well known to those skilled in the art may be used to construct expression vectors containing sequences encoding a polypeptide of interest and appropriate transcriptional and translational control elements. These methods include in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination. Such techniques are described in Sambrook, J. et al. (1989) Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Press, Plainview, N.Y, and Ausubel, F. M. et al. (1989) Current Protocols in Molecular Biology, John Wiley & Sons, New York. N.Y A variety of expression vector/host systems may be utilized to contain and express polynucleotide sequences. These include, but are not limited to, microorganisms such as bacteria transformed with recombinant bacteriophage, plasmid, or cosmid DNA expression vectors; yeast transformed with yeast expression vectors; insect cell systems infected with virus expression vectors (e.g., baculovirus); plant cell systems transformed with virus expression vectors (e.g. , cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV) or with bacterial expression vectors (e.g., Ti or pBR322 plasmids); or animal cell systems.. The "control elements" or "regulatory sequences" present in an expression vector are those non-translated regions of the vector—enhancers, promoters, 5' and 3' untranslated regions— which interact with host cellular proteins to carry out transcription and translation. Such elements may vary in their strength and specificity. Depending on the vector system and host utilized, any number of suitable transcription and translation elements, including constitutive and inducible promoters, may be used. For example, when cloning in bacterial systems, inducible promoters such as the hybrid lacZ promoter of the PBLUESCRIPT phagemid (Stratagene, LaJolla, Calif.) or PSPORT1 plasmid (Gibco BRL) and the like may be used.. In mammalian cell systems, promoters from mammalian genes or from mammalian viruses are generally preferred. If it is necessary to generate a cell line that contains multiple copies of the sequence encoding a polypeptide, vectors based on SV40 or EBV may be advantageously used with an appropriate selectable marker. In bacterial systems, a number of expression vectors may be selected depending upon the use intended for the expressed polypeptide. For example, when large quantities are needed, for example for the induction of antibodies, vectors which direct high level expression of fusion proteins that are readily purified may be used. Such vectors include, but are not limited to, the multifunctional E. coli cloning and expression vectors such as BLUESCRIPT (Stratagene), in which the sequence encoding the polypeptide of interest may be ligated into the vector in frame with sequences for the amino-terminal Met and the subsequent 7 residues of β-galactosidase so that a hybrid protein is produced; pIN vectors (Van Heeke, G. and S. M. Schuster (1989) J. Biol. Chem. 264:5503-5509); and the like. pGEX vectors (Promega, Madison, Wis.) may also be used to express foreign polypeptides as fusion proteins with glutathione S- transferase (GST). In general, such fusion proteins are soluble and can easily be purified from lysed cells by adsorption to glutathione-agarose beads followed by elution in the presence of free glutathione. Proteins made in such systems may be designed to include heparin, thrombin, or factor XA protease cleavage sites so that the cloned polypeptide of interest can be released from the GST moiety at will. In the yeast, Saccharomyces cerevisiae, a number of vectors containing constitutive or inducible promoters such as alpha factor, alcohol oxidase, and PGH may be used. For reviews, see Ausubel et al. (supra) and Grant et al. (1987) Methods Enzymol. 153:516-544. In cases where plant expression vectors are used, the expression of sequences encoding polypeptides may be driven by any of a number of promoters. For example, viral promoters such as the 35S and 19S promoters of CaMV may be used alone or in combination with the omega leader sequence from TMV (Takamatsu, N. (1987) EMBO J. 6:307-311. Alternatively, plant promoters such as the small subunit of RUBISCO or heat shock promoters may be used (Coruzzi, G. et al. (1984) EMBO J. 3:1671-1680; Broglie, R. et al. (1984) Science 224:838-843; and Winter, J. et al. (1991) Results Probl. Cell Differ. 17:85-105). These constructs can be introduced into plant cells by direct DNA transformation or pathogen-mediated transfection. Such techniques are described in a number of generally available reviews (see, for example, Hobbs, S. or Murry, L. E. in McGraw Hill Yearbook of Science and Technology (1992) McGraw Hill, New York, N.Y; pp. 191-196). An insect system may also be used to express a polypeptide of interest. For example, in one such system, Autographa californica nuclear polyhedrosis virus (AcNPV) is used as a vector to express foreign genes in Spodoptera frugiperda cells or in Trichoplusia larvae. The sequences encoding the polypeptide may be cloned into a non-essential region ofthe virus, such as the polyhedrin gene, and placed under control of the polyhedrin promoter. Successful insertion of the polypeptide-encoding sequence will render the polyhedrin gene inactive and produce recombinant virus lacking coat protein. The recombinant viruses may then be used to infect, for example, S. frugiperda cells or Trichoplusia larvae in which the polypeptide of interest may be expressed (Engelhard, E. K. et al. (1994) Proc. Nat. Acad. Sci. 91 :3224-3227). In mammalian host cells, a number of viral-based expression systems are generally available. For example, in cases where an adenovirus is used as an expression vector, sequences encoding a polypeptide of interest may be ligated into an adenovirus transcription/translation complex consisting of the late promoter and tripartite leader sequence. Insertion in a non-essential El or E3 region ofthe viral genome may be used to obtain a viable virus which is capable of expressing the polypeptide in infected host cells (Logan, J. and Shenk, T. (1984) Proc. Natl. Acad. Sci. 81:3655-3659). In addition, transcription enhancers, such as the Rous sarcoma virus (RSV) enhancer, may be used to increase expression in mammalian host cells. Specific initiation signals may also be used to achieve more efficient translation of sequences encoding a polypeptide of interest. Such signals include the ATG initiation codon and adjacent sequences. In cases where sequences encoding the polypeptide, its initiation codon, and upstream sequences are inserted into the appropriate expression vector, no additional transcriptional or translational control signals may be needed. However, in cases where only coding sequence, or a portion thereof, is inserted, exogenous translational control signals including the ATG initiation codon should be provided. Furthermore, the initiation codon should be in the correct reading frame to ensure translation of the entire insert. Exogenous translational elements and initiation codons may be of various origins, both natural and synthetic. The efficiency of expression may be enhanced by the inclusion of enhancers which are appropriate for the particular cell system which is used, such as those described in the literature (Scharf, D. et al. (1994) Results Probl. Cell Differ. 20:125-162). In addition, a host cell strain may be chosen for its ability to modulate the expression of the inserted sequences or to process the expressed protein in the desired fashion. Such modifications of the polypeptide include, but are not limited to, acetylation, carboxylation. glycosylation, phosphorylation, lipidation, and acylation. Post-translational processing which cleaves a "prepro" form of the protein may also be used to facilitate correct insertion, folding and/or function. Different host cells such as CHO, HeLa, MDCK, HEK293, and WI38, which have specific cellular machinery and characteristic mechanisms for such post-translational activities, may be chosen to ensure the correct modification and processing ofthe foreign protein. For long-term, high-yield production of recombinant proteins, stable expression is generally preferred. For example, cell lines which stably express a polynucleotide of interest may be transformed using expression vectors which may contain viral origins of replication and/or endogenous expression elements and a selectable marker gene on the same or on a separate vector. Following the introduction of the vector, cells may be allowed to grow for 1-2 days in an enriched media before they are switched to selective media. The purpose of the selectable marker is to confer resistance to selection, and its presence allows growth and recovery of cells which successfully express the introduced sequences. Resistant clones of stably transformed cells may be proliferated using tissue culture techniques appropriate to the cell type. Any number of selection systems may be used to recover transformed cell lines. These include, but are not limited to, the herpes simplex virus thymidine kinase (Wigler, M. et al. (1977) Cell 11:223-32) and adenine phosphoribosyltransferase (Lowy, I. et al. (1990) Cell 22:817-23) genes which can be employed in tk.sup.- or aprt.sup.- cells, respectively. Also, antimetabolite, antibiotic or herbicide resistance can be used as the basis for selection; for example, dhfr which confers resistance to methotrexate (Wigler, M. et al. (1980) Proc. Natl. Acad. Sci. 77:3567-70); npt, which confers resistance to the aminoglycosides, neomycin and G-418 (Colbere-Garapin, F. et al (1981) J. Mol. Biol. 150:1-14); and als or pat, which confer resistance to chlorsulfuron and phosphinotricin acetyltransferase, respectively (Murry, supra). Additional selectable genes have been described, for example, trpB, which allows cells to utilize indole in place of tryptophan, or hisD, which allows cells to utilize histinol in place of histidine (Hartman, S. C. and R. C. Mulligan (1988) Proc. Natl. Acad. Sci. 85:8047-51). Recently, the use of visible markers has gained popularity with such markers as anthocyanins, β glucuronidase and its substrate GUS, and luciferase and its substrate luciferin, being widely used not only to identify transformants, but also to quantify the amount of transient or stable protein expression attributable to a specific vector system (Rhodes, C. A. et al. (1995) Methods Mol. Biol. 55:121-131). Although the presence/absence of marker gene expression suggests that the gene of interest is also present, its presence and expression may need to be confirmed. For example, if the sequence encoding a polypeptide is inserted within a marker gene sequence, recombinant cells containing sequences can be identified by the absence of marker gene function. Alternatively, a marker gene can be placed in tandem with a polypeptide-encoding sequence under the control of a single promoter. Expression of the marker gene in response to induction or selection usually indicates expression ofthe tandem gene as well. Alternatively, host cells which contain and express a desired polynucleotide sequence may be identified by a variety of procedures known to those of skill in the art. These procedures include, but are not limited to, DNA-DNA or DNA- RNA hybridizations and protein bioassay or immunoassay techniques which include membrane, solution, or chip based technologies for the detection and/or quantification of nucleic acid or protein. A variety of protocols for detecting and measuring the expression of polynucleotide-encoded products, using either polyclonal or monoclonal antibodies specific for the product are known in the art. Examples include enzyme-linked immunosorbent assay (ELISA), radioimmunoassay (RIA), and fluorescence activated cell sorting (FACS). A two-site, monoclonal-based immunoassay utilizing monoclonal antibodies reactive to two non-interfering epitopes on a given polypeptide may be preferred for some applications, but a competitive binding assay may also be employed. These and other assays are described, among other places, in Hampton, R. et al. (1990; Serological Methods, a Laboratory Manual, APS Press, St Paul. Minn.) and Maddox, D. E. et al. (1983; J. Exp. Med. 158:1211-1216). A wide variety of labels and conjugation techniques are known by those skilled in the art and may be used in various nucleic acid and amino acid assays. Means for producing labeled hybridization or PCR probes for detecting sequences related to polynucleotides include oligolabeling, nick translation, end-labeling or PCR amplification using a labeled nucleotide. Alternatively, the sequences, or any portions thereof may be cloned into a vector for the production of an mRNA probe. Such vectors are known in the art, are commercially available, and may be used to synthesize RNA probes in vitro by addition of an appropriate RNA polymerase such as T7, T3, or SP6 and labeled nucleotides. These procedures may be conducted using a variety of commercially available kits Amersham Pharmacia Biotech, Promega, and US Biochemical Corp. Suitable reporter molecules or labels, which may be used, include radionuclides, enzymes, fluorescent, chemiluminescent, or chromogenic agents as well as substrates, cofactors, inhibitors, magnetic particles, and the like. Host cells transformed with a polynucleotide sequence of interest may be cultured under conditions suitable for the expression and recovery of the protein from cell culture. The protein produced by a recombinant cell may be secreted or contained intracellularly depending on the sequence and/or the vector used. As will be understood by those of skill in the art, expression vectors containing polynucleotides of the invention may be designed to contain signal sequences which direct secretion of the encoded polypeptide through a prokaryotic or eukaryotic cell membrane. Other recombinant constructions may be used to join sequences encoding a polypeptide of interest to nucleotide sequence encoding a polypeptide domain which will facilitate purification of soluble proteins. Such purification facilitating domains include, but are not limited to, metal chelating peptides such as histidine-tryptophan modules that allow purification on immobilized metals, protein A domains that allow purification on immobilized immunoglobulin, and the domain utilized in the FLAGS extension/affinity purification system (Immunex Corp., Seattle, Wash.). The inclusion of cleavable linker sequences such as those specific for Factor XA or enterokinase (Invitrogen. San Diego, Calif.) between the purification domain and the encoded polypeptide may be used to facilitate purification. One such expression vector provides for expression of a fusion protein containing a polypeptide of interest and a nucleic acid encoding 6 histidine residues preceding a thioredoxin or an enterokinase cleavage site. The histidine residues facilitate purification on IMIAC (immobilized metal ion affinity chromatography) as described in Porath, J. et al. (1992, Prot. Exp. Purif. 3: 263-281) while the enterokinase cleavage site provides a means for purifying the desired polypeptide from the fusion protein. A discussion of vectors which contain fusion proteins is provided in Kroll, D. J. et al. (1993; DNA Cell Biol. 12:441-453). In addition to recombinant production methods, polypeptides of the invention, and fragments thereof, may be produced by direct peptide synthesis using solid-phase techniques (Merrifield J. (1963) J. Am. Chem. Soc. 85:2149-2154). Protein synthesis may be performed using manual techniques or by automation. Automated synthesis may be achieved, for example, using Applied Biosystems 431 A Peptide Synthesizer (Perkin Elmer). Alternatively, various fragments may be chemically synthesized separately and combined using chemical methods to produce the full length molecule. SITE-SPECIFIC MUTAGENESIS Site-specific mutagenesis is a technique useful in the preparation of individual peptides, biologically functional equivalent polypeptides, and other useful variants, through specific mutagenesis of the underlying polynucleotides that encode them. The technique, well-known to those of skill in the art, further provides a ready ability to prepare and test sequence variants, for example, incorporating one or more of the foregoing considerations, by introducing one or more nucleotide sequence changes into the DNA. Site-specific mutagenesis allows the production of mutants through the use of specific oligonucleotide sequences which encode the DNA sequence of the desired mutation, as well as a sufficient number of adjacent nucleotides, to provide a primer sequence of sufficient size and sequence complexity to form a stable duplex on both sides of the deletion junction being traversed. Mutations may be employed in a selected polynucleotide sequence to improve, alter, decrease, modify, or otherwise change the properties of the polynucleotide itself, and/or alter the properties, activity, composition, stability, or primary sequence ofthe encoded polypeptide. In certain embodiments of the present invention, the inventors contemplate the mutagenesis of the disclosed polynucleotide sequences to alter one or more properties of the encoded polypeptide, such as the antigenicity of a polypeptide vaccine. The techniques of site-specific mutagenesis are well-known in the art, and are widely used to create variants of both polypeptides and polynucleotides. For example, site-specific mutagenesis is often used to alter a specific portion of a DNA molecule. In such embodiments, a primer comprising typically about 14 to about 25 nucleotides or so in length is employed, with about 5 to about 10 residues on both sides of the junction of the sequence being altered. As will be appreciated by those of skill in the art, site-specific mutagenesis techniques have often employed a phage vector that exists in both a single stranded and double stranded form. Typical vectors useful in site-directed mutagenesis include vectors such as the Ml 3 phage. These phage are readily commercially-available and their use is generally well-known to those skilled in the art. Double-stranded plasmids are also routinely employed in site directed mutagenesis that eliminates the step of transferring the gene of interest from a plasmid to a phage. In general, site-directed mutagenesis in accordance herewith is performed by first obtaining a single-stranded vector or melting apart of two strands of a double-stranded vector that includes within its sequence a DNA sequence that encodes the desired peptide. An oligonucleotide primer bearing the desired mutated sequence is prepared, generally synthetically. This primer is then annealed with the single-stranded vector, and subjected to DNA polymerizing enzymes such as E. coli polymerase I Klenow fragment, in order to complete the synthesis of the mutation-bearing strand. Thus, a heteroduplex is formed wherein one strand encodes the original non-mutated sequence and the second strand bears the desired mutation. This heteroduplex vector is then used to transform appropriate cells, such as E. coli cells, and clones are selected which include recombinant vectors bearing the mutated sequence arrangement. The preparation of sequence variants of the selected peptide-encoding DNA segments using site-directed mutagenesis provides a means of producing potentially useful species and is not meant to be limiting as there are other ways in which sequence variants of peptides and the DNA sequences encoding them may be obtained. For example, recombinant vectors encoding the desired peptide sequence may be treated with mutagenic agents, such as hydroxylamine, to obtain sequence variants. Specific details regarding these methods and protocols are found in the teachings of Maloy et al, 1994; Segal, 1976; Prokop and Bajpai, 1991; Kuby, 1994; and Maniatis et al, 1982, each incorporated herein by reference, for that purpose. As used herein, the term "oligonucleotide directed mutagenesis procedure" refers to template-dependent processes and vector-mediated propagation which result in an increase in the concentration of a specific nucleic acid molecule relative to its initial concentration, or in an increase in the concentration of a detectable signal, such as amplification. As used herein, the term "oligonucleotide directed mutagenesis procedure" is intended to refer to a process that involves the template-dependent extension of a primer molecule. The term template dependent process refers to nucleic acid synthesis of an RNA or a DNA molecule wherein the sequence of the newly synthesized strand of nucleic acid is dictated by the well-known rules of complementary base pairing (see, for example, Watson, 1987). Typically, vector mediated methodologies involve the introduction ofthe nucleic acid fragment into a DNA or RNA vector, the clonal amplification of the vector, and the recovery of the amplified nucleic acid fragment. Examples of such methodologies are provided by U. S. Patent No. 4,237,224, specifically incorporated herein by reference in its entirety. POLYNUCLEOTIDE AMPLIFICATION TECHNIQUES A number of template dependent processes are available to amplify the target sequences of interest, i.e., a polynucleotide sequence disclosed herein, that is present in a sample. One of the best known amplification methods is the polymerase chain reaction (PCR™) which is described in detail in U. S. Patent Nos. 4,683,195, 4,683,202 and 4,800,159, each of which is incorporated herein by reference in its entirety. Briefly, in PCR™, two primer sequences are prepared which are complementary to regions on opposite complementary strands of the target sequence. An excess of deoxynucleoside triphosphates is added to a reaction mixture along with a DNA polymerase (e.g., Taq polymerase). If the target sequence is present in a sample, the primers will bind to the target and the polymerase will cause the primers to be extended along the target sequence by adding on nucleotides. By raising and lowering the temperature of the reaction mixture, the extended primers will dissociate from the target to form reaction products, excess primers will bind to the target and to the reaction product and the process is repeated. Preferably reverse transcription and PCR™ amplification procedure may be performed in order to quantify the amount of mRNA amplified. Polymerase chain reaction methodologies are well known in the art. Another method for amplification is the ligase chain reaction (referred to as LCR), disclosed in Eur. Pat. Appl. Publ. No. 320,308 (specifically incoφorated herein by reference in its entirety). In LCR, two complementary probe pairs are prepared, and in the presence of the target sequence, each pair will bind to opposite complementary strands ofthe target such that they abut. In the presence of a ligase, the two probe pairs will link to form a single unit. By temperature cycling, as in PCR™, bound ligated units dissociate from the target and then serve as "target sequences" for ligation of excess probe pairs. U. S. Patent No. 4,883,750, incoφorated herein by reference in its entirety, describes an alternative method of amplification similar to LCR for binding probe pairs to a target sequence. Qbeta Replicase, described in PCT Intl. Pat. Appl. Publ. No. PCT/US87/00880, incoφorated herein by reference in its entirety, may also be used as still another amplification method in the present invention. In this method, a replicative sequence of RNA that has a region complementary to that of a target is added to a sample in the presence of an RNA polymerase. The polymerase will copy the replicative sequence that can then be detected. , An isothermal amplification method, in which restriction endonucleases and ligases are used to achieve the amplification of target molecules that contain nucleotide 5'-[α-thio]triphosphates in one strand of a restriction site (Walker et al, 1992), may also be useful in the amplification of nucleic acids in the present invention. Strand Displacement Amplification (SDA) is another method of carrying out isothermal amplification of nucleic acids which involves multiple rounds of strand displacement and synthesis, i.e,. nick translation. A similar method, called Repair Chain Reaction (RCR) is another method of amplification which may be useful in the present invention and is involves annealing several probes throughout a region targeted for amplification, followed by a repair reaction in which only two of the four bases are present. The other two bases can be added as biotinylated derivatives for easy detection. A similar approach is used in SDA. Sequences can also be detected using a cyclic probe reaction (CPR). In CPR, a probe having a 3' and 5' sequences of non-target DNA and an internal or "middle" sequence of the target protein specific RNA is hybridized to DNA which is present in a sample. Upon hybridization, the reaction is treated with RNaseH, and the products ofthe probe are identified as distinctive products by generating a signal that is released after digestion. The original template is annealed to another cycling probe and the reaction is repeated. Thus, CPR involves amplifying a signal generated by hybridization of a probe to a target gene specific expressed nucleic acid. Still other amplification methods described in Great Britain Pat. Appl. No. 2 202 328, and in PCT Intl. Pat. Appl. Publ. No. PCT/US89/01025, each of which is incoφorated herein by reference in its entirety, may be used in accordance with the present invention. In the former application, "modified" primers are used in a PCR- like, template and enzyme dependent synthesis. The primers may be modified by labeling with a capture moiety (e.g., biotin) and/or a detector moiety (e.g., enzyme). In the latter application, an excess of labeled probes is added to a sample. In the presence of the target sequence, the probe binds and is cleaved catalytically. After cleavage, the target sequence is released intact to be bound by excess probe. Cleavage ofthe labeled probe signals the presence ofthe target sequence. Other nucleic acid amplification procedures include transcription-based amplification systems (TAS) (Kwoh et al, 1989; PCT Intl. Pat. Appl. Publ. No. WO 88/10315, incoφorated herein by reference in its entirety), including nucleic acid sequence based amplification (NASBA) and 3SR. In NASBA, the nucleic acids can be prepared for amplification by standard phenol/chloroform extraction, heat denaturation of a sample, treatment with lysis buffer and minispin columns for isolation of DNA and RNA or guanidinium chloride extraction of RNA. These amplification techniques involve annealing a primer that has sequences specific to the target sequence. Following polymerization, DNA/RNA hybrids are digested with RNase H while double stranded DNA molecules are heat-denatured again. In either case the single stranded DNA is made fully double stranded by addition of second target-specific primer, followed by polymerization. The double stranded DNA molecules are then multiply transcribed by a polymerase such as T7 or SP6. In an isothermal cyclic reaction, the RNAs are reverse transcribed into DNA, and transcribed once again with a polymerase such as T7 or SP6. The resulting products, whether truncated or complete, indicate target-specific sequences. Eur. Pat. Appl. Publ. No. 329,822, incoφorated herein by reference in its entirety, disclose a nucleic acid amplification process involving cyclically synthesizing single-stranded RNA ("ssRNA"), ssDNA, and double-stranded DNA (dsDNA), which may be used in accordance with the present invention. The ssRNA is a first template for a first primer oligonucleotide, which is elongated by reverse transcriptase (RNA-dependent DNA polymerase). The RNA is then removed from resulting DNA:RNA duplex by the action of ribonuclease H (RNase H, an RNase specific for RNA in a duplex with either DNA or RNA). The resultant ssDNA is a second template for a second primer, which also includes the sequences of an RNA polymerase promoter (exemplified by T7 RNA polymerase) 5' to its homology to its template. This primer is then extended by DNA polymerase (exemplified by the large "Klenow" fragment of E. coli DNA polymerase I), resulting as a double-stranded DNA ("dsDNA") molecule, having a sequence identical to that ofthe original RNA between the primers and having additionally, at one end, a promoter sequence. This promoter sequence can be used by the appropriate RNA polymerase to make many RNA copies ofthe DNA. These copies can then re-enter the cycle leading to very swift amplification. With proper choice of enzymes, this amplification can be done isothermally without addition of enzymes at each cycle. Because of the cyclical nature of this process, the starting sequence can be chosen to be in the form of either DNA or RNA. PCT Intl. Pat. Appl. Publ. No. WO 89/06700, incoφorated herein by reference in its entirety, disclose a nucleic acid sequence amplification scheme based on the hybridization of a promoter/primer sequence to a target single-stranded DNA ("ssDNA") followed by transcription of many RNA copies of the sequence. This scheme is not cyclic; i.e,. new templates are not produced from the resultant RNA transcripts. Other amplification methods include "RACE" (Frohman, 1990), and "one-sided PCR" (Ohara, 1989) which are well-known to those of skill in the art. Methods based on ligation of two (or more) oligonucleotides in the presence of nucleic acid having the sequence of the resulting "di-oligonucleotide", thereby amplifying the di-oligonucleotide (Wu and Dean, 1996, incoφorated herein by reference in its entirety), may also be used in the amplification of DNA sequences ofthe present invention. BIOLOGICAL FUNCTIONAL EQUIVALENTS Modification and changes may be made in the structure of the polynucleotides and polypeptides ofthe present invention and still obtain a "functional" molecule that encodes a polypeptide with desirable characteristics. As mentioned above, it is often desirable to introduce one or more mutations into a specific polynucleotide sequence. In certain circumstances, the resulting encoded polypeptide sequence is altered by this mutation, or in other cases, the sequence of the polypeptide is unchanged by one or more mutations in the encoding polynucleotide. When it is desirable to alter the amino acid sequence of a polypeptide to create an equivalent, or even an improved, second-generation molecule, the amino acid changes may be achieved by changing one or more ofthe codons ofthe encoding DNA sequence, according to Table 1. For example, certain amino acids may be substituted for other amino acids in a protein structure without appreciable loss of interactive binding capacity with structures such as, for example, antigen-binding regions of antibodies or binding sites on substrate molecules. Since it is the interactive capacity and nature of a protein that defines that protein's biological functional activity, certain amino acid sequence substitutions can be made in a protein sequence, and, of course, its underlying DNA coding sequence, and nevertheless obtain a protein with like properties. It is thus contemplated by the inventors that various changes may be made in the peptide sequences of the disclosed compositions, or corresponding DNA sequences which encode said peptides without appreciable loss of their biological utility or activity. TABLE 1 Amino Acids Codons Alanine Ala A GCA GCC GCG GCU Cysteine Cys C UGC UGU Aspartic acid Asp D GAC GAU Glutamic acid Glu E GAA GAG Phenylalanine Phe F UUC uuu Glycine Gly G GGA GGC GGG GGU Histidine His H CAC CAU Isoleucine Ile I AUA AUC AUU Lysine Lys K AAA AAG Leucine Leu L UUA UUG CUA CUC CUG CUU Methionine Met M AUG Asparagine Asn N AAC AAU Proline Pro P CCA CCC CCG CCU Glutamine Gin Q CAA CAG Arginine Arg R AGA AGG CGA CGC CGG CGU Serine Ser S AGC AGU UCA UCC UCG UCU Threonine Thr T ACA ACC ACG ACU Valine Val V GUA GUC GUG GUU Tryptophan Trp w UGG Tyrosine Tyr Y UAC UAU In making such changes, the hydropathic index of amino acids may be considered. The importance of the hydropathic amino acid index in conferring interactive biologic function on a protein is generally understood in the art (Kyte and Doolittle, 1982, incoφorate herein by reference). It is accepted that the relative hydropathic character of the amino acid contributes to the secondary structure of the resultant protein, which in turn defines the interaction of the protein with other molecules, for example, enzymes, substrates, receptors, DNA, antibodies, antigens, and the like. Each amino acid has been assigned a hydropathic index on the basis of its hydrophobicity and charge characteristics (Kyte and Doolittle, 1982). These values are: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5); methionine (+1.9); alanine (+1.8); glycine (-0.4); threonine (-0.7); serine (- 0.8); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (- 3.5); glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9); and arginine (- 4.5). It is known in the art that certain amino acids may be substituted by other amino acids having a similar hydropathic index or score and still result in a protein with similar biological activity, i.e., still obtain a biological functionally equivalent protein. In making such changes, the substitution of amino acids whose hydropathic indices are within +2 is preferred, those within +1 are particularly preferred, and those within ±0.5 are even more particularly preferred. It is also understood in the art that the substitution of like amino acids can be made effectively on the basis of hydrophilicity. U. S. Patent 4,554,101 (specifically incoφorated herein by reference in its entirety), states that the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with a biological property ofthe protein. As detailed in U. S. Patent 4,554,101, the following hydrophilicity values have been assigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0 ± 1); glutamate (+3.0 ± 1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (-0.4); proline (-0.5 ± 1); alanine (-0.5); histidine (-0.5); cysteine (-1.0); methionine (—1.3); valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3); phenylalanine (-2.5); tryptophan (-3.4). It is understood that an amino acid can be substituted for another having a similar hydrophilicity value and still obtain a biologically equivalent, and in particular, an immunologically equivalent protein. In such changes, the substitution of amino acids whose hydrophilicity values are within ±2 is preferred, those within ±1 are particularly preferred, and those within ±0.5 are even more particularly preferred. As outlined above, amino acid substitutions are generally therefore based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. Exemplary substitutions that take various ofthe foregoing characteristics into consideration are well known to those of skill in the art and include: arginine and lysine; glutamate and aspartate; serine and threonine; glutamine and asparagine; and valine, leucine and isoleucine. In addition, any polynucleotide may be further modified to increase stability in vivo. Possible modifications include, but are not limited to, the addition of flanking sequences at the 5' and/or 3' ends; the use of phosphorothioate or 2' O-methyl rather than phosphodiesterase linkages in the backbone; and/or the inclusion of nontraditional bases such as inosine, queosine and wybutosine, as well as acetyl- methyl-, thio- and other modified forms of adenine, cytidine, guanine, thymine and uridine. IN VIVO POLYNUCLEOTIDE DELIVERY TECHNIQUES In additional embodiments, genetic constructs comprising one or more of the polynucleotides of the invention are introduced into cells in vivo. This may be achieved using any of a variety or well known approaches, several of which are outlined below for the puφose of illustration. 1. ADENOVIRUS One ofthe preferred methods for in vivo delivery of one or more nucleic acid sequences involves the use of an adenovirus expression vector. "Adenovirus expression vector" is meant to include those constructs containing adenovirus sequences sufficient to (a) support packaging of the construct and (b) to express a polynucleotide that has been cloned therein in a sense or antisense orientation. Of course, in the context of an antisense construct, expression does not require that the gene product be synthesized. The expression vector comprises a genetically engineered form of an adenovirus. Knowledge of the genetic organization of adenovirus, a 36 kb, linear, double-stranded DNA virus, allows substitution of large pieces of adenoviral DNA with foreign sequences up to 7 kb (Grunhaus and Horwitz, 1992). In contrast to retrovirus, the adenoviral infection of host cells does not result in chromosomal integration because adenoviral DNA can replicate in an episomal manner without potential genotoxicity. Also, adenoviruses are structurally stable, and no genome rearrangement has been detected after extensive amplification. Adenovirus can infect virtually all epithelial cells regardless of their cell cycle stage. So far, adenoviral infection appears to be linked only to mild disease such as acute respiratory disease in humans. Adenovirus is particularly suitable for use as a gene transfer vector because of its mid-sized genome, ease of manipulation, high titer, wide target-cell range and high infectivity. Both ends ofthe viral genome contain 100-200 base pair inverted repeats (ITRs), which are cis elements necessary for viral DNA replication and packaging. The early (E) and late (L) regions of the genome contain different transcription units that are divided by the onset of viral DNA replication. The El region (El A and E1B) encodes proteins responsible for the regulation of transcription of the viral genome and a few cellular genes. The expression ofthe E2 region (E2A and E2B) results in the synthesis of the proteins for viral DNA replication. These proteins are involved in DNA replication, late gene expression and host cell shut-off (Renan, 1990). The products of the late genes, including the majority of the viral capsid proteins, are expressed only after significant processing of a single primary transcript issued by the major late promoter (MLP). The MLP, (located at 16.8 m.u.) is particularly efficient during the late phase of infection, and all the mRNA's issued from this promoter possess a 5'-tripartite leader (TPL) sequence which makes them preferred mRNA's for translation. In a current system, recombinant adenovirus is generated from homologous recombination between shuttle vector and provirus vector. Due to the possible recombination between two proviral vectors, wild-type adenovirus may be generated from this process. Therefore, it is critical to isolate a single clone of virus from an individual plaque and examine its genomic structure. Generation and propagation of the current adenovirus vectors, which are replication deficient, depend on a unique helper cell line, designated 293, which was transformed from human embryonic kidney cells by Ad5 DNA fragments and constitutively expresses El proteins (Graham et al, 1977). Since the E3 region is dispensable from the adenovirus genome (Jones and Shenk, 1978), the current adenovirus vectors, with the help of 293 cells, carry foreign DNA in either the El, the D3 or both regions (Graham and Prevec, 1991). In nature, adenovirus can package approximately 105% of the wild-type genome (Ghosh-Choudhury et al, 1987), providing capacity for about 2 extra kB of DNA. Combined with the approximately 5.5 kB of DNA that is replaceable in the El and E3 regions, the maximum capacity of the current adenovirus vector is under 7.5 kB, or about 15% ofthe total length ofthe vector. More than 80% of the adenovirus viral genome remains in the vector backbone and is the source of vector-borne cytotoxicity. Also, the replication deficiency of the El- deleted virus is incomplete. For example, leakage of viral gene expression has been observed with the currently available vectors at high multiplicities of infection (MOI) (Mulligan, 1993). Helper cell lines may be derived from human cells such as human embryonic kidney cells, muscle cells, hematopoietic cells or other human embryonic mesenchymal or epithelial cells. Alternatively, the helper cells may be derived from the cells of other mammalian species that are permissive for human adenovirus. Such cells include, e.g., Vero cells or other monkey embryonic mesenchymal or epithelial cells. As stated above, the currently preferred helper cell line is 293. Recently, Racher et al. (1995) disclosed improved methods for culturing 293 cells and propagating adenovirus. In one format, natural cell aggregates are grown by inoculating individual cells into 1 liter siliconized spinner flasks (Techne, Cambridge, UK) containing 100-200 ml of medium. Following stirring at 40 φm, the cell viability is estimated with trypan blue. In another format, Fibra-Cel microcarriers (Bibby Sterlin, Stone, UK) (5 g/1) are employed as follows. A cell inoculum, resuspended in 5 ml of medium, is added to the carrier (50 ml) in a 250 ml Erlenmeyer flask and left stationary, with occasional agitation, for 1 to 4 h. The medium is then replaced with 50 ml of fresh medium and shaking initiated. For virus production, cells are allowed to grow to about 80% confluence, after which time the medium is replaced (to 25% ofthe final volume) and adenovirus added at an MOI of 0.05. Cultures are left stationary overnight, following which the volume is increased to 100% and shaking commenced for another 72 h. Other than the requirement that the adenovirus vector be replication defective, or at least conditionally defective, the nature of the adenovirus vector is not believed to be crucial to the successful practice ofthe invention. The adenovirus may be of any of the 42 different known serotypes or subgroups A-F. Adenovirus type 5 of subgroup C is the preferred starting material in order to obtain the conditional replication- defective adenovirus vector for use in the present invention. This is because Adenovirus type 5 is a human adenovirus about which a great deal of biochemical and genetic information is known, and it has historically been used for most constructions employing adenovirus as a vector. As stated above, the typical vector according to the present invention is replication defective and will not have an adenovirus El region. Thus, it will be most convenient to introduce the polynucleotide encoding the gene of interest at the position from which the El -coding sequences have been removed. However, the position of insertion of the construct within the adenovirus sequences is not critical to the invention. The polynucleotide encoding the gene of interest may also be inserted in lieu of the deleted E3 region in E3 replacement vectors as described by Karlsson et al. (1986) or in the E4 region where a helper cell line or helper virus complements the E4 defect. Adenovirus is easy to grow and manipulate and exhibits broad host range in vitro and in vivo. This group of viruses can be obtained in high titers, e.g., 10 - 10 π plaque-forming units per ml, and they are highly infective. The life cycle of adenovirus does not require integration into the host cell genome. The foreign genes delivered by adenovirus vectors are episomal and, therefore, have low genotoxicity to host cells. No side effects have been reported in studies of vaccination with wild-type adenovirus (Couch et al, 1963; Top et al, 1971), demonstrating their safety and therapeutic potential as in vivo gene transfer vectors. Adenovirus vectors have been used in eukaryotic gene expression (Levrero et al, 1991; Gomez-Foix et al, 1992) and vaccine development (Gru haus and Horwitz, 1992; Graham and Prevec, 1992). Recently, animal studies suggested that recombinant adenovirus could be used for gene therapy (Stratford-Perricaudet and Perricaudet, 1991; Stratford-Perricaudet et al, 1990; Rich et al, 1993). Studies in administering recombinant adenovirus to different tissues include trachea instillation (Rosenfeld et al, 1991; Rosenfeld et al, 1992), muscle injection (Ragot et al, 1993), peripheral intravenous injections (Herz and Gerard, 1993) and stereotactic inoculation into the brain (Le Gal La Salle et al, 1993). 2. RETROVIRUSES The retroviruses are a group of single-stranded RNA viruses characterized by an ability to convert their RNA to double-stranded DNA in infected cells by a process of reverse-transcription (Coffin, 1990). The resulting DNA then stably integrates into cellular chromosomes as a provirus and directs synthesis of viral proteins. The integration results in the retention of the viral gene sequences in the recipient cell and its descendants. The retroviral genome contains three genes, gag, pol, and env that code for capsid proteins, polymerase enzyme, and envelope components, respectively. A sequence found upstream from the gag gene contains a signal for packaging of the genome into virions. Two long terminal repeat (LTR) sequences are present at the 5' and 3' ends of the viral genome. These contain strong promoter and enhancer sequences and are also required for integration in the host cell genome (Coffin, 1990). In order to construct a retroviral vector, a nucleic acid encoding one or more oligonucleotide or polynucleotide sequences of interest is inserted into the viral genome in the place of certain viral sequences to produce a virus that is replication- defective. In order to produce virions, a packaging cell line containing the gag, pol, and env genes but without the LTR and packaging components is constructed (Mann et al, 1983). When a recombinant plasmid containing a cDNA, together with the retroviral LTR and packaging sequences is introduced into this cell line (by calcium phosphate precipitation for example), the packaging sequence allows the RNA transcript of the recombinant plasmid to be packaged into viral particles, which are then secreted into the culture media (Nicolas and Rubenstein, 1988; Temin, 1986; Mann et al, 1983). The media containing the recombinant retroviruses is then collected, optionally concentrated, and used for gene transfer. Retroviral vectors are able to infect a broad variety of cell types. However, integration and stable expression require the division of host cells (Paskind et al, 1975). A novel approach designed to allow specific targeting of retrovirus vectors was recently developed based on the chemical modification of a retrovirus by the chemical addition of lactose residues to the viral envelope. This modification could permit the specific infection of hepatocytes via sialoglycoprotein receptors. A different approach to targeting of recombinant retroviruses was designed in which biotinylated antibodies against a retroviral envelope protein and against a specific cell receptor were used. The antibodies were coupled via the biotin components by using streptavidin (Roux et al, 1989). Using antibodies against major histocompatibility complex class I and class II antigens, they demonstrated the infection of a variety of human cells that bore those surface antigens with an ecotropic virus in vitro (Roux et al , 1989). There are certain limitations to the use of retrovirus vectors in all aspects of the present invention. For example, retrovirus vectors usually integrate into random sites in the cell genome. This can lead to insertional mutagenesis through the interruption of host genes or through the insertion of viral regulatory sequences that can interfere with the function of flanking genes (Varmus et al., 1981). Another concern with the use of defective retrovirus vectors is the potential appearance of wild-type replication-competent virus in the packaging cells. This can result from recombination events in which the intact sequence from the recombinant virus inserts upstream from the gag, pol, and env sequence integrated in the host cell genome. However, new packaging cell lines are now available that should greatly decrease the likelihood of recombination (Markowitz et al., 1988; Hersdorffer et al, 1990). 3. ADENO-ASSOCIATED VIRUSES AAV (Ridgeway, 1988; Hermonat and Muzycska, 1984) is a paroviras, discovered as a contamination of adenoviral stocks. It is a ubiquitous virus (antibodies are present in 85% ofthe US human population) that has not been linked to any disease. It is also classified as a dependovirus, because its replications is dependent on the presence of a helper virus, such as adenovirus. Five serotypes have been isolated, of which AAV-2 is the best characterized. AAV has a single-stranded linear DNA that is encapsidated into capsid proteins VP1, VP2 and VP3 to form an icosahedral virion of 20 to 24 nm in diameter (Muzyczka and McLaughlin, 1988). The AAV DNA is approximately 4.7 kilobases long. It contains two open reading frames and is flanked by two ITRs (FIG. 2). There are two major genes in the AAV genome: rep and cap. The rep gene codes for proteins responsible for viral replications, whereas cap codes for capsid protein VP1-3. Each ITR forms a T-shaped haiφin structure. These terminal repeats are the only essential cis components of the AAV for chromosomal integration. Therefore, the AAV can be used as a vector with all viral coding sequences removed and replaced by the cassette of genes for delivery. Three viral promoters have been identified and named p5, pi 9, and p40, according to their map position. Transcription from p5 and pi 9 results in production of rep proteins, and transcription from p40 produces the capsid proteins (Hermonat and Muzyczka, 1984). There are several factors that prompted researchers to study the possibility of using rAAV as an expression vector One is that the requirements for delivering a gene to integrate into the host chromosome are smprisingly few. It is necessary to have the 145-bp ITRs, which are only 6% ofthe AAV genome. This leaves room in the vector to assemble a 4.5-kb DNA insertion. Wliile this carrying capacity may prevent the AAV from delivering large genes, it is amply suited for delivering the antisense constructs ofthe present invention. AAV is also a good choice of delivery vehicles due to its safety. There is a relatively complicated rescue mechanism: not only wild type adenovirus but also AAV genes are required to mobilize rAAV. Likewise, AAV is not pathogenic and not associated with any disease. The removal of viral coding sequences minimizes immune reactions to viral gene expression, and therefore, rAAV does not evoke an inflammatory response. 4. OTHER VIRAL VECTORS AS EXPRESSION CONSTRUCTS Other viral vectors may be employed as expression constructs in the present invention for the delivery of oligonucleotide or polynucleotide sequences to a host cell. Vectors derived from viruses such as vaccinia virus (Ridgeway, 1988; Coupar et al, 1988), lentiviruses, polio viruses and heφes viruses may be employed. They offer several attractive features for various mammalian cells (Friedmann, 1989; Ridgeway, 1988; Coupar et al, 1988; Horwich et al, 1990). With the recent recognition of defective hepatitis B viruses, new insight was gained into the structure-function relationship of different viral sequences. In vitro studies showed that the virus could retain the ability for helper-dependent packaging and reverse transcription despite the deletion of up to 80% of its genome (Horwich et al, 1990). This suggested that large portions of the genome could be replaced with foreign genetic material. The hepatotropism and persistence (integration) were particularly attractive properties for liver-directed gene transfer. Chang et al. (1991) introduced the chloramphenicol acetyltransferase (CAT) gene into duck hepatitis B virus genome in the place ofthe polymerase, surface, and pre-surface coding sequences. It was cotransfected with wild-type virus into an avian hepatoma cell line. Culture media containing high titers of the recombinant virus were used to infect primary duckling hepatocytes. Stable CAT gene expression was detected for at least 24 days after transfection (Chang et al, 1991 ). 5. NON-VIRAL VECTORS In order to effect expression of the oligonucleotide or polynucleotide sequences of the present invention, the expression construct must be delivered into a cell. This delivery may be accomplished in vitro, as in laboratory procedures for transforming cells lines, or in vivo or ex vivo, as in the treatment of certain disease states. As described above, one preferred mechanism for delivery is via viral infection where the expression construct is encapsidated in an infectious viral particle. Once the expression construct has been delivered into the cell the nucleic acid encoding the desired oligonucleotide or polynucleotide sequences may be positioned and expressed at different sites. In certain embodiments, the nucleic acid encoding the construct may be stably integrated into the genome of the cell. This integration may be in the specific location and orientation via homologous recombination (gene replacement) or it may be integrated in a random, non-specific location (gene augmentation). In yet further embodiments, the nucleic acid may be stably maintained in the cell as a separate, episomal segment of DNA. Such nucleic acid segments or "episomes" encode sequences sufficient to permit maintenance and replication independent of or in synchronization with the host cell cycle. How the expression construct is delivered to a cell and where in the cell the nucleic acid remains is dependent on the type of expression construct employed. In certain embodiments of the invention, the expression construct comprising one or more oligonucleotide or polynucleotide sequences may simply consist of naked recombinant DNA or plasmids. Transfer of the construct may be performed by any of the methods mentioned above which physically or chemically permeabilize the cell membrane. This is particularly applicable for transfer in vitro but it may be applied to in vivo use as well. Dubensky et al. (1984) successfully injected polyomavirus DNA in the form of calcium phosphate precipitates into liver and spleen of adult and newborn mice demonstrating active viral replication and acute infection. Benvenisty and Reshef (1986) also demonstrated that direct intraperitoneal injection of calcium phosphate-precipitated plasmids results in expression ofthe transfected genes. It is envisioned that DNA encoding a gene of interest may also be transferred in a similar manner in vivo and express the gene product. Another embodiment of the invention for transferring a naked DNA expression construct into cells may involve particle bombardment. This method depends on the ability to accelerate DNA-coated microprojectiles to a high velocity allowing them to pierce cell membranes and enter cells without killing them (Klein et al, 1987). Several devices for accelerating small particles have been developed. One such device relies on a high voltage discharge to generate an electrical current, which in turn provides the motive force (Yang et al, 1990). The microprojectiles used have consisted of biologically inert substances such as tungsten or gold beads. Selected organs including the liver, skin, and muscle tissue of rats and mice have been bombarded in vivo (Yang et al, 1990; Zelenin et al, 1991). This may require surgical exposure of the tissue or cells, to eliminate any intervening tissue between the gun and the target organ, i.e., ex vivo treatment. Again, DNA encoding a particular gene may be delivered via this method and still be incoφorated by the present invention. ANTISENSE OLIGONUCLEOTIDES The end result of the flow of genetic information is the synthesis of protein. DNA is transcribed by polymerases into messenger RNA and translated on the ribosome to yield a folded, functional protein. Thus, even from this simplistic description of an extremely complex set of reactions, it is obvious that there are several steps along the route where protein synthesis can be inhibited. The native DNA segment coding for a polypeptide described herein, as all such mammalian DNA strands, has two strands: a sense strand and an antisense strand held together by hydrogen bonding. The messenger RNA coding for polypeptide has the same nucleotide sequence as the sense DNA strand except that the DNA thymidine is replaced by uridine. Thus, synthetic antisense nucleotide sequences will bind to a mRNA and inhibit expression of the protein encoded by that mRNA. Thus, the targeting of antisense oligonucleotides to bind mRNA is one mechanism to shut down protein synthesis, and, consequently, represents a powerful and targeted therapeutic approach. For example, the synthesis of polygalactauronase and the muscarine type 2 acetylcholine receptor are inhibited by antisense oligonucleotides directed to their respective mRNA sequences (U. S. Patent 5,739,119 and U. S. Patent 5,759,829, each specifically incoφorated herein by reference in its entirety). Further, examples of antisense inhibition have been demonstrated with the nuclear protein cyclin, the multiple drug resistance gene (MDG1), ICAM-1, E-selectin, STK-1, striatal GABAA receptor and human EGF (Jaskulski et al, 1988; Vasanthakumar and Ahmed, 1989; Peris et al, 1998; U. S. Patent 5,801,154; U. S. Patent 5,789,573; U. S. Patent 5,718,709 and U. S. Patent 5,610,288, each specifically incoφorated herein by reference in its entirety). Antisense constructs have also been described that inhibit and can be used to treat a variety of abnormal cellular proliferations, e.g., cancer (U. S. Patent 5,747,470; U. S. Patent 5,591,317 and U. S. Patent 5,783,683, each specifically incoφorated herein by reference in its entirety). Therefore, in exemplary embodiments, the invention provides oligonucleotide sequences that comprise all, or a portion of, any sequence that is capable of specifically binding to polynucleotide sequence described herein, or a complement thereof. In one embodiment, the antisense oligonucleotides comprise DNA or derivatives thereof. In another embodiment, the oligonucleotides comprise RNA or derivatives thereof. In a third embodiment, the oligonucleotides are modified DNAs comprising a phosphorothioated modified backbone. In a fourth embodiment, the oligonucleotide sequences comprise peptide nucleic acids or derivatives thereof. In each case, preferred compositions comprise a sequence region that is complementary, and more preferably substantially-complementary, and even more preferably, completely complementary to one or more portions of polynucleotides disclosed herein. Selection of antisense compositions specific for a given gene sequence is based upon analysis ofthe chosen target sequence (t.e.,in these illustrative examples the rat and human sequences) and determination of secondary structure, T m , binding energy, relative stability, and antisense compositions were selected based upon their relative inability to form dimers, haiφins, or other secondary structures that would reduce or prohibit specific binding to the target mRNA in a host cell. Highly preferred target regions of the mRNA, are those which are at or near the AUG translation initiation codon, and those sequences which were substantially complementary to 5' regions of the mRNA. These secondary structure analyses and target site selection considerations were performed using v.4 of the OLIGO primer analysis software (Rychlik, 1997) and the BLASTN 2.0.5 algorithm software (Altschul et al, 1997). The recent development of an antisense delivery method based on the use of a short peptide vector, termed MPG (27 residues), is also contemplated. The MPG peptide contains a hydrophobic domain derived from the fusion sequence of HIV gp41 and a hydrophilic domain from the nuclear localization sequence of SV40 T- antigen (Morris et al, 1997). It was demonstrated in that several molecules of the MPG peptides coat the antisense oligonucleotides and can be delivered into cultured mammalian cells in less than 1 hour with relatively high efficiency (90%). Further, the interaction with MPG strongly increases both the stability of the oligonucleotide to nuclease and the ability to cross the plasma membrane (Morris et al, 1997). RIBOZYMES Although proteins traditionally have been used for catalysis of nucleic acids, another class of macromolecules has emerged as useful in this endeavor. Ribozymes are RNA-protein complexes that cleave nucleic acids in a site-specific fashion. Ribozymes have specific catalytic domains that possess endonuclease activity (Kim and Cech, 1987; Gerlach et al, 1987; Forster and Symons, 1987). For example, a large number of ribozymes accelerate phosphoester transfer reactions with a high degree of specificity, often cleaving only one of several phosphoesters in an oligonucleotide substrate (Cech et al, 1981; Michel and Westhof, 1990; Reinhold-Hurek and Shub, 1992). This specificity has been attributed to the requirement that the substrate bind via specific base-pairing interactions to the internal guide sequence ("IGS") of the ribozyme prior to chemical reaction. Ribozyme catalysis has primarily been observed as part of sequence- specific cleavage/ligation reactions involving nucleic acids (Joyce, 1989; Cech et al, 1981). For example, U. S. Patent No. 5,354,855 (specifically incoφorated herein by reference) reports that certain ribozymes can act as endonucleases with a sequence specificity greater than that of known ribonucleases and approaching that of the DNA restriction enzymes. Thus, sequence-specific ribozyme-mediated inhibition of gene expression may be particularly suited to therapeutic applications (Scanlon et al, 1991; Sarver et al, 1990). Recently, it was reported that ribozymes elicited genetic changes in some cells lines to which they were applied; the altered genes included the oncogenes H-ras, c-fos and genes of HIV. Most of this work involved the modification of a target mRNA, based on a specific mutant codon that is cleaved by a specific ribozyme. Six basic varieties of naturally-occurring enzymatic RNAs are known presently. Each can catalyze the hydrolysis of RNA phosphodiester bonds in trans (and thus can cleave other RNA molecules) under physiological conditions. In general, enzymatic nucleic acids act by first binding to a target RNA. Such binding occurs through the target binding portion of a enzymatic nucleic acid which is held in close proximity to an enzymatic portion of the molecule that acts to cleave the target RNA. Thus, the enzymatic nucleic acid first recognizes and then binds a target RNA through complementary base-pairing, and once bound to the correct site, acts enzymatically to cut the target RNA. Strategic cleavage of such a target RNA will destroy its ability to direct synthesis of an encoded protein. After an enzymatic nucleic acid has bound and cleaved its RNA target, it is released from that RNA to search for another target and can repeatedly bind and cleave new targets. The enzymatic nature of a ribozyme is advantageous over many technologies, such as antisense technology (where a nucleic acid molecule simply binds to a nucleic acid target to block its translation) since the concentration of ribozyme necessary to affect a therapeutic treatment is lower than that of an antisense oligonucleotide. This advantage reflects the ability of the ribozyme to act enzymatically. Thus, a single ribozyme molecule is able to cleave many molecules of target RNA. In addition, the ribozyme is a highly specific inhibitor, with the specificity of inhibition depending not only on the base pairing mechanism of binding to the target RNA, but also on the mechanism of target RNA cleavage. Single mismatches, or base- substitutions, near the site of cleavage can completely eliminate catalytic activity of a ribozyme. Similar mismatches in antisense molecules do not prevent their action (Woolf et al, 1992). Thus, the specificity of action of a ribozyme is greater than that of an antisense oligonucleotide binding the same RNA site. The enzymatic nucleic acid molecule may be formed in a hammerhead, haiφin, a hepatitis δ virus, group I intron or RNaseP RNA (in association with an RNA guide sequence) or Neurospora VS RNA motif. Examples of hammerhead motifs are described by Rossi et al (1992). Examples of haiφin motifs are described by Hampel et al. (Eur. Pat. Appl. Publ. No. EP 0360257), Hampel and Tritz (1989), Hampel et al. (1990) and U. S. Patent 5,631,359 (specifically incoφorated herein by reference). An example of the hepatitis δ virus motif is described by Perrotta and Been (1992); an example ofthe RNaseP motif is described by Guerrier-Takada et al. (1983); Neurospora VS RNA ribozyme motif is described by Collins (Saville and Collins, 1990; Saville and Collins, 1991; Collins and Olive, 1993); and an example of the Group I intron is described in (U. S. Patent 4,987,071, specifically incoφorated herein by reference). All that is important in an enzymatic nucleic acid molecule of this invention is that it has a specific substrate binding site which is complementary to one or more ofthe target gene RNA regions, and that it have nucleotide sequences within or surrounding that substrate binding site which impart an RNA cleaving activity to the molecule. Thus the ribozyme constructs need not be limited to specific motifs mentioned herein. In certain embodiments, it may be important to produce enzymatic cleaving agents which exhibit a high degree of specificity for the RNA of a desired target, such as one of the sequences disclosed herein. The enzymatic nucleic acid molecule is preferably targeted to a highly conserved sequence region of a target mRNA. Such enzymatic nucleic acid molecules can be delivered exogenously to specific cells as required. Alternatively, the ribozymes can be expressed from DNA or RNA vectors that are delivered to specific cells. Small enzymatic nucleic acid motifs (e.g., of the hammerhead or the haiφin structure) may also be used for exogenous delivery. The simple structure of these molecules increases the ability of the enzymatic nucleic acid to invade targeted regions ofthe mRNA structure. Alternatively, catalytic RNA molecules can be expressed within cells from eukaryotic promoters. Those skilled in the art realize that any ribozyme can be expressed in eukaryotic cells from the appropriate DNA vector. The activity of such ribozymes can be augmented by their release from the primary transcript by a second ribozyme (Int. Pat. Appl. Publ. No. WO 93/23569, and Int. Pat. Appl. Publ. No. WO 94/02595, both hereby incoφorated by reference; Ohkawa et al, 1992; Taira et al, 1991; and Ventura etal, 1993). Ribozymes may be added directly, or can be complexed with cationic lipids, lipid complexes, packaged within liposomes, or otherwise delivered to target cells. The RNA or RNA complexes can be locally administered to relevant tissues ex vivo, or in vivo through injection, aerosol inhalation, infusion pump or stent, with or without their incoφoration in biopolymers. Ribozymes may be designed as described in Int. Pat. Appl. Publ. No. WO 93/23569 and Int. Pat. Appl. Publ. No. WO 94/02595, each specifically incoφorated herein by reference) and synthesized to be tested in vitro and in vivo, as described. Such ribozymes can also be optimized for delivery. While specific examples are provided, those in the art will recognize that equivalent RNA targets in other species can be utilized when necessary. Hammerhead or haiφin ribozymes may be individually analyzed by computer folding (Jaeger et al, 1989) to assess whether the ribozyme sequences fold into the appropriate secondary structure. Those ribozymes with unfavorable intramolecular interactions between the binding arms and the catalytic core are eliminated from consideration. Varying binding arm lengths can be chosen to optimize activity. Generally, at least 5 or so bases on each arm are able to bind to, or otherwise interact with, the target RNA. Ribozymes of the hammerhead or haiφin motif may be designed to anneal to various sites in the mRNA message, and can be chemically synthesized. The method of synthesis used follows the procedure for normal RNA synthesis as described in Usman et al. (1987) and in Scaringe et al. (1990) and makes use of common nucleic acid protecting and coupling groups, such as dimethoxytrityl at the 5'-end, and phosphoramidites at the 3'-end. Average stepwise coupling yields are typically >98%. Haiφin ribozymes may be synthesized in two parts and annealed to reconstruct an active ribozyme (Chowrira and Burke, 1992). Ribozymes may be modified extensively to enhance stability by modification with nuclease resistant groups, for example, 2'- amino, 2'-C-allyl, 2'-flouro, 2'-o-methyl, 2'-H (for a review see e.g., Usman and Cedergren, 1992). Ribozymes may be purified by gel electrophoresis using general methods or by high pressure liquid chromatography and resuspended in water. Ribozyme activity can be optimized by altering the length of the ribozyme binding arms, or chemically synthesizing ribozymes with modifications that prevent their degradation by serum ribonucleases (see e.g., Int. Pat. Appl. Publ. No. WO 92/07065; Perrault et al, 1990; Pieken et al, 1991; Usman and Cedergren, 1992; Int. Pat. Appl. Publ. No. WO 93/15187; Int. Pat. Appl. Publ. No. WO 91/03162; Eur. Pat. Appl. Publ. No. 92110298.4; U. S. Patent 5,334,711; and Int. Pat. Appl. Publ. No. WO 94/13688, which describe various chemical modifications that can be made to the sugar moieties of enzymatic RNA molecules), modifications which enhance their efficacy in cells, and removal of stem II bases to shorten RNA synthesis times and reduce chemical requirements. Sullivan et al. (Int. Pat. Appl. Publ. No. WO 94/02595) describes the general methods ' for delivery of enzymatic RNA molecules. Ribozymes may be administered to cells by a variety of methods known to those familiar to the art, including, but not restricted to, encapsulation in liposomes, by iontophoresis, or by incoφoration into other vehicles, such as hydrogels, cyclodextrins, biodegradable nanocapsules, and bioadhesive microspheres. For some indications, ribozymes may be directly delivered ex vivo to cells or tissues with or without the aforementioned vehicles. Alternatively, the RNA/vehicle combination may be locally delivered by direct inhalation, by direct injection or by use of a catheter, infusion pump or stent. Other routes of delivery include, but are not limited to, intravascular, intramuscular, subcutaneous or joint injection, aerosol inhalation, oral (tablet or pill form), topical, systemic, ocular, intraperitoneal and/or intrathecal delivery. More detailed descriptions of ribozyme delivery and administration are provided in Int. Pat. Appl. Publ. No. WO 94/02595 and Int. Pat. Appl. Publ. No. WO 93/23569, each specifically incoφorated herein by reference. Another means of accumulating high concentrations of a ribozyme(s) within cells is to incoφorate the ribozyme-encoding sequences into a DNA expression vector. Transcription of the ribozyme sequences are driven from a promoter for eukaryotic RNA polymerase I (pol I), RNA polymerase II (pol II), or RNA polymerase III (pol III). Transcripts from pol II or pol III promoters will be expressed at high levels in all cells; the levels of a given pol II promoter in a given cell type will depend on the nature of the gene regulatory sequences (enhancers, silencers, etc.) present nearby. Prokaryotic RNA polymerase promoters may also be used, providing that the prokaryotic RNA polymerase enzyme is expressed in the appropriate cells (Elroy-Stein and Moss, 1990; Gao and Huang, 1993; Lieber et al, 1993; Zhou et al, 1990). Ribozymes expressed from such promoters can function in mammalian cells (e.g., Kashani-Saber et al, 1992; Ojwang et al, 1992; Chen et al, 1992; Yu et al, 1993; L'Huillier et al, 1992; Lisziewicz et al, 1993). Such transcription units can be incoφorated into a variety of vectors for introduction into mammalian cells, including but not restricted to, plasmid DNA vectors, viral DNA vectors (such as adenovirus or adeno-associated vectors), or viral RNA vectors (such as retroviral, semliki forest virus, sindbis virus vectors). Ribozymes of this invention may be used as diagnostic tools to examine genetic drift and mutations within diseased cells. They can also be used to assess levels of the target RNA molecule. The close relationship between ribozyme activity and the structure of the target RNA allows the detection of mutations in any region of the molecule which alters the base-pairing and three-dimensional structure ofthe target RNA. By using multiple ribozymes described in this invention, one may map nucleotide changes which are important to RNA structure and function in vitro, as well as in cells and tissues. Cleavage of target RNAs with ribozymes may be used to inhibit gene expression and define the role (essentially) of specified gene products in the progression of disease. In this manner, other genetic targets may be defined as important mediators of the disease. These studies will lead to better treatment of the disease progression by affording the possibility of combinational therapies (e.g., multiple ribozymes targeted to different genes, ribozymes coupled with known small molecule inhibitors, or intermittent treatment with combinations of ribozymes and/or other chemical or biological molecules). Other in vitro uses of ribozymes of this invention are well known in the art, and include detection ofthe presence of mRNA associated with an IL-5 related condition. Such RNA is detected by determining the presence of a cleavage product after treatment with a ribozyme using standard methodology. PEPTIDE NUCLEIC ACIDS In certain embodiments, the inventors contemplate the use of peptide nucleic acids (PNAs) in the practice of the methods of the invention. PNA is a DNA mimic in which the nucleobases are attached to a pseudopeptide backbone (Good and Nielsen, 1997). PNA is able to be utilized in a number methods that traditionally have used RNA or DNA. Often PNA sequences perform better in techniques than the corresponding RNA or DNA sequences and have utilities that are not inherent to RNA or DNA. An excellent review of PNA including methods of making, characteristics of, and methods of using, is provided by Corey (1997) and is incoφorated herein by reference. As such, in certain embodiments, one may prepare PNA sequences that are complementary to one or more portions of the ACE mRNA sequence, and such PNA compositions may be used to regulate, alter, decrease, or reduce the translation of ACE- specific mRNA, and thereby alter the level of ACE activity in a host cell to which such PNA compositions have been administered. PNAs have 2-aminoethyl-glycine linkages replacing the normal phosphodiester backbone of DNA (Nielsen et al, 1991; Hanvey et al, 1992; Hyrup and Nielsen, 1996; Neilsen, 1996). This chemistry has three important consequences: firstly, in contrast to DNA or phosphorothioate oligonucleotides, PNAs are neutral molecules; secondly, PNAs are achiral, which avoids the need to develop a stereoselective synthesis; and thirdly, PNA synthesis uses standard Boc (Dueholm et al, 1994) or Fmoc (Thomson et al, 1995) protocols for solid-phase peptide synthesis, although other methods, including a modified Merrifield method, have been used (Christensen et al, 1995). PNA monomers or ready-made oligomers are commercially available from PerSeptive Biosystems (Framingham, MA, USA). PNA syntheses by either Boc or Fmoc protocols are straightforward using manual or automated protocols (Norton et al, 1995). The manual protocol lends itself to the production of chemically modified PNAs or the simultaneous synthesis of families of closely related PNAs. As with peptide synthesis, the success of a particular PNA synthesis will depend on the properties ofthe chosen sequence. For example, while in theory PNAs can incoφorate any combination of nucleotide bases, the presence of adjacent purines can lead to deletions of one or more residues in the product. In expectation of this difficulty, it is suggested that, in producing PNAs with adjacent purines, one should repeat the coupling of residues likely to be added inefficiently. This should be followed by the purification of PNAs by reverse-phase high-pressure liquid chromatography (Norton et al, 1995) providing yields and purity of product similar to those observed during the synthesis of peptides. Modifications of PNAs for a given application may be accomplished by coupling amino acids during solid-phase synthesis or by attaching compounds that contain a carboxylic acid group to the exposed N-terminal amine. Alternatively, PNAs can be modified after synthesis by coupling to an introduced lysine or cysteine. The ease with which PNAs can be modified facilitates optimization for better solubility or for specific functional requirements. Once synthesized, the identity of PNAs and their derivatives can be confirmed by mass spectrometry. Several studies have made and utilized modifications of PNAs (Norton et al, 1995; Haaima et al, 1996; Stetsenko et al, 1996; Petersen et al, 1995; Ulmann et al, 1996; Koch et al, 1995; Orum et al, 1995; Footer et al, 1996; Griffith et al, 1995; Kremsky et al, 1996; Pardridge et al, 1995; Boffa et al, 1995; Landsdoφ et al, 1996; Gambacorti-Passerini et al, 1996; Armitage et al, 1997; Seeger et al, 1997; Ruskowski et al, 1997). United States Patent No. 5,700,922 discusses PNA-DNA-PNA chimeric molecules and their uses in diagnostics, modulating protein in organisms, and treatment of conditions susceptible to therapeutics. In contrast to DNA and RNA, which contain negatively charged linkages, the PNA backbone is neutral, i spite of this dramatic alteration, PNAs recognize complementary DNA and RNA by Watson-Crick pairing (Egholm et al. , 1993), validating the initial modeling by Nielsen et al. (1991). PNAs lack 3' to 5' polarity and can bind in either parallel or antiparallel fashion, with the antiparallel mode being preferred (Egholm et α/., 1993). Hybridization of DNA oligonucleotides to DNA and RNA is destabilized by electrostatic repulsion between the negatively charged phosphate backbones of the complementary strands. By contrast, the absence of charge repulsion in PNA-DNA or PNA-RNA duplexes increases the melting temperature (T m ) and reduces the dependence of T m on the concentration of mono- or divalent cations (Nielsen et al, 1991). The enhanced rate and affinity of hybridization are significant because they are responsible for the suφrising ability of PNAs to perform strand invasion of complementary sequences within relaxed double-stranded DNA. In addition, the efficient hybridization at inverted repeats suggests that PNAs can recognize secondary structure effectively within double- stranded DNA. Enhanced recognition also occurs with PNAs immobilized on surfaces, and Wang et al. have shown that support-bound PNAs can be used to detect hybridization events (Wang et al, 1996). One might expect that tight binding of PNAs to complementary sequences would also increase binding to similar (but not identical) sequences, reducing the sequence specificity of PNA recognition. As with DNA hybridization, however, selective recognition can be achieved by balancing oligomer length and incubation temperature. Moreover, selective hybridization of PNAs is encouraged by PNA-DNA hybridization being less tolerant of base mismatches than DNA-DNA hybridization. For example, a single mismatch within a 16 bp PNA-DNA duplex can reduce the T m by up to 15°C (Egholm et al, 1993). This high level of discrimination has allowed the development of several PNA-based strategies for the analysis of point mutations (Wang et al, 1996; Carisson et al, 1996; Thiede et al, 1996; Webb and Hurskainen, 1996; Perry-O'Keefe et al, 1996). High-affinity binding provides clear advantages for molecular recognition and the development of new applications for PNAs. For example, 11-13 nucleotide PNAs inhibit the activity of telomerase, a ribonucleo-protein that extends telomere ends using an essential RNA template, while the analogous DNA oligomers do not (Norton et al, 1996). Neutral PNAs are more hydrophobic than analogous DNA oligomers, and this can lead to difficulty solubilizing them at neutral pH, especially if the PNAs have a high purine content or if they have the potential to form secondaiy structures. Their solubility can be enhanced by attaching one or more positive charges to the PNA termini (Nielsen et al, 1991). Findings by Allfrey and colleagues suggest that strand invasion will occur spontaneously at sequences within chromosomal DNA (Boffa et al, 1995; Boffa et al, 1996). These studies targeted PNAs to triplet repeats ofthe nucleotides CAG and used this recognition to purify transcriptionally active DNA (Boffa et al, 1995) and to inhibit transcription (Boffa et al, 1996). This result suggests that if PNAs can be delivered within cells then they will have the potential to be general sequence-specific regulators of gene expression. Studies and reviews concerning the use of PNAs as antisense and anti-gene agents include Nielsen et al. (1993b), Hanvey et al. (1992), and Good and Nielsen (1997). Koppelhus et al. (1997) have used PNAs to inhibit HTV-1 inverse transcription, showing that PNAs may be used for antiviral therapies. Methods of characterizing the antisense binding properties of PNAs are discussed in Rose (1993) and Jensen et al. (1997). Rose uses capillary gel electrophoresis to determine binding of PNAs to their complementary oligonucleotide, measuring the relative binding kinetics and stoicliiometry. Similar types of measurements were made by Jensen et al. using BIAcore™ technology. Other applications of PNAs include use in DNA strand invasion (Nielsen et al, 1991), antisense inhibition (Hanvey et al, 1992), mutational analysis (Orum et al, 1993), enhancers of transcription (MoUegaard et al, 1994), nucleic acid purification (Orum et al, 1995), isolation of transcriptionally active genes (Boffa et al, 1995), blocking of transcription factor binding (Vickers et al, 1995), genome cleavage (Veselkov et al, 1996), biosensors (Wang et al, 1996), in situ hybridization (Thisted et al, 1996), and in a alternative to Southern blotting (Perry-O'Keefe, 1996). POLYPEPTIDE COMPOSITIONS As used herein, the term "polypeptide" " is used in its conventional meaning, i.e., as a sequence of amino acids. The polypeptides are not limited to a specific length of the product; thus, peptides, oligopeptides, and proteins are included within the definition of polypeptide, and such terms may be used interchangeably herein unless specifically indicated otherwise. This term also does not refer to or exclude post-expression modifications of the polypeptide, for example, glycosylations, acetylations, phosphorylations and the like, as well as other modifications known in the art, both naturally occurring and non-naturally occurring. A polypeptide may be an entire protein, or a subsequence thereof. Particular polypeptides of interest in the context of this invention are amino acid subsequences comprising epitopes, i.e., antigenic determinants substantially responsible for the immunogenic properties of a polypeptide and being capable of evoking an immune response. Generally, a polypeptide of the invention will be an isolated polypeptide (or an epitope, variant, or active fragment thereof) derived from a mammalian species. In one preferred embodiment, the polypeptide is encoded within a polynucleotide sequence disclosed herein, i.e., in SEQ ID NOs: 1-299, or a sequence which hybridizes under moderately stringent conditions to such a polynucleotide sequence. Illustratively, the polypeptide composition of the invention is selected from among the group consisting of SEQ ID NOs:300-29,212. ' In the present invention, a polypeptide composition is also understood to comprise one or more polypeptides that are immunologically reactive with antibodies generated against a polypeptide ofthe invention, particularly a polypeptide encoded by one or more of SEQ ID NOs: 1-299, or a polypeptide having a sequence set forth in any one of SEQ ID NOs: 300-29,212, or to active fragments, or to variants or biological functional equivalents thereof. Likewise, a polypeptide composition of the present invention is understood to comprise one or more polypeptides that are capable of eliciting antibodies that are immunologically reactive with one or more polypeptides encoded by one or more contiguous nucleic acid sequences contained in SEQ ID NOs: 1-299, or a polypeptide having a sequence set forth in any one of SEQ ID NOs: 300-29,212, or to active fragments, or to strain variants thereof, or to one or more nucleic acid sequences which hybridize to one or more of these sequences under conditions of moderate to high stringency. As used herein, an active fragment of a polypeptide includes a whole or a portion of a polypeptide which is modified by conventional techniques, e.g., mutagenesis, or by addition, deletion, or substitution, but which active fragment exhibits substantially the same structure function, antigenicity, etc., as a native polypeptide as described herein. In certain illustrative embodiments, the polypeptides of the invention will comprise at least an immunogenic portion of a Propiombacterium acnes protein or a variant thereof, as described herein. Proteins that are Propiombacterium acnes proteins also react detectably within an immunoassay (such as an ELISA) with antisera from a patient infected with Propiombacterium acnes . Polypeptides as described herein may be of any length. Additional sequences derived from the native protein and/or heterologous sequences may be present, and such sequences may (but need not) possess further immunogenic or antigenic properties. An "immunogenic portion," as used herein is a portion of a protein that is recognized (i.e., specifically bound) by a B-cell and/or T-cell surface antigen receptor. Such immunogenic portions generally comprise at least 5 amino acid residues, more preferably at least 10, and still more preferably at least 20 amino acid residues of a Propiombacterium acnes protein or a variant thereof. Certain preferred immunogenic portions include peptides in which an N-terminal leader sequence and/or transmembrane domain have been deleted. Other preferred immunogenic portions may contain a small N- and/or C-terminal deletion (e.g., 1-30 amino acids, preferably 5-15 amino acids), relative to the mature protein. Immunogenic portions may generally be identified using well known techniques, such as those summarized in Paul, Fundamental Immunology, 3rd ed., 243- 247 (Raven Press, 1993) and references cited therein. Such techniques include screening polypeptides for the ability to react with antigen-specific antibodies, antisera and/or T-cell lines or clones. As used herein, antisera and antibodies are "antigen- specific" if they specifically bind to an antigen (i.e., they react with the protein in an ELISA or other immunoassay, and do not react detectably with unrelated proteins). Such antisera and antibodies may be prepared as described herein, and using well known techniques. An immunogenic portion of a native Propiombacterium acnes protein is a portion that reacts with such antisera and/or T-cells at a level that is not substantially less than the reactivity of the full length polypeptide (e.g., in an ELISA and/or T-cell reactivity assay). Such immunogenic portions may react within such assays at a level that is similar to or greater than the reactivity of the full length polypeptide. Such screens may generally be performed using methods well known to those of ordinary skill in the art, such as those described in Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, 1988. For example, a polypeptide may be immobilized on a solid support and contacted with patient sera to allow binding of antibodies within the sera to the immobilized polypeptide. Unbound sera may then be removed and bound antibodies detected using, for example, I- labeled Protein A. In one preferred embodiment, an immunogenic portion of a polypeptide ofthe present invention is a portion that reacts with antisera and/or T-cells at a level that is not substantially less than the reactivity of the full-length polypeptide (e.g., in an ELISA and/or T-cell reactivity assay). Preferably, the level of immunogenic activity of the immunogenic portion is at least about 50%, preferably at least about 70% and most preferably greater than about 90% of the immunogenicity for the full-length polypeptide. In some instances, preferred immunogenic portions will be identified that have a level of immunogenic activity greater than that of the corresponding full-length polypeptide, e.g., having greater than about 100% or 150% or more immunogenic activity. As noted above, a composition may comprise a variant of a native Propiombacterium acnes protein. A polypeptide "variant," as used herein, is a polypeptide that differs from a native Propiombacterium acnes protein in that it will generally have less than five, preferably less than 10 and more preferably less than 25 substitutions, deletions, additions and/or insertions relative to the native polypeptide, such that the immunogenicity ofthe polypeptide variant is not substantially diminished. In other words, the ability of a variant to react with antigen-specific antisera may be enhanced or unchanged, relative to the native protein, or may be diminished by less than 50%, and preferably less than 20%, relative to the native protein. Such variants may generally be identified by modifying one of the above polypeptide sequences and evaluating the reactivity ofthe modified polypeptide with antigen-specific antibodies or antisera as described herein. Preferred variants include those in which one or more portions, such as an N-terminal leader sequence or transmembrane domain, have been removed. Other preferred variants include variants in which a small portion (e.g., 1-30 amino acids, preferably 5-15 amino acids) has been removed from the N- and/or C- terminal ofthe mature protein. In one preferred embodiment, the polypeptide fragments and variants provided by the present invention are immunologically reactive with an antibody and/or T-cell that reacts with a full-length R acnes polypeptide specifically set forth herein. In another preferred embodiment, the polypeptide fragments and variants provided by the present invention exhibit a level of immunogenic activity of at least about 50%), preferably at least about 10%, and most preferably at least about 90% or more of that exhibited by a full-length R acnes polypeptide sequence specifically set forth herein. Polypeptide variants encompassed by the present invention include those exhibiting at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% or more identity (determined as described above) to the polypeptides disclosed herein. Preferably, a variant contains conservative substitutions. A "conservative substitution" is one in which an amino acid is substituted for another amino acid that has similar properties, such that one skilled in the art of peptide chemistry would expect the secondary structure and hydropathic nature of the polypeptide to be substantially unchanged. Amino acid substitutions may generally be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or the amphipathic nature of the residues. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; and amino acids with uncharged polar head groups having similar hydrophilicity values include leucine, isoleucine and valine; glycine and alanine; asparagine and glutamine; and serine, threonine, phenylalanine and tyrosine. Other groups of amino acids that may represent conservative changes include: (1) ala, pro, gly, glu, asp, gin, asn, ser, thr; (2) cys, ser, tyr, thr; (3) val, ile, leu, met, ala, phe; (4) lys, arg, his; and (5) phe, tyr, tip, his. A variant may also, or alternatively, contain nonconservative changes. In a preferred embodiment, variant polypeptides differ from a native sequence by substitution, deletion or addition of five amino acids or fewer. Variants may also (or alternatively) be modified by, for example, the deletion or addition of amino acids that have minimal influence on the immunogenicity, secondary structure and hydropathic nature ofthe polypeptide. As noted above, polypeptides may comprise a signal (or leader) sequence at the N-terminal end of the protein, which co-translationally or post- translationally directs transfer of the protein. The polypeptide may also be conjugated to a linker or other sequence for ease of synthesis, purification or identification of the polypeptide (e.g., poly-His), or to enhance binding ofthe polypeptide to a solid support. For example, a polypeptide may be conjugated to an immunoglobulin Fc region. Polypeptides may be prepared using any of a variety of well known techniques. Recombinant polypeptides encoded by DNA sequences as described above may be readily prepared from the DNA sequences using any of a variety of expression vectors known to those of ordinary skill in the art. Expression may be achieved in any appropriate host cell that has been transformed or transfected with an expression vector containing a DNA molecule that encodes a recombinant polypeptide. Suitable host cells include prokaryotes, yeast, and higher eukaryotic cells, such as mammalian cells and plant cells. Preferably, the host cells employed are E. coli, yeast or a mammalian cell line such as COS or CHO. Supematants from suitable host/vector systems which secrete recombinant protein or polypeptide into culture media may be first concentrated using a commercially available filter. Following concentration, the concentrate may be applied to a suitable purification matrix such as an affinity matrix or an ion exchange resin. Finally, one or more reverse phase HPLC steps can be employed to further purify a recombinant polypeptide. Portions and other variants having less than about 100 amino acids, and generally less than about 50 amino acids, may also be generated by synthetic means, using techniques well known to those of ordinary skill in the art. For example, such polypeptides may be synthesized using any of the commercially available solid-phase techniques, such as the Merrifield solid-phase synthesis method, where amino acids are sequentially added to a growing amino acid chain. See Merrifield, J. Am. Chem. Soc. 55:2149-2146, 1963. Equipment for automated synthesis of polypeptides is commercially available from suppliers such as Perkin Elmer/ Applied Bio Systems Division (Foster City, CA), and may be operated according to the manufacturer's instructions. Within certain specific embodiments, a polypeptide may be a fusion protein that comprises multiple polypeptides as described herein, or that comprises at least one polypeptide as described herein and an unrelated sequence, such as a known protein. A fusion partner may, for example, assist in providing T helper epitopes (an immunological fusion partner), preferably T helper epitopes recognized by humans, or may assist in expressing the protein (an expression enhancer) at higher yields than the native recombinant protein. Certain preferred fusion partners are both immunological and expression enhancing fusion partners. Other fusion partners may be selected so as to increase the solubility ofthe protein or to enable the protein to be targeted to desired intracellular compartments. Still further fusion partners include affinity tags, which facilitate purification ofthe protein. Fusion proteins may generally be prepared using standard techniques, including chemical conjugation. Preferably, a fusion protein is expressed as a recombinant protein, allowing the production of increased levels, relative to a non-fused protein, in an expression system. Briefly, DNA sequences encoding the polypeptide components may be assembled separately, and ligated into an appropriate expression vector. The 3' end of the DNA sequence encoding one polypeptide component is ligated, with or without a peptide linker, to the 5' end of a DNA sequence encoding the second polypeptide component so that the reading frames ofthe sequences are in phase. This permits translation into a single fusion protein that retains the biological activity of both component polypeptides. A peptide linker sequence may be employed to separate the first and second polypeptide components by a distance sufficient to ensure that each polypeptide folds into its secondary and tertiary structures. Such a peptide linker sequence is incoφorated into the fusion protein using standard techniques well known in the art. Suitable peptide linker sequences may be chosen based on the following factors: (1) their ability to adopt a flexible extended conformation; (2) their inability to adopt a secondary structure that could interact with functional epitopes on the first and second polypeptides; and (3) the lack of hydrophobic or charged residues that might react with the polypeptide functional epitopes. Preferred peptide linker sequences contain Gly, Asn and Ser residues. Other near neutral amino acids, such as Thr and Ala may also be used in the linker sequence. Amino acid sequences which may be usefully employed as linkers include those disclosed in Maratea et al., Gene 40:39-46, 1985; Muφhy et al., Proc. Natl. Acad. Sci. USA 53:8258-8262, 1986; U.S. Patent No. 4,935,233 and U.S. Patent No. 4,751,180. The linker sequence may generally be from 1 to about 50 amino acids in length. Linker sequences are not required when the first and second polypeptides have non-essential N-terminal amino acid regions that can be used to separate the functional domains and prevent steric interference. The ligated DNA sequences are operably linked to suitable franscriptional or translational regulatory elements. The regulatory elements responsible for expression of DNA are located only 5' to the DNA sequence encoding the first polypeptides. Similarly, stop codons required to end translation and transcription termination signals are only present 3' to the DNA sequence encoding the second polypeptide. Fusion proteins are also provided. Such proteins comprise a polypeptide as described herein together with an unrelated immunogenic protein. Preferably the immunogenic protein is capable of eliciting a recall response. Examples of such proteins include tetanus, tuberculosis and hepatitis proteins (see, for example, Stoute et al. New Engl. J. Med., 336:86-91, 1997). Within preferred embodiments, an immunological fusion partner is derived from protein D, a surface protein of the gram-negative bacterium Haemophilus influenza B (WO 91/18926). Preferably, a protein D derivative comprises approximately the first third of the protein (e.g., the first N-terminal 100-110 amino acids), and a protein D derivative may be lipidated. Within certain preferred embodiments, the first 109 residues of a Lipoprotein D fusion partner is included on the N-terminus to provide the polypeptide with additional exogenous T-cell epitopes and to increase the expression level in E. coli (thus functioning as an expression enhancer). The lipid tail ensures optimal presentation of the antigen to antigen presenting cells. Other fusion partners include the non-structural protein from influenzae virus, NSl (hemaglutinin). Typically, the N-terminal 81 amino acids are used, although different fragments that include T-helper epitopes may be used. In another embodiment, the immunological fusion partner is the protein known as LYTA, or a portion thereof (preferably a C-terminal portion). LYTA is derived from Streptococcus pneumoniae, which synthesizes an N-acetyl-L-alanine amidase known as amidase LYTA (encoded by the LytA gene; Gene 43:265-292, 1986). LYTA is an autolysin that specifically degrades certain bonds in the peptidoglycan backbone. The C-terminal domain ofthe LYTA protein is responsible for the affinity to the choline or to some choline analogues such as DEAE. This property has been exploited for the development of E. coli C-LYTA expressing plasmids useful for expression of fusion proteins. Purification of hybrid proteins containing the C-LYTA fragment at the amino terminus has been described (see Biotechnology 10:195-198, 1992). Within a preferred embodiment, a repeat portion of LYTA may be incoφorated into a fusion protein. A repeat portion is found in the C-terminal region starting at residue 178. A particularly preferred repeat portion incoφorates residues 188-305. In general, polypeptides (including fusion proteins) and polynucleotides as described herein are isolated. An "isolated" polypeptide or polynucleotide is one that is removed from its original environment. For example, a naturally-occurring protein is isolated if it is separated from some or all of the coexisting materials in the natural system. Preferably, such polypeptides are at least about 90% pure, more preferably at least about 95% pure and most preferably at least about 99% pure. A polynucleotide is considered to be isolated if, for example, it is cloned into a vector that is not a part ofthe natural environment. BINDING AGENTS The present invention further provides agents, such as antibodies and antigen-binding fragments thereof, that specifically bind to a Propiombacterium acnes protein. As used herein, an antibody, or antigen-binding fragment thereof, is said to "specifically bind" to a Propiombacterium acnes protein if it reacts at a detectable level (within, for example, an ELISA) with a Propiombacterium acnes protein, and does not react detectably with unrelated proteins under similar conditions. As used herein, "binding" refers to a noncovalent association between two separate molecules such that a complex is formed. The ability to bind may be evaluated by, for example, determining a binding constant for the formation ofthe complex. The binding constant is the value obtained when the concentration of the complex is divided by the product ofthe component concentrations. In general, two compounds are said to "bind," in the context of the present invention, when the binding constant for complex formation exceeds about 10 3 L/mol. The binding constant may be determined using methods well known in the art. Binding agents may be further capable of differentiating between patients with and without Propiombacterium acnes using the representative assays provided herein. In other words, antibodies or other binding agents that bind to a Propiombacterium acnes protein will generate a signal indicating its presence in at least about 20% of patients with the disease, and will generate a negative signal indicating the absence of the disease in at least about 90% of individuals without the disease. To determine whether a binding agent satisfies this requirement, biological samples (e.g., blood, sera, sputum and/or urine) from patients with and without acne (as determined using standard clinical tests) may be assayed as described herein for the presence of polypeptides that bind to the binding agent. It will be apparent that a statistically significant number of samples with and without the disease should be assayed. Each binding agent should satisfy the above criteria; however, those of ordinary skill in the art will recognize that binding agents may be used in combination to improve sensitivity. Any agent that satisfies the above requirements may be a binding agent. For example, a binding agent may be a ribosome, with or without a peptide component, an RNA molecule or a polypeptide. In a preferred embodiment, a binding agent is an antibody or an antigen-binding fragment thereof. Antibodies may be prepared by any of a variety of techniques known to those of ordinary skill in the art. See, e.g., Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, 1988. In general, antibodies can be produced by cell culture techniques, including the generation of monoclonal antibodies as described herein, or via transfection of antibody genes into suitable bacterial or mammalian cell hosts, in order to allow for the production of recombinant antibodies. In one technique, an immunogen comprising the polypeptide is initially injected into any of a wide variety of mammals (e.g., mice, rats, rabbits, sheep or goats). In this step, the polypeptides of this invention may serve as the immunogen without modification. Alternatively, particularly for relatively short polypeptides, a superior immune response may be elicited if the polypeptide is joined to a carrier protein, such as bovine serum albumin or keyhole limpet hemocyanin. The immunogen is injected into the animal host, preferably according to a predetermined schedule incoφorating one or more booster immunizations, and the animals are bled periodically. Polyclonal antibodies specific for the polypeptide may then be purified from such antisera by, for example, affinity chromatography using the polypeptide coupled to a suitable solid support. Monoclonal antibodies specific for an antigenic polypeptide of interest may be prepared, for example, using the technique of Kohler and Milstein, Eur. J. Immunol (5:511-519, 1976, and improvements thereto. Briefly, these methods involve the preparation of immortal cell lines capable of producing antibodies having the desired specificity (i.e., reactivity with the polypeptide of interest). Such cell lines may be produced, for example, from spleen cells obtained from an animal immunized as described above. The spleen cells are then immortalized by, for example, fusion with a myeloma cell fusion partner, preferably one that is syngeneic with the immunized animal. A variety of fusion techniques may be employed. For example, the spleen cells and myeloma cells may be combined with a nonionic detergent for a few minutes and then plated at low density on a selective medium that supports the growth of hybrid cells, but not myeloma cells. A preferred selection technique uses HAT (hypoxanthine, aminopterin, thymidine) selection. After a sufficient time, usually about 1 to 2 weeks, colonies of hybrids are observed. Single colonies are selected and their culture supematants tested for binding activity against the polypeptide. Hybridomas having high reactivity and specificity are preferred. Monoclonal antibodies may be isolated from the supematants of growing hybridoma colonies. In addition, various techniques may be employed to enhance the yield, such as injection ofthe hybridoma cell line into the peritoneal cavity of a suitable vertebrate host, such as a mouse. Monoclonal antibodies may then be harvested from the ascites fluid or the blood. Contaminants may be removed from the antibodies by conventional techniques, such as chromatography, gel filtration, precipitation, and extraction. The polypeptides of this invention may be used in the purification process in, for example, an affinity chromatography step. Within certain embodiments, the use of antigen-binding fragments of antibodies may be preferred. Such fragments include Fab fragments, which may be prepared using standard teclmiques. Briefly, immunoglobulins may be purified from rabbit serum by affinity chromatography on Protein A bead columns (Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, 1988) and digested by papain to yield Fab and Fc fragments. The Fab and Fc fragments may be separated by affinity chromatography on protein A bead columns. Monoclonal antibodies ofthe present invention may be coupled to one or more therapeutic agents. Suitable agents in this regard include radionuclides, differentiation inducers, drugs, toxins, and derivatives thereof. Preferred radionuclides include 90 Y, 123 I, 125 I, 131 I, 186 Re, I88 Re, 21I At, and 212 Bi. Preferred drugs include methotrexate, and pyrimidine and purine analogs. Preferred differentiation inducers include phorbol esters and butyric acid. Preferred toxins include ricin, abrin, diptheria toxin, cholera toxin, gelonin, Pseudomonas exotoxin, Shigella toxin, and pokeweed antiviral protein. A therapeutic agent may be coupled (e.g., covalently bonded) to a suitable monoclonal antibody either directly or indirectly (e.g., via a linker group). A direct reaction between an agent and an antibody is possible when each possesses a substituent capable of reacting with the other. For example, a nucleophilic group, such as an amino or sulfhydryl group, on one may be capable of reacting with a carbonyl- containing group, such as an anhydride or an acid halide, or with an alkyl group containing a good leaving group (e.g., a halide) on the other. Alternatively, it may be desirable to couple a therapeutic agent and an antibody via a linker group. A linker group can function as a spacer to distance an antibody from an agent in order to avoid interference with binding capabilities. A linker group can also serve to increase the chemical reactivity of a substituent on an agent or an antibody, and thus increase the coupling efficiency. An increase in chemical reactivity may also facilitate the use of agents, or functional groups on agents, which otherwise would not be possible. It will be evident to those skilled in the art that a variety of bifunctional or polyfunctional reagents, both homo- and hetero-functional (such as those described in the catalog ofthe Pierce Chemical Co., Rockford, IL), may be employed as the linker group. Coupling may be effected, for example, through amino groups, carboxyl groups, sulfhydryl groups or oxidized carbohydrate residues. There are numerous references describing such methodology, e.g., U.S. Patent No. 4,671,958, to Rodwell et al. Where a therapeutic agent is more potent when free from the antibody portion of the immunoconjugates of the present invention, it may be desirable to use a linker group which is cleavable during or upon intemalization into a cell. A number of different cleavable linker groups have been described. The mechanisms for the intracellular release of an agent from these linker groups include cleavage by reduction of a disulfide bond (e.g., U.S. Patent No. 4,489,710, to Spitler), by irradiation of a photolabile bond (e.g., U.S. Patent No. 4,625,014, to Senter et al.), by hydrolysis of derivatized amino acid side chains (e.g., U.S. Patent No. 4,638,045, to Kohn et al.), by serum complement-mediated hydrolysis (e.g., U.S. Patent No. 4,671,958, to Rodwell et al.), and acid-catalyzed hydrolysis (e.g., U.S. Patent No. 4,569,789, to Blattler et al.). It may be desirable to couple more than one agent to an antibody. In one embodiment, multiple molecules of an agent are coupled to one antibody molecule. In another embodiment, more than one type of agent may be coupled to one antibody. Regardless of the particular embodiment, immunoconjugates with more than one agent may be prepared in a variety of ways. For example, more than one agent may be coupled directly to an antibody molecule, or linkers that provide multiple sites for attachment can be used. Alternatively, a carrier can be used. A carrier may bear the agents in a variety of ways, including covalent bonding either directly or via a linker group. Suitable carriers include proteins such as albumins (e.g., U.S. Patent No. 4,507,234, to Kato et al.), peptides and polysaccharides such as aminodextran (e.g., U.S. Patent No. 4,699,784, to Shih et al). A carrier may also bear an agent by noncovalent bonding or by encapsulation, such as within a liposome vesicle (e.g., U.S. Patent Nos. 4,429,008 and 4,873,088). Carriers specific for radionuclide agents include radiohalogenated small molecules and chelating compounds. For example, U.S. Patent No. 4,735,792 discloses representative radiohalogenated small molecules and their synthesis. A radionuclide chelate may be formed from chelating compounds that include those containing nitrogen and sulfur atoms as the donor atoms for binding the metal, or metal oxide, radionuclide. For example, U.S. Patent No. 4,673,562, to Davison et al. discloses representative chelating compounds and their synthesis. A variety of routes of administration for the antibodies and immunoconjugates may be used. It will be evident that the precise dose of the antibody/immunoconjugate will vary depending upon the antibody used, the antigen density, and the rate of clearance ofthe antibody. T CELLS Immunotherapeutic compositions may also, or alternatively, comprise T cells specific for a Propiombacterium acnes protein. Such cells may generally be prepared in vitro or ex vivo, using standard procedures. For example, T cells may be isolated from bone marrow, peripheral blood, or a fraction of bone marrow or peripheral blood of a patient, using a commercially available cell separation system, such as the Isolex™ System, available from Nexell Therapeutics, Inc. (Irvine, CA; see also U.S. Patent No. 5,240,856; U.S. Patent No. 5,215,926; WO 89/06280; WO 91/16116 and WO 92/07243). Alternatively, T cells may be derived from related or unrelated humans, non-human mammals, cell lines or cultures. T cells may be stimulated with a Propiombacterium acnes polypeptide, polynucleotide encoding a Propiombacterium acnes polypeptide and/or an antigen presenting cell (APC) that expresses such a polypeptide. Such stimulation is performed under conditions and for a time sufficient to permit the generation of T cells that are specific for the polypeptide. Preferably, a Propiombacterium acnes polypeptide or polynucleotide is present within a delivery vehicle, such as a microsphere, to facilitate the generation of specific T cells. T cells are considered to be specific for a Propiombacterium acnes polypeptide if the T cells specifically proliferate, secrete cytokines or kill target cells coated with the polypeptide or expressing a gene encoding the polypeptide. T cell specificity may be evaluated using any of a variety of standard techniques. For example, within a chromium release assay or proliferation assay, a stimulation index of more than two fold increase in lysis and/or proliferation, compared to negative controls, indicates T cell specificity. Such assays may be performed, for example, as described in Chen et al., Cancer Res. 54:1065-1070, 1994. Alternatively, detection of the proliferation of T cells may be accomplished by a variety of known techniques. For example, T cell proliferation can be detected by measuring an increased rate of DNA synthesis (e.g., by pulse-labeling cultures of T cells with tritiated thymidine and measuring the amount of tritiated thymidine incoφorated into DNA). Contact with a Propiombacterium acnes polypeptide (100 ng/ml - 100 μg/ml, preferably 200 ng/ml - 25 μg/ml) for 3 - 7 days should result in at least a two fold increase in proliferation ofthe T cells. Contact as described above for 2-3 hours should result in activation of the T cells, as measured using standard cytokine assays in which a two fold increase in the level of cytokine release (e.g., TNF or IFN-γ) is indicative of T cell activation (see Coligan et al., Current Protocols in Immunology, vol. 1, Wiley Interscience (Greene 1998)). T cells that have been activated in response to a Propiombacterium acnes polypeptide, polynucleotide or polypeptide-expressing APC may be CD4 + and/or CD8 . Propiombacterium acnes protein-specific T cells may be expanded using standard techniques. Within preferred embodiments, the T cells are derived from a patient, a related donor or an unrelated donor, and are administered to the patient following stimulation and expansion. For therapeutic puφoses, CD4 + or CD8 + T cells that proliferate in response to a Propiombacterium acnes polypeptide, polynucleotide or APC can be expanded in number either in vitro or in vivo. Proliferation of such T cells in vitro may be accomplished in a variety of ways. For example, the T cells can be re-exposed to a Propiombacterium acnes polypeptide, or a short peptide corresponding to an immunogenic portion of such a polypeptide, with or without the addition of T cell growth factors, such as interleukin-2, and/or stimulator cells that synthesize a Propiombacterium acnes polypeptide. Alternatively, one or more T cells that proliferate in the presence of a Propiombacterium acnes protein can be expanded in number by cloning. Methods for cloning cells are well known in the art, and include limiting dilution. PHARMACEUTICAL COMPOSITIONS In additional embodiments, the present invention concerns formulation of one or more of the polynucleotide, polypeptide, T-cell and/or antibody compositions disclosed herein in pharmaceutically-acceptable solutions for administration to a cell or an animal, either alone, or in combination with one or more other modalities of therapy. It will also be understood that, if desired, the nucleic acid segment, RNA, DNA or PNA compositions that express a polypeptide as disclosed herein may be administered in combination with other agents as well, such as, e.g., other proteins or polypeptides or various pharmaceutically-active agents. In fact, there is virtually no limit to other components that may also be included, given that the additional agents do not cause a significant adverse effect upon contact with the target cells or host tissues. The compositions may thus be delivered along with various ' other agents as required in the particular instance. Such compositions may be purified from host cells or other biological sources, or alternatively may be chemically synthesized as described herein. Likewise, such compositions may further comprise substituted or derivatized RNA or DNA compositions. Formulation of pharmaceutically-acceptable excipients and carrier solutions is well-known to those of skill in the art, as is the development of suitable dosing and treatment regimens for using the particular compositions described herein in a variety of treatment regimens, including e.g., oral, parenteral, intravenous, intranasal, and intramuscular administration and formulation. 1. ORAL DELIVERY In certain applications, the pharmaceutical compositions disclosed herein may be delivered via oral administration to an animal. As such, these compositions may be formulated with an inert diluent or with an assimilable edible carrier, or they may be enclosed in hard- or soft-shell gelatin capsule, or they may be compressed into tablets, or they may be incoφorated directly with the food ofthe diet. The active compounds may even be incoφorated with excipients and used in the form of ingestible tablets, buccal tables, troches, capsules, elixirs, suspensions, syrups, wafers, and the like (Mathiowitz et al, 1997; Hwang et al, 1998; U. S. Patent 5,641,515; U. S. Patent 5,580,579 and U. S. Patent 5,792,451, each specifically incoφorated herein by reference in its entirety). The tablets, troches, pills, capsules and the like may also contain the following: a binder, as gum fragacanth, acacia, cornstarch, or gelatin; excipients, such as dicalcium phosphate; a disintegrating agent, such as com starch, potato starch, alginic acid and the like; a lubricant, such as magnesium stearate; and a sweetening agent, such as sucrose, lactose or saccharin may be added or a flavoring agent, such as peppermint, oil of wintergreen, or cherry flavoring. When the dosage unit foπn is a capsule, it may contain, in addition to materials of the above type, a liquid carrier. Various other materials may be present as coatings or to otherwise modify the physical form of the dosage unit. For instance, tablets, pills, or capsules may be coated with shellac, sugar, or both. A syrup of elixir may contain the active compound sucrose as a sweetening agent methyl and propylparabens as preservatives, a dye and flavoring, such as cherry or orange flavor. Of course, any material used in preparing any dosage unit form should be pharmaceutically pure and substantially non-toxic in the amounts employed. In addition, the active compounds may be incoφorated into sustained-release preparation and formulations. Typically, these formulations may contain at least about 0.1% of the active compound or more, although the percentage of the active ingredient(s) may, of course, be varied and may conveniently be between about 1 or 2% and about 60% or 70% or more ofthe weight or volume ofthe total formulation. Naturally, the amount of active compound(s) in each therapeutically useful composition may be prepared is such a way that a suitable dosage will be obtained in any given unit dose ofthe compound. Factors such as solubility, bioavailability, biological half-life, route of administration, product shelf life, as well as other pharmacological considerations will be contemplated by one skilled in the art of preparing such pharmaceutical formulations, and as such, a variety of dosages and treatment regimens may be desirable. For oral administration the compositions of the present invention may alternatively be incoφorated with one or more excipients in the form of a mouthwash, dentifrice, buccal tablet, oral spray, or sublingual orally-administered formulation. For example, a mouthwash may be prepared incoφorating the active ingredient in the required amount in an appropriate solvent, such as a sodium borate solution (Dobell's Solution). Alternatively, the active ingredient may be incoφorated into an oral solution such as one containing sodium borate, glycerin and potassium bicarbonate, or dispersed in a dentifrice, or added in a therapeutically-effective amount to a composition that may include water, binders, abrasives, flavoring agents, foaming agents, and humectants. Alternatively the compositions may be fashioned into a tablet or solution form that may be placed under the tongue or otherwise dissolved in the mouth. 2. INJECTABLE DELIVERY In certain circumstances it will be desirable to deliver the pharmaceutical compositions disclosed herein parenterally, intravenously, intramuscularly, or even intraperitoneally as described in U. S. Patent 5,543,158; U. S. Patent 5,641,515 and U. S. Patent 5,399,363 (each specifically incoφorated herein by reference in its entirety). Solutions of the active compounds as free base or pharmacologically acceptable salts may be prepared in water suitably mixed with a surfactant, such as hydroxypropylcellulose. Dispersions may also be prepared in glycerol, liquid polyethylene glycols, and mixtures thereof and in oils. Under ordinary conditions of storage and use, these preparations contain a preservative to prevent the growth of microorganisms. The pharmaceutical forms suitable for injectable use include sterile aqueous solutions or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersions (U. S. Patent 5,466,468, specifically incoφorated herein by reference in its entirety). In all cases the form must be sterile and must be fluid to the extent that easy syringability exists. It must be stable under the conditions of manufacture and storage and must be preserved against the contaminating action of microorganisms, such as bacteria and fungi. The carrier can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (e.g., glycerol, propylene glycol, and liquid polyethylene glycol, and the like), suitable mixtures thereof, and/or vegetable oils. Proper fluidity may be maintained, for example, by the use of a coating, such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of surfactants. The prevention of the action of microorganisms can be facilitated by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, sorbic acid, tbimerosal, and the like. In many cases, it will be preferable to include isotonic agents, for example, sugars or sodium chloride. Prolonged absoφtion of the injectable compositions can be brought about by the use in the compositions of agents delaying absoφtion, for example, aluminum monostearate and gelatin. For parenteral administration in an aqueous solution, for example, the solution should be suitably buffered if necessary and the liquid diluent first rendered isotonic with sufficient saline or glucose. These particular aqueous solutions are especially suitable for intravenous, intramuscular, subcutaneous and intraperitoneal administration. In this connection, a sterile aqueous medium that can be employed will be known to those of skill in the art in light ofthe present disclosure. For example, one dosage may be dissolved in 1 ml of isotonic NaCl solution and either added to 1000 ml of hypodermoclysis fluid or injected at the proposed site of infusion, (see for example, "Remington's Pharmaceutical Sciences" 15th Edition, pages 1035-1038 and 1570- 1580). Some variation in dosage will necessarily occur depending on the condition of the subject being treated. The person responsible for administration will, in any event, determine the appropriate dose for the individual subject. Moreover, for human administration, preparations should meet sterility, pyrogenicity, and the general safety and purity standards as required by FDA Office of Biologies standards. Sterile injectable solutions are prepared by incoφorating the active compounds in the required amount in the . appropriate solvent with various of the other ingredients enumerated above, as required, followed by filtered sterilization. Generally, dispersions are prepared by incoφorating the various sterilized active ingredients into a sterile vehicle which contains the basic dispersion medium and the required other ingredients from those enumerated above. In the case of sterile powders for the preparation of sterile injectable solutions, the preferred methods of preparation are vacuum-drying and freeze-drying techniques which yield a powder of the active ingredient plus any additional desired ingredient from a previously sterile-filtered solution thereof. The compositions disclosed herein may be formulated in a neutral or salt form. Pharmaceutically-acceptable salts, include the acid addition salts (formed with the free amino groups of the protein) and which are formed with inorganic acids such as, for example, hydrochloric or phosphoric acids, or such organic acids as acetic, oxalic, tartaric, mandelic, and the like. Salts formed with the free carboxyl groups can also be derived from inorganic bases such as, for example, sodium, potassium, ammonium, calcium, or ferric hydroxides, and such organic bases as isopropylamine, trimethylamine, histidine, procaine and the like. Upon formulation, solutions will be administered in a manner compatible with the dosage formulation and in such amount as is therapeutically effective. The formulations are easily administered in a variety of dosage forms such as injectable solutions, drug-release capsules, and the like. As used herein, "carrier" includes any and all solvents, dispersion media, vehicles, coatings, diluents, antibacterial and antifungal agents, isotonic and absoφtion delaying agents, buffers, carrier solutions, suspensions, colloids, and the like. The use of such media and agents for pharmaceutical active substances is well known in the art. Except insofar as any conventional media or agent is incompatible with the active ingredient, its use in the therapeutic compositions is contemplated. Supplementary active ingredients can also be incoφorated into the compositions. The phrase "pharmaceutically-acceptable" refers to molecular entities and compositions that do not produce an allergic or similar untoward reaction when administered to a human. The preparation of an aqueous composition that contains a protein as an active ingredient is well understood in the art. Typically, such compositions are prepared as injectables, either as liquid solutions or suspensions; solid forms suitable for solution in, or suspension in, liquid prior to injection can also be prepared. The preparation can also be emulsified. 3. NASAL DELIVERY In certain embodiments, the pharmaceutical compositions may be delivered by intranasal sprays, inhalation, and/or other aerosol delivery vehicles. Methods for delivering genes, nucleic acids, and peptide compositions directly to the lungs via nasal aerosol sprays has been described e.g., in U. S. Patent 5,756,353 and U. S. Patent 5,804,212 (each specifically incoφorated herein by reference in its entirety). Likewise, the delivery of drugs using intranasal microparticle resins (Takenaga et al, 1998) and lysophosphatidyl-glycerol compounds (U. S. Patent 5,725,871, specifically incoφorated herein by reference in its entirety) are also well-known in the pharmaceutical arts. Likewise, transmucosal drug delivery in the form of a polytetrafluoroetheylene support matrix is described in U. S. Patent 5,780,045 (specifically incoφorated herein by reference in its entirety). 4. LIPOSOME-, NANOCAPSULE-, AND MICROPARTICLE-MEDIATED DELIVERY In certain embodiments, the inventors contemplate the use of liposomes, nanocapsules, microparticles, microspheres, lipid particles, vesicles, and the like, for the introduction of the compositions of the present invention into suitable host cells. In particular, the compositions ofthe present invention may be formulated for delivery either encapsulated in a lipid particle, a liposome, a vesicle, a nanosphere, or a nanoparticle or the like. Such formulations may be prefened for the introduction of pharmaceutically-acceptable formulations of the nucleic acids or constructs disclosed herein. The formation and use of liposomes is generally known to those of skill in the art (see for example, Couvreur et al, 1911; Couvreur, 1988; Lasic, 1998; which describes the use of liposomes and nanocapsules in the targeted antibiotic therapy for intracellular bacterial infections and diseases). Recently, liposomes were developed with improved serum stability and circulation half-times (Gabizon and Papahadjopoulos, 1988; Allen and Choun, 1987; U. S. Patent 5,741,516, specifically incoφorated herein by reference in its entirety). Further, various methods of liposome and liposome like preparations as potential drug carriers have been reviewed (Takakura, 1998; Chandran et al, 1997; Margalit, 1995; U. S. Patent 5,567,434; U. S. Patent 5,552,157; U. S. Patent 5,565,213; U. S. Patent 5,738,868 and U. S. Patent 5,795,587, each specifically incoφorated herein by reference in its entirety). Liposomes have been used successfully with a number of cell types that are normally resistant to fransfection by other procedures including T cell suspensions, primary hepatocyte cultures and PC 12 cells (Renneisen et al, 1990; Muller et al, 1990). In addition, liposomes are free ofthe DNA length constraints that are typical of viral-based delivery systems. Liposomes have been used effectively to introduce genes, drugs (Heath and Martin, 1986; Heath et al, 1986; Balazsovits et al, 1989; Fresta and Puglisi, 1996), radiotherapeutic agents (Pikul et al, 1987), enzymes (Imaizumi et al, 1990a; Imaizumi et al, 1990b), viruses (Faller and Baltimore, 1984), transcription factors and allosteric effectors (Nicolau and Gersonde, 1979) into a variety of cultured cell lines and animals. In addition, several successful clinical trails examining the effectiveness of liposome-mediated drug delivery have been completed (Lopez- Berestein et al, 1985a; 1985b; Coune, 1988; Sculier et al, 1988). Furthermore, several studies suggest that the use of liposomes is not associated with autoimmune responses, toxicity or gonadal localization after systemic delivery (Mori and Fukatsu, 1992). Liposomes are formed from phospholipids that are dispersed in an aqueous medium and spontaneously form multilamellar concentric bilayer vesicles (also termed multilamellar vesicles (MLVs). MLVs generally have diameters of from 25 nm to 4 μm. Sonication of MLVs results in the formation of small unilamellar vesicles (SUVs) with diameters in the range of 200 to 500 A, containing an aqueous solution in the core. Liposomes bear resemblance to cellular membranes and are contemplated for use in connection with the present invention as carriers for the peptide compositions. They are widely suitable as both water- and lipid-soluble substances can be entrapped, z.e.,in the aqueous spaces and within the bilayer itself, respectively. It is possible that the drug-bearing liposomes may even be employed for site-specific delivery of active agents by selectively modifying the liposomal formulation. In addition to the teachings of Couvreur et al. (1977; 1988), the following information may be utilized in generating liposomal formulations. Phospholipids can form a variety of structures other than liposomes when dispersed in water, depending on the molar ratio of lipid to water. At low ratios the liposome is the preferred structure. The physical characteristics of liposomes depend on pH, ionic strength and the presence of divalent cations. Liposomes can show low permeability to ionic and polar substances, but at elevated temperatures undergo a phase transition which markedly alters their peπneability. The phase transition involves a change from a closely packed, ordered structure, known as the gel state, to a loosely packed, less- ordered structure, known as the fluid state. This occurs at a characteristic phase- transition temperature and results in an increase in permeability to ions, sugars and drugs. In addition to temperature, exposure to proteins can alter the permeability of liposomes. Certain soluble proteins, such as cytochrome c, bind, deform and penetrate the bilayer, thereby causing changes in permeability. Cholesterol inhibits this penetration of proteins, apparently by packing the phospholipids more tightly. It is contemplated that the most useful liposome formations for antibiotic and inhibitor delivery will contain cholesterol. The ability to trap solutes varies between different types of liposomes. For example, MLVs are moderately efficient at trapping solutes, but SUVs are extremely inefficient. SUVs offer the advantage of homogeneity and reproducibility in size distribution, however, and a compromise between size and trapping efficiency is offered by large unilamellar vesicles (LUVs). These are prepared by ether evaporation and are three to four times more efficient at solute entrapment than MLVs. In addition to liposome characteristics, an important determinant in entrapping compounds is the physicochemical properties ofthe compound itself. Polar compounds are trapped in the aqueous spaces and nonpolar compounds bind to the lipid bilayer of the vesicle. Polar compounds are released through permeation or when the bilayer is broken, but nonpolar compounds remain affiliated with the bilayer unless it is disrupted by temperature or exposure to lipoproteins. Both types show maximum efflux rates at the phase transition temperature. Liposomes interact with cells via four different mechanisms: Endocytosis by phagocytic cells ofthe reticuloendothelial system such as macrophages and neutrophils; adsoφtion to the cell surface, either by nonspecific weak hydrophobic or electrostatic forces, or by specific interactions with cell-surface components; fusion with the plasma cell membrane by insertion ofthe lipid bilayer of the liposome into the plasma membrane, with simultaneous release of liposomal contents into the cytoplasm; and by transfer of liposomal lipids to cellular or subcellular membranes, or vice versa, without any association of the liposome contents. It often is difficult to determine which mechanism is operative and more than one may operate at the same time. The fate and disposition of intravenously injected liposomes depend on their physical properties, such as size, fluidity, and surface charge. They may persist in tissues for h or days, depending on their composition, and half lives in the blood range from min to several h. Larger liposomes, such as MLVs and LUVs, are taken up rapidly by phagocytic cells of the reticuloendothelial system, but physiology of the circulatory system restrains the exit of such large species at most sites. They can exit only in places where large openings or pores exist in the capillary endothelium, such as the sinusoids of the liver or spleen. Thus, these organs are the predominate site of uptake. On the other hand, SUVs show a broader tissue distribution but still are sequestered highly in the liver and spleen. In general, this in vivo behavior limits the potential targeting of liposomes to only those organs and tissues accessible to their large size. These include the blood, liver, spleen, bone marrow, and lymphoid organs. Targeting is generally not a limitation in terms of the present invention. However, should specific targeting be desired, methods are available for this to be accomplished. Antibodies may be used to bind to the liposome surface and to direct the antibody and its drug contents to specific antigenic receptors located on a particular cell-type surface. Carbohydrate determinants (glycoprotein or glycolipid cell-surface components that play a role in cell-cell recognition, interaction and adhesion) may also be used as recognition sites as they have potential in directing liposomes to particular cell types. Mostly, it is contemplated that intravenous injection of liposomal preparations would be used, but other routes of administration are also conceivable. Alternatively, the invention provides for pharmaceutically-acceptable nanocapsule formulations of the compositions of the present invention. Nanocapsules can generally entrap compounds in a stable and reproducible way (Henry-Michelland et al, 1987; Quintanar-Guerrero et al, 1998; Douglas et al, 1987). To avoid side effects due to intracellular polymeric overloading, such ultrafine particles (sized around 0.1 μm) should be designed using polymers able to be degraded in vivo. Biodegradable polyalkyl-cyanoacrylate nanoparticles that meet these requirements are contemplated for use in the present invention. Such particles may be are easily made, as described (Couvreur et al, 1980; 1988; zur Muhlen et al, 1998; Zambaux et al. 1998; Pinto- Alphandry et al, 1995 and U. S. Patent 5,145,684, specifically incoφorated herein by reference in its entirety). VACCINES In certain preferred embodiments, pharmaceutical compositions are provided for use as vaccines. The vaccines will generally comprise one or more pharmaceutical compositions, such as those discussed above, in combination with an immunostimulant. An immunostimulant may be any substance that enhances or potentiates an immune response (antibody and/or cell-mediated) to an exogenous antigen. Examples of immunostimulants include adjuvants, biodegradable microspheres (e.g., polylactic galactide) and liposomes (into which the compound is incoφorated; see e.g., Fullerton, U.S. Patent No. 4,235,877). Vaccine preparation is generally described in, for example, M.F. Powell and M.J. Newman, eds., "Vaccine Design (the subunit and adjuvant approach)," Plenum Press (NY, 1995). Pharmaceutical compositions and vaccines within the scope of the present invention may also contain other compounds, which may be biologically active or inactive. For example, one or more immunogenic portions of other antigens may be present, either incoφorated into a fusion polypeptide or as a separate compound, within the composition or vaccine. Illustrative vaccines may contain DNA encoding one or more of the polypeptides as described above, such that the polypeptide is generated in situ. As noted above, the DNA may be present within any of a variety of delivery systems known to those of ordinary skill in the art, including nucleic acid expression systems, bacteria and viral expression systems. Numerous gene delivery techniques are well known in the art, such as those described by Rolland, Crit. Rev. Therap. Drug Carrier Systems 75:143-198, 1998, and references cited therein. Appropriate nucleic acid expression systems contain the necessary DNA sequences for expression in the patient (such as a suitable promoter and terminating signal). Bacterial delivery systems involve the administration of a bacterium (such as Bacillus-Calmette-Guerrin) that expresses an immunogenic portion of the polypeptide on its cell surface or secretes such an epitope. In a preferred embodiment, the DNA may be introduced using a viral expression system (e.g., vaccinia or other pox virus, retrovirus, or adenovirus), which may involve the use of a non-pathogenic (defective), replication competent virus. Suitable systems are disclosed, for example, in Fisher-Hoch et al., Proc. Natl. Acad. Sci. USA 86:311-321, 1989; Flexner et al., Ann. N.Y. Acad. Sci. 569:86-103, 1989; Flexner et al., Vaccine 5:17-21, 1990; U.S. Patent Nos. 4,603,112, 4,769,330, and 5,017,487; WO 89/01973; U.S. Patent No. 4,777,127; GB 2,200,651; EP 0,345,242; WO 91/02805; Berkner, Biotechniques 6:616-621, 1988; Rosenfeld et al, Science 252:431-434, 1991; Kolls et al., Proc. Natl. Acad. Sci. USA 97:215-219, 1994; Kass-Eisler et al., Proc. Natl. Acad. Sci. USA 90:11498-11502, 1993; Guzman et al., Circulation 55:2838-2848, 1993; and Guzman et al., Cir. Res. 73:1202-1201, 1993. Techniques for incoφorating DNA into such expression systems are well known to those of ordinary skill in the art. The DNA may also be "naked," as described, for example, in Ulmer et al., Science 259:1145- 1749, 1993 and reviewed by Cohen, Science 259:1691-1692, 1993. The uptake of naked DNA may be increased by coating the DNA onto biodegradable beads, which are efficiently transported into the cells. It will be apparent that a vaccine may comprise both a polynucleotide and a polypeptide component. Such vaccines may provide for an enhanced immune response. It will be apparent that a vaccine may contain pharmaceutically acceptable salts of the polynucleotides and polypeptides provided herein. Such salts may be prepared from pharmaceutically acceptable non-toxic bases, including organic bases (e.g., salts of primary, secondary and tertiary amines and basic amino acids) and inorganic bases (e.g., sodium, potassium, lithium, ammonium, calcium and magnesium salts). While any suitable carrier known to those of ordinary skill in the art may be employed in the vaccine compositions of this invention, the type of carrier will vary depending on the mode of administration. Compositions of the present invention may be formulated for any appropriate manner of administration, including for example, topical, oral, nasal, intravenous, intracranial, intraperitoneal, subcutaneous or intramuscular administration. For parenteral administration, such as subcutaneous injection, the carrier preferably comprises water, saline, alcohol, a fat, a wax or a buffer. For oral administration, any of the above carriers or a solid carrier, such as mannitol, lactose, starch, magnesium stearate, sodium saccharine, talcum, cellulose, glucose, sucrose, and magnesium carbonate, may be employed. Biodegradable microspheres (e.g., polylactate polyglycolate) may also be employed as carriers for the pharmaceutical compositions of this invention. Suitable biodegradable microspheres are disclosed, for example, in U.S. Patent Nos. 4,897,268; 5,075,109; 5,928,647; 5,811,128; 5,820,883; 5,853,763; 5,814,344 and 5,942,252. One may also employ a carrier comprising the particulate-protein complexes described in U.S. Patent No. 5,928,647, which are capable of inducing a class I-restricted cytotoxic T lymphocyte responses in a host. Such compositions may also comprise buffers (e.g., neutral buffered saline or phosphate buffered saline), carbohydrates (e.g., glucose, mannose, sucrose or dextrans), mannitol, proteins, polypeptides or amino acids such as glycine, antioxidants, bacteriostats, chelating agents such as EDTA or glutathione, adjuvants (e.g., aluminum hydroxide), solutes that render the formulation isotonic, hypotonic or weakly hypertonic with the blood of a recipient, suspending agents, thickening agents and/or preservatives. Alternatively, compositions of the present invention may be formulated as a lyophilizate. Compounds may also be encapsulated within liposomes using well known technology. Any of a variety of immunostimulants may be employed in the vaccines of this invention. For example, one or more adjuvants may be included. Many adjuvants contain a substance designed to protect the antigen from rapid catabolism, such as aluminum hydroxide or mineral oil, and a stimulator of immune responses, such as lipid A, Bortadella pertussis or Mycobacterium tuberculosis derived proteins. Suitable adjuvants are commercially available as, for example, Freund's Incomplete Adjuvant and Complete Adjuvant (Difco Laboratories, Detroit, MI); Merck Adjuvant 65 (Merck and Company, Inc., Rahway, NJ); AS-2 (SmithKline Beecham, Philadelphia, PA); aluminum salts such as aluminum hydroxide gel (alum) or aluminum phosphate; salts of calcium, iron or zinc; an insoluble suspension of acylated tyrosine; acylated sugars; cationically or anionically derivatized polysaccharides; polyphosphazenes; biodegradable microspheres; monophosphoryl lipid A and quil A. Cytokines, such as GM-CSF or interleukin-2, -7, or -12, may also be used as adjuvants. Within certain vaccines provided herein, the adjuvant composition is preferably designed to induce an immune response predominantly ofthe Thl type. High levels of Thl-type cytokines (e.g., IFN-γ, TNFα, IL-2 and IL-12) tend to favor the induction of cell mediated immune responses to an administered antigen. In contrast, high levels of Th2-type cytokines (e.g., IL-4, IL-5, IL-6 and IL-10) tend to favor the induction of humoral immune responses. Following application of a vaccine as provided herein, a patient will support an immune response that includes Thl- and Th2-type responses. Within a preferred embodiment, in which a response is predominantly Thl- type, the level of Thl-type cytokines will increase to a greater extent than the level of Th2-type cytokines. The levels of these cytokines may be readily assessed using standard assays. For a review ofthe families of cytokines, see Mosmann and Coffman, Ann. Rev. Immunol. 7:145-173, 1989. Preferred adjuvants for use in eliciting a predominantly Thl-type response include, for example, a combination of monophosphoryl lipid A, preferably 3- de-O-acylated monophosphoryl lipid A (3D-MPL), together with an aluminum salt. MPL adjuvants are available from Corixa Coφoration (Seattle, WA; see US Patent Nos. 4,436,727; 4,877,611; 4,866,034 and 4,912,094). CpG-containing oligonucleotides (in which the CpG dinucleotide is unmethylated) also induce a predominantly Thl response. Such oligonucleotides are well known and are described, for example, in WO 96/02555, WO 99/33488 and U.S. Patent Nos. 6,008,200 and 5,856,462. Immunostimulatory DNA sequences are also described, for example, by Sato et al., Science 273:352, 1996. Another preferred adjuvant is a saponin, preferably QS21 (Aquila Biopharmaceuticals Inc., Framingham, MA), which may be used alone or in combination with other adjuvants. For example, an enhanced system involves the combination of a monophosphoryl lipid A and saponin derivative, such as the combination of QS21 and 3D-MPL as described in WO 94/00153, or a less reactogenic composition where the QS21 is quenched with cholesterol, as described in WO 96/33739. Other preferred formulations comprise an oil-in-water emulsion and tocopherol. A particularly potent adjuvant formulation involving QS21, 3D-MPL and tocopherol in an oil-in-water emulsion is described in WO 95/17210. Saponin analog adjuvants are described, for example, in U.S. Patent No. 5,977,081. Other preferred adjuvants include Montanide ISA 720 (Seppic, France), SAF (Chiron, California, United States), ISCOMS (CSL), MF-59 (Chiron), the SBAS series of adjuvants (e.g., SBAS-2 or SBAS-4, available from SmithKline Beecham, Rixensart, Belgium), Detox (Corixa, Hamilton, MT), RC-529 (Corixa, Hamilton, MT) and other aminoalkyl glucosaminide 4-phosphates (AGPs), such as those described in pending U.S. Patent Application Serial Nos. 08/853,826 and 09/074,720, the disclosures of which are incoφorated herein by reference in their entireties. Any vaccine provided herein may be prepared using well known methods that result in a combination of antigen, immune response enhancer and a suitable carrier or excipient. The compositions described herein may be administered as part of a sustained release formulation (i.e., a formulation such as a capsule, sponge or gel (composed of polysaccharides, for example) that effects a slow release of compound following administration). Such formulations may generally be prepared using well known technology (see, e.g., Coombes et al, Vaccine 74:1429-1438, 1996) and administered by, for example, oral, rectal or subcutaneous implantation, or by implantation at the desired target site. Sustained-release formulations may contain a polypeptide, polynucleotide or antibody dispersed in a carrier matrix and/or contained within a reservoir surrounded by a rate controlling membrane. Carriers for use within such formulations are biocompatible, and may also be biodegradable; preferably the formulation provides a relatively constant level of active component release. Such carriers include microparticles of poly(lactide-co- glycolide), polyacrylate, latex, starch, cellulose, dextran and the like. Other delayed- release carriers include supramolecular biovectors, which comprise a non-liquid hydrophilic core (e.g., a cross-linked polysaccharide or oligosaccharide) and, optionally, an external layer comprising an amphiphilic compound, such as a phospholipid (see * e.g., U.S. Patent No. 5,151,254 and PCT applications WO 94/20078, WO/94/23701 and WO 96/06638). The amount of active compound contained within a sustained release formulation depends upon the site of implantation, the rate and expected duration of release and the nature ofthe condition to be treated or prevented. Any of a variety of delivery vehicles may be employed within pharmaceutical compositions and vaccines to facilitate production of an antigen- specific immune response that targets Propiombacterium acnes. Delivery vehicles include antigen presenting cells (APCs), such as dendritic cells, macrophages, B cells, monocytes and other cells that may be engineered to be efficient APCs. Such cells may, but need not, be genetically modified to increase the capacity for presenting the antigen, to improve activation and/or maintenance of the T cell response, to have anti- Propiombacterium acnes effects per se and/or to be immunologically compatible with the receiver (i.e., matched HLA haplotype). APCs may generally be isolated from any of a variety of biological fluids and organs, and may be autologous, allogeneic, syngeneic or xenogeneic cells. Certain preferred embodiments of the present invention use dendritic cells or progenitors thereof as antigen-presenting cells. Dendritic cells are highly potent APCs (Banchereau and Steinman, Nature 392:245-251, 1998) and have been shown to be effective as a physiological adjuvant for eliciting prophylactic or therapeutic antitumor immunity (see Timmerman and Levy, Ann. Rev. Med. 50:501-529, 1999). In general, dendritic cells may be identified based on their typical shape (stellate in situ, with marked cytoplasmic processes (dendrites) visible in vitro), their ability to take up, process and present antigens with high efficiency and their ability to activate naive T cell responses. Dendritic cells may, of course, be engineered to express specific cell- surface receptors or ligands that are not commonly found on dendritic cells in vivo or ex vivo, and such modified dendritic cells are contemplated by the present invention. As an alternative to dendritic cells, secreted vesicles antigen-loaded dendritic cells (called exosomes) may be used within a vaccine (see Zitvogel et al., Nature Med. 4:594-600, 1998). Dendritic cells and progenitors may be obtained from peripheral blood, bone marrow, lymph nodes, spleen, skin, umbilical cord blood or any other suitable tissue or fluid. For example, dendritic cells may be differentiated ex vivo by adding a combination of cytokines such as GM-CSF, IL-4, IL-13 and/or TNFα to cultures of monocytes harvested from peripheral blood. Alternatively, CD34 positive cells harvested from peripheral blood, umbilical cord blood or bone marrow may be differentiated into dendritic cells by adding to the culture medium combinations of GM- CSF, IL-3, TNFα, CD40 ligand, LPS, flt3 ligand and/or other compound(s) that induce differentiation, maturation and proliferation of dendritic cells. Dendritic cells are conveniently categorized as "immature" and "mature" cells, which allows a simple way to discriminate between two well characterized phenotypes. However, this nomenclature should not be construed to exclude all possible intermediate stages of differentiation. Immature dendritic cells are characterized as APC with a high capacity for antigen uptake and processing, which correlates with the high expression of Fcγ receptor and mannose receptor. The mature phenotype is typically characterized by a lower expression of these markers, but a high expression of cell surface molecules responsible for T cell activation such as class I and class II MHC, adhesion molecules (e.g., CD54 and CD11) and costimulatory molecules (e.g., CD40, CD80, CD86 and 4-lBB). APCs may generally be transfected with a polynucleotide encoding a Propiombacterium acnes protein (or portion or other variant thereof) such that the Propiombacterium acnes polypeptide, or an immunogenic portion thereof, is expressed on the cell surface. Such transfection may take place ex vivo, and a composition or vaccine comprising such transfected cells may then be used for therapeutic puφoses, as described herein. Alternatively, a gene delivery vehicle that targets a dendritic or other antigen presenting cell may be administered to a patient, resulting in transfection that occurs in vivo. In vivo and ex vivo transfection of dendritic cells, for example, may generally be performed using any methods known in the art, such as those described in WO 97/24447, or the gene gun approach described by Mahvi et al., Immunology and cell Biology 75:456-460, 1997. Antigen loading of dendritic cells may be achieved by incubating dendritic cells or progenitor cells with the Propiombacterium acnes polypeptide, DNA (naked or within a plasmid vector) or RNA; or with antigen- expressing recombinant bacterium or viruses (e.g., vaccinia, fowlpox, adenovirus or lentivirus vectors). Prior to loading, the polypeptide may be covalently conjugated to an immunological partner that provides T cell help (e.g., a carrier molecule). Alternatively, a dendritic cell may be pulsed with a non-conjugated immunological partner, separately or in the presence ofthe polypeptide. Vaccines and pharmaceutical compositions may be presented in unit-dose or multi-dose containers, such as sealed ampoules or vials. Such containers are preferably hermetically sealed to preserve sterility of the formulation until use. In general, formulations may be stored as suspensions, solutions or emulsions in oily or aqueous vehicles. Alternatively, a vaccine or pharmaceutical composition may be stored in a freeze-dried condition requiring only the addition of a sterile liquid carrier immediately prior to use. ACNE THERAPY In further aspects of the present invention, the compositions described herein may be used for immunotherapy of acne. Within such methods, pharmaceutical compositions and vaccines are typically administered to a patient. As used herein, a "patient" refers to any warm-blooded animal, preferably a human. A patient may or may not be afflicted with acne. Accordingly, the above pharmaceutical compositions and vaccines may be used to prevent the development of acne or to treat a patient afflicted with a acne. Acne may be diagnosed using criteria generally accepted in the art. Administration may be by any suitable method but will most typically be oral or topical. Within certain embodiments, immunotherapy may be active immunotherapy, in which treatment relies on the in vivo stimulation of the endogenous host immune system to react against Propiombacterium acnes with the administration of immune response-modifying agents (such as polypeptides and polynucleotides as provided herein). Within other embodiments, immunotherapy may be passive immunotherapy, in which treatment involves the delivery of agents with established Propiombacterium acnes -immune reactivity (such as effector cells or antibodies) that can directly or indirectly mediate therapeutic effects and does not necessarily depend on an intact host immune system. Examples of effector cells include T cells as discussed above, T lymphocytes (such as CD8 + cytotoxic T lymphocytes and CD4 + T-helper lymphocytes), killer cells (such as Natural Killer cells and lymphokine-activated killer cells), B cells and antigen-presenting cells (such as dendritic cells and macrophages) expressing a polypeptide provided herein. T cell receptors and antibody receptors specific for the polypeptides recited herein may be cloned, expressed and transferred into other vectors or effector cells for adoptive immunotherapy. The polypeptides provided herein may also be used to generate antibodies or anti-idiotypic antibodies (as described above and in U.S. Patent No. 4,918,164, for example) for passive immunotherapy. Effector cells may generally be obtained in sufficient quantities for adoptive immunotherapy by growth in vitro, as described herein. Culture conditions for expanding single antigen-specific effector cells to several billion in number with retention of antigen recognition in vivo are well known in the art. Such in vitro culture conditions typically use intermittent stimulation with antigen, often in the presence of cytokines (such as IL-2) and non-dividing feeder cells. As noted above, immunoreactive polypeptides as provided herein may be used to rapidly expand antigen-specific T cell cultures in order to generate a sufficient number of cells for immunotherapy. In particular, antigen-presenting cells, such as dendritic, macrophage, monocyte, fibroblast and or B cells, may be pulsed with immunoreactive polypeptides or transfected with one or more polynucleotides using standard techniques well known in the art. For example, antigen-presenting cells can be transfected with a polynucleotide having a promoter appropriate for increasing expression in a recombinant virus or other expression system. Cultured effector cells for use in therapy must be able to grow and distribute widely, and to survive long term in vivo. Studies have shown that cultured effector cells can be induced to grow in vivo and to survive long term in substantial numbers by repeated stimulation with antigen supplemented with IL-2 (see, for example, Cheever et al., Immunological Reviews 757: 177, 1997). Alternatively, a vector expressing a polypeptide recited herein may be introduced into antigen presenting cells taken from a patient and clonally propagated ex vivo for transplant back into the same patient. Transfected cells may be reintroduced into the patient using any means known in the art, preferably in sterile form by intravenous, intracavitary or intraperitoneal administration. Routes and frequency of administration of the therapeutic compositions described herein, as well as dosage, will vary from individual to individual, and may be readily established using standard techniques. In general, the pharmaceutical compositions and vaccines may be administered by injection (e.g., intracutaneous, intramuscular, intravenous or subcutaneous), intranasally (e.g., by aspiration), orally, sublingually or, preferably, topically. Generally, between 1 and 10 doses may be administered over a 52 week period. For example, 6 doses may be administered, at intervals of 1 month, and booster vaccinations may be given periodically thereafter. Alternate protocols may be appropriate for individual patients. A suitable dose is an amount of a compound that, when administered as described above, is capable of promoting an anti-acne immune response, and is at least 10-50%) above the basal (i.e., untreated) level. Such response can be monitored by measuring the anti- Propionibacterium acnes antibodies in a patient or by vaccine-dependent generation of cytolytic effector cells capable of killing the patient's Propiombacterium acnes cells in vitro. In general, for pharmaceutical compositions and vaccines comprising one or more polypeptides, the amount of each polypeptide present in a dose ranges from about 25 μg to 5 mg per kg of host. Suitable dose sizes will vary with the size ofthe patient, but will typically range from about 0.1 mL to about 5 mL. In general, an appropriate dosage and treatment regimen provides the active compound(s) in an amount sufficient to provide therapeutic and/or prophylactic benefit. Such a response can be monitored by establishing an improved clinical outcome in treated patients as compared to non-treated patients. Increases in preexisting immune responses to a Propiombacterium acnes protein generally correlate with an improved clinical outcome. Such immune responses may generally be evaluated using standard proliferation, cytotoxicity or cytokine assays, which may be performed using samples obtained from a patient before and after treatment. PROPIONIBACTERIUMACNES DETECTION AND DIAGNOSIS In general, Propiombacterium acnes may be detected in a patient based on the presence of one or more Propiombacterium acnes proteins and/or polynucleotides encoding such proteins in a biological sample (for example, blood, sera, sputum and/or urine) obtained from the patient. In other words, such proteins may be used as markers to indicate the presence or absence of Propiombacterium acnes. In addition, such proteins may be useful for the detection of other organisms related to Propiombacterium acnes. The binding agents provided herein generally permit detection of the level of antigen that binds to the agent in the biological sample. Polynucleotide primers and probes may be used to detect the level of mRNA encoding a Propiombacterium acnes protein, which is also indicative ofthe presence or absence of Propiombacterium acnes. There are a variety of assay formats known to those of ordinary skill in the art for using a binding agent to detect polypeptide markers in a sample. See, e.g., Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, 1988. In general, the presence or absence of Propiombacterium acnes in a patient may be determined by (a) contacting a biological sample obtained from a patient with a binding agent; (b) detecting in the sample a level of polypeptide that binds to the binding agent; and (c) comparing the level of polypeptide with a predetermined cut-off value. In a preferred embodiment, the assay involves the use of binding agent immobilized on a solid support to bind to and remove the polypeptide from the remainder of the sample. The bound polypeptide may then be detected using a detection reagent that contains a reporter group and specifically binds to the binding agent/polypeptide complex. Such detection reagents may comprise, for example, a binding agent that specifically binds to the polypeptide or an antibody or other agent that specifically binds to the binding agent, such as an anti-immunoglobulin, protein G, protein A or a lectin. Alternatively, a competitive assay may be utilized, in which a polypeptide is labeled with a reporter group and allowed to bind to the immobilized binding agent after incubation of the binding agent with the sample. The extent to which components of the sample inhibit the binding of the labeled polypeptide to the binding agent is indicative ofthe reactivity ofthe sample with the immobilized binding agent. Suitable polypeptides for use within such assays include full length Propiombacterium acnes proteins and portions thereof to which the binding agent binds, as described above. The solid support may be any material known to those of ordinary skill in the art to which the protein may be attached. For example, the solid support may be a test well in a microtiter plate or a nitrocellulose or other suitable membrane. Alternatively, the support may be a bead or disc, such as glass, fiberglass, latex or a plastic material such as polystyrene or polyvinylchloride. The support may also be a magnetic particle or a fiber optic sensor, such as those disclosed, for example, in U.S. Patent No. 5,359,681. The binding agent may be immobilized on the solid support using a variety of techniques known to those of skill in the art, which are amply described in the patent and scientific literature. In the context of the present invention, the term "immobilization" refers to both noncovalent association, such as adsoφtion, and covalent attachment (which may be a direct linkage between the agent and functional groups on the support or may be a linkage by way of a cross-linking agent). Immobilization by adsoφtion to a well in a microtiter plate or to a membrane is preferred. In such cases, adsoφtion may be achieved by contacting the binding agent, in a suitable buffer, with the solid support for a suitable amount of time. The contact time varies with temperature, but is typically between about 1 hour and about 1 day. In general, contacting a well of a plastic microtiter plate (such as polystyrene or polyvinylchloride) with an amount of binding agent ranging from about 10 ng to about 10 μg, and preferably about 100 ng to about 1 μg, is sufficient to immobilize an adequate amount of binding agent. Covalent attachment of binding agent to a solid support may generally be achieved by first reacting the support with a bifunctional reagent that will react with both the support and a functional group, such as a hydroxyl or amino group, on the binding agent. For example, the binding agent may be covalently attached to supports having an appropriate polymer coating using benzoquinone or by condensation of an aldehyde group on the support with an amine and an active hydrogen on the binding partner (see, e.g., Pierce Immunotechnology Catalog and Handbook, 1991, at A12-A13). In certain embodiments, the assay is a two-antibody sandwich assay. This assay may be performed by first contacting an antibody that has been immobilized on a solid support, commonly the well of a microtiter plate, with the sample, such that polypeptides within the sample are allowed to bind to the immobilized antibody. Unbound sample is then removed from the immobilized polypeptide-antibody complexes and a detection reagent (preferably a second antibody capable of binding to a different site on the polypeptide) containing a reporter group is added. The amount of detection reagent that remains bound to the solid support is then determined using a method appropriate for the specific reporter group. More specifically, once the antibody is immobilized on the support as described above, the remaining protein binding sites on the support are typically blocked. Any suitable blocking agent known to those of ordinary skill in the art, such as bovine serum albumin or Tween 20™ (Sigma Chemical Co., St. Louis, MO). The immobilized antibody is then incubated with the sample, and polypeptide is allowed to bind to the antibody. The sample may be diluted with a suitable diluent, such as phosphate-buffered saline (PBS) prior to incubation. In general, an appropriate contact time (i.e., incubation time) is a period of time that is sufficient to detect the presence of polypeptide within a sample obtained from an individual having Propiombacterium acnes. Preferably, the contact time is sufficient to achieve a level of binding that is at least about 95% of that achieved at equilibrium between bound and unbound polypeptide. Those of ordinary skill in the art will recognize that the time necessary to achieve equilibrium may be readily determined by assaying the level of binding that occurs over a period of time. At room temperature, an incubation time of about 30 minutes is generally sufficient. Unbound sample may then be removed by washing the solid support with an appropriate buffer, such as PBS containing 0.1%) Tween 20™. The second antibody, which contains a reporter group, may then be added to the solid support. Preferred reporter groups include those groups recited above. The detection reagent is then incubated with the immobilized antibody- polypeptide complex for an amount of time sufficient to detect the bound polypeptide. An appropriate amount of time may generally be determined by assaying the level of binding that occurs over a period of time. Unbound detection reagent is then removed and bound detection reagent is detected using the reporter group. The method employed for detecting the reporter group depends upon the nature of the reporter group. For radioactive groups, scintillation counting or autoradiographic methods are generally appropriate. Spectroscopic methods may be used to detect dyes, luminescent groups and fluorescent groups. Biotin may be detected using avidin, coupled to a different reporter group (commonly a radioactive or fluorescent group or an enzyme). Enzyme reporter groups may generally be detected by the addition of substrate (generally for a specific period of time), followed by spectroscopic or other analysis of the reaction products. To determine the presence or absence of Propiombacterium acnes, the signal detected from the reporter group that remains bound to the solid support is generally compared to a signal that corresponds to a predetermined cut-off value. In one embodiment, the cut-off value for the detection of a Propiombacterium acnes is the average mean signal obtained when the immobilized antibody is incubated with samples from patients without Propiombacterium acnes. In one embodiment, a sample generating a signal that is three standard deviations above the predetermined cut-off value is considered positive for the test. In an alternate embodiment, the cut-off value is determined using a Receiver Operator Curve, according to the method of Sackett et al., Clinical Epidemiology: A Basic Science for Clinical Medicine, Little Brown and Co., 1985, p. 106-7. Briefly, in this embodiment, the cut-off value may be determined from a plot of pairs of true positive rates (i.e., sensitivity) and false positive rates (100%- specificity) that correspond to each possible cut-off value for the diagnostic test result. The cut-off value on the plot that is the closest to the upper left-hand comer (i.e., the value that encloses the largest area) is the most accurate cut-off value, and a sample generating a signal that is higher than the cut-off value determined by this method may be considered positive. Alternatively, the cut-off value may be shifted to the left along the plot, to minimize the false positive rate, or to the right, to minimize the false negative rate. In general, a sample generating a signal that is higher than the cut-off value determined by this method is considered positive for Propiombacterium acnes . In a related embodiment, the assay is performed in a flow-through or strip test format, wherein the binding agent is immobilized on a membrane, such as nitrocellulose. In the flow-through test, polypeptides within the sample bind to the immobilized binding agent as the sample passes through the membrane. A second, labeled binding agent then binds to the binding agent-polypeptide complex as a solution containing the second binding agent flows through the membrane. The detection of bound second binding agent may then be performed as described above. In the strip test format, one end of the membrane to which binding agent is bound is immersed in a solution containing the sample. The sample migrates along the membrane through a region containing second binding agent and to the area of immobilized binding agent. Concentration of second binding agent at the area of immobilized antibody indicates the presence of Propiombacterium acnes. Typically, the concentration of second binding agent at that site generates a pattern, such as a line, that can be read visually. The absence of such a pattern indicates a negative result. In general, the amount of binding agent immobilized on the membrane is selected to generate a visually discernible pattern when the biological sample contains a level of polypeptide that would be sufficient to generate a positive signal in the two-antibody sandwich assay, in the format discussed above. Preferred binding agents for use in such assays are antibodies and antigen-binding fragments thereof. Preferably, the amount of antibody immobilized on the membrane ranges from about 25 ng to about lμg, and more preferably from about 50 ng to about 500 ng. Such tests can typically be performed with a very small amount of biological sample. Of course, numerous other assay protocols exist that are suitable for use with the Propiombacterium acnes proteins or binding agents of the present invention. The above descriptions are intended to be exemplary only. For example, it will be apparent to those of ordinary skill in the art that the above protocols may be readily modified to use Propiombacterium acnes polypeptides to detect antibodies that bind to such polypeptides in a biological sample. The detection of such Propiombacterium acnes protein-specific antibodies may correlate with the presence of Propiombacterium acnes. Propiombacterium acnes may also, or alternatively, be detected based on the presence of T cells that specifically react with a Propiombacterium acnes protein in a biological sample. Within certain methods, a biological sample comprising CD4 + and/or CD8 + T cells isolated from a patient is incubated with a Propiombacterium acnes polypeptide, a polynucleotide encoding such a polypeptide and/or an APC that expresses at least an immunogenic portion of such a polypeptide, and the presence or absence of specific activation ofthe T cells is detected. Suitable biological samples include, but are not limited to, isolated T cells. For example, T cells may be isolated from a patient by routine techniques (such as by Ficoll/Hypaque density gradient centrifugation of peripheral blood lymphocytes). T cells may be incubated in vitro for 2-9 days (typically 4 days) at 37°C with polypeptide (e.g., 5 - 25 μg/ml). It may be desirable to incubate another aliquot of a T cell sample in the absence of Propiombacterium acnes polypeptide to serve as a control. For CD4 + T cells, activation is preferably detected by evaluating proliferation of the T cells. For CD8 + T cells, activation is preferably detected by evaluating cytolytic activity. As noted above, Propiombacterium acnes may also, or alternatively, be detected based on the level of mRNA encoding a Propiombacterium acnes protein in a biological sample. For example, at least two oligonucleotide primers may be employed in a polymerase chain reaction (PCR) based assay to amplify a portion of a Propiombacterium acnes cDNA derived from a biological sample, wherein at least one of the oligonucleotide primers is specific for (i.e., hybridizes to) a polynucleotide encoding the Propiombacterium acnes protein. The amplified cDNA is then separated and detected using techniques well known in the art, such as gel electrophoresis. Similarly, oligonucleotide probes that specifically hybridize to a polynucleotide encoding a Propiombacterium acnes protein may be used in a hybridization assay to detect the presence of polynucleotide encoding the Propiombacterium acnes protein in a biological sample. To permit hybridization under assay conditions, oligonucleotide primers and probes should comprise an oligonucleotide sequence that has at least about 60%, preferably at least about 75% and more preferably at least about 90%, identity to a portion of a polynucleotide encoding a Propiombacterium acnes protein that is at least 10 nucleotides, and preferably at least 20 nucleotides, in length. Preferably, oligonucleotide primers and/or probes hybridize to a polynucleotide encoding a polypeptide described herein under moderately stringent conditions, as defined above. Oligonucleotide primers and/or probes which may be usefully employed in the diagnostic methods described herein preferably are at least 10-40 nucleotides in length. In a preferred embodiment, the oligonucleotide primers comprise at least 10 contiguous nucleotides, more preferably at least 15 contiguous nucleotides, of a DNA molecule described herein. Techniques for both PCR based assays and hybridization assays are well known in the art (see, for example, Mullis et al., Cold Spring Harbor Symp. Quant. Biol, 51:263, 1987; Erlich ed., PCR Technology, Stockton Press, NY, 1989). In another embodiment, the compositions described herein may be used as markers for the progression of acne disease by monitoring the presence of Propiombacterium acnes. In this embodiment, assays as described above for detection of Propiombacterium acnes may be performed over time, and the change in the level of reactive polypeptide(s) or polynucleotide(s) evaluated. For example, the assays may be performed every 24-72 hours for a period of 6 months to 1 year, and thereafter performed as needed. Certain in vivo diagnostic assays may be performed directly on a lesion. One such assay involves contacting lesion cells with a binding agent. The bound binding agent may then be detected directly or indirectly via a reporter group. Such binding agents may also be used in histological applications. Alternatively, polynucleotide probes may be used within such applications. As noted above, to improve sensitivity, multiple Propiombacterium acnes protein markers may be assayed within a given sample. It will be apparent that binding agents specific for different proteins provided herein may be combined within a single assay. Further, multiple primers or probes may be used concurrently. The selection of Propiombacterium acnes protein markers may be based on routine experiments to determine combinations that results in optimal sensitivity. In addition, or alternatively, assays for Propiombacterium acnes proteins provided herein may be combined with assays for other known or implicated acne causing proteins. The present invention further provides kits for use within any of the above diagnostic methods. Such kits typically comprise two or more components necessary for performing a diagnostic assay. Components may be compounds, reagents, containers and/or equipment. For example, one container within a kit may contain a monoclonal antibody or fragment thereof that specifically binds to a Propiombacterium acnes protein. Such antibodies or fragments may be provided attached to a support material, as described above. One or more additional containers may enclose elements, such as reagents or buffers, to be used in the assay. Such kits may also, or alternatively, contain a detection reagent as described above that contains a reporter group suitable for direct or indirect detection of antibody binding. Alternatively, a kit may be designed to detect the level of mRNA encoding a Propiombacterium acnes protein in a biological sample. Such kits generally comprise at least one oligonucleotide probe or primer, as described above, that hybridizes to a polynucleotide encoding a Propiombacterium acnes protein. Such an oligonucleotide may be used, for example, within a PCR or hybridization assay. Additional components that may be present within such kits include a second oligonucleotide and/or a diagnostic reagent or container to facilitate the detection of a polynucleotide encoding a Propiombacterium acnes protein. The following Examples are offered by way of illustration and not by way of limitation. EXAMPLES EXAMPLE 1 : IDENTIFICATION OF PROPIOMBACTERIUM ACNES GENOMIC DNA SEQUENCES Propiombacterium acnes (ATCC No. 6919; typed strain) was obtained from ATCC. The lyophilized bacteria was resuspended in 1ml of thioglycollate media and -200 ul transferred to each of several culture tubes containing ~15 ml fluid thioglycollate and incubated at 37°C for 7 to 10 days. Each 15 ml dense culture was subsequently used to seed 500 ml culture volumes of thioglycolate media with little void volume (air space) to allow for anaerobic growth. The cultures were grown at 37°C for ~ 3 weeks or tmtil turbid growth was apparent. P. acnes pellets were harvested by centrifugation and the pellets washed three times with 1 X PBS by multiple resuspension and centrifugation. Final centrifugation was at 10,000 φm and residual liquid was removed. The washed pellets were used to prepare 1) high molecular weight DNA for shotgun DNA cloning and genome sequencing or 2) whole cell lysate for biochemical and immunological evaluation. High molecular weight DNA was prepared as follows: P. acnes pellets were heat inactivated for 20 minutes at 80°C in a water bath followed by enzymatic lysis with a 20mg/ml solution of lysozyme (0.1 Og lysozyme in 5ml TE) in TE (lOmM tris; ImM EDTA) at 37°C for lhr. Subsequently, lOul Prot K (lOmg/ml) and 70ul of 10 % SDS for every 0.5 ml of lysis buffer were added (Step 3 above) and the suspension rocked for ~ 10 minutes at room temperature. This was followed by incubation at 65°C for 15 minutes and the addition of lOOul of a 5M NaCl solution per 500ul of lysis buffer while still at 65°C. Finally, 80 ul of a 10% CTAB solution (lOg CTAB; 14ml 5M NaCl, 86 ml water) was added for every 500 ul lysis buffer and the incubation continued at 65°C for lOmin. Genomic DNA was extracted from the lysed pellets by the addition of an equal volume of phenol and a few drops of chloroform:isoamyl alcohol (24:1), followed by mixing. The homogeneous "white" solution was centrifuged and the aqueous phase re-extracted two more times. This was followed by the addition of 0.6 volume of isopropanol to precipitate the genomic DNA. For the preparation of a genomic library, the high molecular weight DNA was randomly sheared by sonication and fragments with an average size of —1,200 bp were purified and made blunt end by a standard filling process. Insert DNA was ligated into a PUC vector and transformed into E. coli host cells to generate a library of independent clones. DNA was isolated from the individual clones were sequenced from the R acnes genomic library. Overlapping clones representing approximately 8.6 full length genome equivalents were aligned to form 299 linear contigs. Sequences identified in this manner are set forth in SEQ ID NOs: 1-299, and are further identified by contig names and lengths in Table 2 (located in a separate document attached to the application). These 299 contigs represent a total assembled length of about 2,656,860 nucleotides covering more than 90% ofthe P. acnes genome. Using the contig polynucleotide sequences set forth in SEQ ID NOs: 1- 299, 6-frame translation was performed in order to predict open reading frames (ORFs) encoding P. acnes polypeptide sequences greater than equal to 50 amino acid residues in length. The ORF polypeptide sequences resulting from this analysis are set forth in SEQ ID NOs: 300-29,212. These ORFs are further referenced in Table 3 (located in a separate document attached to the application) relative to the DNA contigs from which they originate, the specific nucleotide positions on the contigs that encode the ORFs, and the frame (1, 2 , 3, -1, -2, -3) from which the ORFs are translated. EXAMPLE 2 : IDENTIFICATION OF IMMUNOGENIC COMPONENTS OF P. A CNES Whole cell lysates of P. acnes were prepared by sonication and the total protein content determined by standard analysis. 10 ug each was resolved by standard SDS/PAGE and the resolved species transferred to nitrocellulose for use in the immunological probing with sera. Sera from five donors (1 through 5) with severe cases of facial acnes were used on the immunoblots (containing 10 ug of R acnes lysate) to identify antigenic components of P. acnes. As illustrated in Figure 1, sera from individuals with severe cases of facial acnes reacted with several dominant species having the following sizes: 18 -28 kDa; 35-40 kDa; ~50 kDa; -70 kDa; ~100kDa, as well as several low molecular weight species below 18kDa. EXAMPLE 3: BIOINFORMATIC ANALYSIS OF P. ACNES GENOMIC DNA BLAST ANALYSIS Open reading frames (ORFs) were generated from the P. acnes genomic DNA sequence by translation of all contigs in all six possible reading frames, as discussed in Example 1. Any ORFs of 50 residues or greater were retained for further analysis. There were a total of 28,913 ORFs of 50 residues or greater, as disclosed in SEQ ID NOs:300-29,212, and as referenced in Table 3. The 28,913 predicted P. acnes ORF amino acid sequences were used as queries in a BLASTP sequence homology search of the GenBank non-redundant nr protein database (GenBank nr protein, release date 9/25/2000). This database is composed of all non-redundant GenBank protein sequences (CDS translations+PDB+SwissProt+PIR). Details of the database can be found at http://www.ncbi.rrtm.nih.gov/Genban^ The parameters for the BLASTP search were set to the standard defaults with the exception that a significant "hit" was defined as any match with an "E- value" (expected value) of 10 e-8 or less. The E value represents the odds of a particular stretch ,of homology observed between two sequences occurring by chance. Therefore, the lower the E value, the higher the statistical probability that the observed homology is real and that the predicted ORF polypeptide represents a authentic translation product. The 28,913 predicted P. acnes ORF amino acid sequences were also used as queries in a TBLASTN sequence homology search ofthe GenBank non-redundant (nr) nucleic acid database (GenBank nr, release date 11/06/2000). This database comprises all non-redundant nucleic acid sequences (GenBank +EMBL+DDBJ+PDB). Details of the database can be found at: http: / / www.ncbi.nlrn.rtih.gov / Genban / index.html. TBLASTN uses a protein query to search a DNA database that is translated in all six reading frames. The parameters for this TBLASTN search were set to the standard defaults with the exception that a significant "hit" was defined as any match with an "E- value" (expected value) of 10 e-8 or less. GENEMARK ANALYSIS GeneMark software (Georgia Institute of Technology; Atlanta, GA) is a bioinformatics software program used to identify protein-coding regions from DNA sequence based on Markov models, and is discussed at http://genemark.biology.gatech.edu/GeneMark/, which contains information and references particular to the model. Genemark matrices derived from the seven prokaryotic genomes that have been completely sequenced and annotated and are from organisms believed to be similar to P. acnes were used to identify protein-coding sequences in P. acnes. All predicted R. acnes open reading frames (ORFs) with a size of 50 residues or more, as discussed above, were used for this comparative analysis. The BLAST sequence comparison program was then used to compare these ORFs to amino acid sequences in Genebank protein database (blastp) and amino acid sequences translated from DNA sequences in Genebank DNA sequence (tblastn). Seven GeneMark matrices (or training sets) derived from seven different prokaryotic organisms (see below) were selected that had: • complete genomic sequence and annotation available • the highest numbers of protein-coding sequences similar to those of P. acnes These seven GeneMark matrices were used to identify ORFs in the P. acnes genome. The seven organisms used were E.coli, Bacillus subtilis, Helicobacter pylori, Chlamydia pneumoniae, Chlamydia trachomatis, Mycoplasma genitalium and Mycobacterium tuberculosis. Each matrix predicts a set of protein coding sequences from the P. acnes genomic sequence. Some protein-coding sequences were predicted from all 7 organisms and some were predicted from a subset of the 7 organisms. The number of times that a particular ORF is predicted by the 7 matrices is listed in Table 4 (located in a separate document attached to the application) as the "Genemark Score". Thus, the higher the genemark score, the more likely that an ORF represents an authentic P. acnes protein sequence because it is predicted from multiple matrices, indicating that the protein is evolutionarily conserved. Table 4 summarizes the BLAST and GeneMark analysis data ORFs that met the following criteria: i. 50 residues or greater and ii. generated a BLASTP hit with an E value of 10 e-8 or less and/or iii. generated a TBLASTN hit with an E value of 10 e-8 or less and/or iv. was predicted from at least six (6) of the GeneMark matrices. ORFs not meeting criteria (i) and at least one of the other criteria (ii) - (iv) were not included in the final list of ORFs described in Table 4. Table 4 contains the following information: • ORF SEQ ID: SEQ ID assigned to each ORF as defined in Table 3. • DNA SEQ ID: corresponding DNA SEQ ID as defined in Table 2 from which that ORF was derived (translated). • Contig Name: Sequence name assigned in original genomic sequence analysis. • Frame: Reading frame on the DNA contig used to derive the ORF. Forward frames 1, 2 or 3. Reverse frames -1, -2 or -3. • Nucleotide location on DNA contig (Start): Start position of the ORF as located on the DNA contig sequence. • Nucleotide location on DNA contig (End): End position of the ORF as located on the DNA contig sequence. • ORF length: Length of ORF in number of amino acid residues. • Best BLASTP hit, GenBank description line: If a significant BLASTP hit (i.e., by definition, a hit with an E value of 10 e-8 or smaller) was obtained, the description line of the best hit is given here. If no significant hit was obtained, cell is empty. • BLASTP E value: E value of best BLASTP hit. If no significant hit was obtained, cell is empty. • Best TBLASTN hit, GenBank description line: If a significant TBLASTN hit (i.e., by definition, a hit with an E value of 10 e-8 or smaller) was obtained, the description line of the best hit is given here. If no significant hit was obtained, cell is empty. • TBLASTN E value: E value of best TBLASTN hit. If no significant hit was obtained, cell is empty. • GeneMark Score: Number of times that a particular ORF was predicted by the 7 prokaryotic matrices (blank cell indicates that the ORF was not predicted by any ofthe GeneMark matrices) From these BLAST and Genemark bioinformatic analyses, greater than 4500 P. acnes proteins were identified that met the above criteria. This number of P. acnes proteins was identified using a E value threshold of 10 e-8 or smaller, as discussed above, however altering this threshold to 10e-15 gives rise to about 3400 ORFs, altering the threshold to 1 Oe-20 gives rise to about 2900 ORFs and altering the threshold to 10e-25 gives rise to about 2600 ORFs. It is believed that there are roughly 2500-3500 proteins encoded by the P. acnes genome given its size and based on information available for other related microbial organisms. In this regard, certain preferred P. acnes polypeptides ofthe present invention will included those identified in Table 4 as having a BLASTP and/or TBLASTN E value in the range of 10e-15 to lOe- 25, or less. From the results of these combined analyses, one of ordinary skill in the art would view the data of Table 4 as substantially supporting that the proteins identified herein represent authentic translation products ofthe P. acnes genome. EXAMPLE 4: SEROLOGICAL EXPRESSION CLONING OΈP. ACNES ANTIGENS An expression library was constructed as follows: total genomic DNA from the P. acnes strain 6919 was randomly sheared by sonication for 5 seconds at 30%o power (Fisher Sonic Dismembrator) and then termini were filled-in with DNA polymerease I (Klenow fragment; Life Technologies, Rockville, MD) at room temperature for 30 minutes, followed by Pfu polymerase (Stratagene, La Jolla, CA) at 72°C for 30 minutes. EcoRI adaptors (Stratagene, La Jolla, CA) were next ligated to the blunted fragments for 48 hours at 4°C and after heat inactivation of the ligase, adaptors were phosphorylated with T4 polynucleotide kinase for 30 minutes at 37°C. DNA fragments were finally size selected with a Sephacryl S-400 HR (Sigma, St. Louis, MO) column before being ligated into an EcoRI-digested Lambda ZAP Express (Stratagene, La Jolla, CA) vector for 48 hrs at 4°C and packaged with Gigapack III Gold packaging extract (Stratagene, La Jolla, CA). The expression library was screened with 1) sera from pooled individuals with history of severe acnes and 2) with a rabbit poly-clonal Ab raised against P. acnes lysate. This resulted in the cloning of several genes. Sequencing of these resulted in 5' and 3' sequences and in several cases, the sequences of the "full-length" inserts were cloned by a bioinfomiatic approach using the genome sequences generated for P. acnes and described in Example 1. These P. acnes (PA) clones are designated as hPA or rPA depending on whether they were cloned using the human (h) or rabbit (r) sera. Eight ofthe completed clones were obtained with the human sera screen (clones hPA-2,4, 14,20,21,23, 25 and 29) and nine with the rabbit screening (rPA-2,3,7, 15, 17, 19,28,34b and 40). These clones and their positions on the R acnes DNA contigs of SEQ ID NOs: 1-299 are shown below in Table 5. Also shown are the SEQ ID NOs: of the polypeptide sequences encoded within the respective regions on the DNA contigs. Thus, certain of these polypeptides are reactive with sera from pooled individuals with history of severe acnes and/or with rabbit poly- clonal antibody raised against P. acnes lysate and therefore represent immunogenic P. acnes proteins. Table 5 EXAMPLE 5: P. ACNES PROTEINS WITH HOMOLOGIES TO COHEMOLYSIN OF STREPTOCOCCI Whole cell lysates from Propiombacterium acnes strains (ATCC#6919 (NCTC737) and two clinical isolates (PA-1 and PA-2)) were resolved by SDS-PAGE, silver stained and their protein profiles compared. The results revealed the presence of two abundant protein species in both clinical isolates that are lacking in the ATCC strain. These proteins, ZI and ZII, migrated with molecular weights of -28 and 24-kDa respectively (Figure 2). A duplicate gel was transferred onto PVDF membrane and the resolved species visualized following staining with Coomassie brilliant blue. N- terminal sequencing of ZI and ZII derived directly from the PVDF blot revealed the amino acid sequences APVAPIVAVSATQPN and SLLDTQKSAKKAFAPAN respectively. A search of the public data base did not reveal any significant homology with either of these two peptide sequences. However, a similar search performed on the translated ORF's of the sequenced P. acnes genome (see Example 1) revealed the presence of sequences with identities to both ZI and ZII. Both peptides were found within the same ORF of the sequenced P. acnes genome designated by SEQ ID NO: 15127. The sequence ofthe ORF is 313 amino acids long. However, since the first methionine residue is located at amino acid No. 29 of the ORF, presumably, the full- length protein (FL pre-pro) starts at this position and is therefore only 289 amino acid long (with a predicted molecular weight of 30.4 kDa). The first -25 to 30 amino acids of the full length protein (FL pre-pro) is rich in hydrophobic residues, suggestive of the presence of a signal peptide. Thus, ZI/II are presumably membrane bound/secreted. The N-terminal sequence of ZI is located upstream of ZII suggesting that both forms are derived from the same gene product (possibly resulting from differential processing). In addition, mass spec sequencing following tryptic digests of ZI and ZII revealed sequence information similar to those identified by N-terminal sequencing as well as additional internal fragments. The sizes of the these ORFs of ZI and ZII are 27.7 (257 residues) and 24-KDa (222 residues) respectively. Mass Spectrometry analysis was conducted as follows. The two bands (ZI and ZII) were excised and digested in-gel with trypsin. The digested proteins were extracted by 50%) acetonitrile in 5% acetic acid, and concentrated in a speed vacuum. The digested peptides were separated by micro-capillary LC and analyzed by on-line tandem mass spectrometry (LCQ, Finnigan). Identified peptide sequences are as follows: ZI peptides: I) A.APVAPIVAVSATQPNK.T 2) K.TLSVAEAQK.E 3) K.ELQVVNAR.I 4) R.IASLLDTQK.S 5) R.VELLVTMVDTVNGAAHTLQDK.A 6) P.DLKPNDVATFYTK.T 7) K.M*PDLKPNDVATFYTK.T 8) .MPDLKPNDVATF-YTK.T 9) K.ATGVLM*EPLVRN 10) K.ATGVLMEPLVRN II) RNSEVDQAITDVK.A ZII peptides: 1) A.SLLDTQK.S 2) RNELLNTMVDTVΝGAAHTLQDK.A 3) K.M*PDLKPNDVATFYTK.T 4) K.MPDLKPNDNATFYTK.T 5) RNSEVDQAITDVK.A The full length protein sequence of ZI/II was subsequently used to search the ORFs of the sequenced P. acnes genome. The search revealed that ZI/II (SEQ ID NO: 15127) belongs to a family of proteins and shares significant homology with five other related proteins identified in the translated genome of P. acnes (SEQ ID NO: 25540; 6706; 23076; 8751; 27533). Since the entire ORFs of ZI and II were identified in the sequenced genome of the ATCC#6919 culture isolate, failure to detect the corresponding products (in the ATCC#6919) by silver staining of SDS/PAGE gels, cannot be attributed to deletion of the gene but rather from supression of the transcription translation machinary. Finally, a search of the full length protein sequence of ZI/ZII with the GenBank database revealed significant homology with the CAMP factor proteins identified in Groups A and B streptococci (e.g., Streptococcus uberis, agalactiae, pyogenes). The CAMP factor proteins comprise one of two components participating in the CAMP reaction: the synergistic lysis of sheep blood erythrocytes by Staphylococcus aureus spingomyelinase C (beta-toxin). Also, CAMP proteins have been shown to bind with the Fc part of immunoglobulins G and M. Hence, these identified P. acnes proteins may represent virulence factors that could impair the host immune response. EXAMPLE 6: P. ACNES PROTEIN IDENTIFICATION P. acnes (strain ATCC#6919) cell pellet was lysed by French Press. The lysate was run on ion exchange chromatography column (pH=8, in 20 mM Tris, 0 to 30 min gradient from 0 to 300 mM sodium chloride) for pre-fractionation, and each fraction (10 μl out of 10 ml) was run on ID gel. Each band was labeled by fraction number (FP) and estimated molecular weight (e.g., FP24-28KDA). Each fraction was further concentrated down by Centricom (3000 cut off, Millipore) at 5x, lOx, and lOOx depending on the protein concentration in each fraction. The band of interest was cut and in-gel digested. The digested peptides mixture was run on microcapiUary LC online coupled with ESI and tandem mass spectrometry (LCQ, Finnigan). The obtained tandem mass spectra were used to search against P. acnes translated ORFs. The tandem mass spectrometry data were manually reviewed after Sequest search for each experiment. The P. acnes database search results gave the protein sequence, then each identified P. acnes protein was searched against GenBank Protein to find a similarity match (E value, typically E <0.001 for a good match) to determine the presumed protein function. Generally, positive identification of a protein was defined by three peptides identified from the same protein. Sometimes a single peptide matched (with a significant match score) was also used as a positive identification for a protein. A total of 108 proteins were identified using this procedure, and correspond to the following SEQ ID NOs: 20036; 19872; 6373; 8769; 5991; 19299 ; 5011 (two matches); 12317; 11062; 4958; 6923; 11989; 24369; 21491; 7887; 10447 3070; 7878; 25103; 6868; 9121 (two matches); 24474; 12029; 20955; 16555; 15237 20973; 20475; 15259; 6427; 4967; 20100; 10141; 15657; 3608; 16608; 21710; 25380 4853; 25957; 9071; 3659; 13512; 3697; 7384; 24722; 10674; 1282; 1209; 6501; 3691 12347; 21762; 15197; 1165; 23091; 6428; 5429; 24758; 3590; 3723; 9106; 12217: 7270; 2913; 1187; 1585; 16537; 24679; 26397; 26691 (two matches); 7397; 6695 6892; 19926; 4754; 26692; 15670; 3652; 20510; 3449; 20070; 19245; 20108; 19427 10564; 10678; 21172; 21780; 3334; 6338; 5379; 11580; 15693; 9994; 24973; 20684 7865; 16573; 11864; 12324; 20439; 1230; 14278; 3412. EXAMPLE 7: P. ACNES PROTEIN IDENTIFICATION Using the methods described in Example 6, additional proteins were identified and correspond to the proteins disclosed in SEQ ID NOs: 12317; 5991; 6923 10741; 5373; 19299; 383; 1284; 12228; 26402; 4673; 7887; 9004; 384; 25103; 6373 12029; 20036; 16555; 17521; 20476; 15237; 24581; 3659; 14031; 9071; 4958; 15259 12904; 5440; 23560; 3697; 3608; 25957; 7384; 24722; 15863; 8135; 20585; 3691 12217; 16439; 1645; 5514; 21710; 24895; 4853; 23420; 5437; 1278; 16992; 12126 20934; 20475; 17970; 20955; 3070; 6564; 9069; 12666; 7864; 18692; 2453; 1209 20973; 7419; 15197 (two matches); 23591; 20100; 23065; 6337; 10989; 1585; 17841; 6868. EXAMPLE 8: P. ACNES IMMUNOTHERAPEUTIC TARGET IDENTIFICATION Certain classes of proteins are known to represent attractive immunotherapeutic targets based on their roles, for example, in host defense to agents expressing these proteins. For example, enterotoxins as vaccine targets are discussed in Immunology 707:154-160 (2000). Lipoproteins as vaccines are discussed in J. Bacteriol 177:1123-1128 (1995); Infection 24:195-202 (1996); J. Appl Microbiol 87- 250 (1999); and J. Mol. Biol. 302:1153-1164 (2000). Membrane proteins as vaccines are discussed in Vaccine 77:1952-1961 (2000); J. Biotechnol 44:145-153 (1996); Vaccine 75:1456-1466 (2000); Vaccine 73:821-829 (1995); New Eng. J. Med. 23:216- 222 (1998); Infect. Imm. 69:3510-3515 (2001); and J. Infect. Dis. 183:1019-1086 (2001). Permeases play a role in penicillin tolerance in Streptococcus pneumoniae (Mol. Microbiol. 29: 1285- 1296 (1998)). Enterobactin receptor are involved in iron uptake (J. Dairy Sci. 57:2151-02158 (1998)) have been used for immunization of animals (J Bacteriol. 1999 May;181(9):2895-901). Proteases/proteinases as vaccines are discussed in Infect. Imm. 66:899-906 (1998) and Infect. Imm. 65:4055-4063 (2000). A putative proteinase maturation Protein A of Streptococcus pneumoniae is disclosed as having the potential to elicit an immune response, in Infect. Immun. (55:4180-4188 (2000). Potential vaccines based on secreted proteins, or protein involved in secretion are discussed in Infect Immun. 69:3100-3109 (2001); Infect. Immun. 68: 4180-4188 (2000); Proc. Natl. Acad. Sci. USA 7:13853-13858 (2000); and Indian J. Exp. Biol. 37:1157- 1166 (1999). Vaccines based on the antigen superoxide dismutase (SOD) are discussed in Infect. Immun 65:1286-1292 (1997); Infect. Immun. 65:3286-3289 (2000); and Infect. Immun. 67:986-988 (1999). The use of proteins in the adhesin family as vaccines, and their structure, is discussed in Vaccine 7°(Suppl. l):S87-95 (2000); J. Infect. Dis. 752:1146-1152 (2000); Emerg. Infect. Dis. 5:395-403 (1999); Structure 6:1553-1561 (1998); and Mol. Microbiol. 29:1285-1296 (1998). Transporter proteins and their immunogenic properties are discussed in Mol. Microbiol 36:68-84 (2000); Structure 75:1553-1561 (1998); FEMS Immunol Med. Microbiol 19:131-150 (1997); J. Immunol 762:1113-1119 (1999); and Mol. Microbiol. 37:1094-1105 (2000). Haemolysin is described in Microbiology 144:1205-1211 (1998) and vaccination using a Penicillin Binding Protein is described in J. Antimicrob. Chemother. 44:161-114 (1999). Sialidase as a virulence factor and/or an immunogen is discussed in Microb. Drug Resist 3:1-10 (1997); Ann. Rev. Microbiol. 47:89-115 (1993); and crob. Pathog. 6:461-467 (1998). Siderophore binding for iron acquisition by bacteria is described in J. Bacteriol. 181:2895-2901 and Mol. Microbiol. 35:1117-1123 (1999). The role of zinc in PsaA antigen structure is discussed in Structure 6:1553-1561 (1998). The role of bacterial proteins in iron acquisition and transport is described in Mol Microbiol. 36:68-84 (2000); Mol. Microbiol. 32:1117-1123 (1999); and J. Bacteriol. 777:2626-2633 (1989). Manganese and its role in antigen structure is described in FEMS Immunol. Med. Microbiol. 25:245-254; Structure 6:1553-1561 (1998); and Immunol. Med. Microbiol. 79:137-150 (1997). The role of lipase in Staphylococcus pathogenicity is described in Can. J. Microbiol. 36:455-463 (1990). Given the importance of these classes of proteins as vaccine targets, the blastp and tblastn columns of Table 4 were searched using as queries the following keywords: transferase, enterotoxin, Hpoprotein, membrane, permease, enterobactin, protease/proteinase, protein A, secret(ed/ion ory), dismutase, adhesin, transporter, haemolysin, penicillin binding protein, sialidase, siderophore, zinc, iron, manganese and lipase. These searches led to the identification of R acnes proteins, referenced in Table 6 below by their SEQ ID NOs:, that have significant homology to microbial proteins containing these keywords in their blastp and tblastn search result descriptors of Table 4. Therefore, Table 6 below contains a list of P. acnes proteins, referenced by SEQ ID NO:, that likely belong to each of these important classes of proteins that therefore represent valuable targets for immunotherapeutic/vaccine development. Table 6: Illustrative P. acnes Immunotherapeutic Targets EXAMPLE 9: Synthesis of Polypeptides Polypeptides may be synthesized on a Perkin Elmer/Applied Biosystems Division 430 A peptide synthesizer using FMOC chemistry with HPTU (O- Benzotriazole-N,N,N',N'-tetramethyluronium hexafluorophosphate) activation. A Gly- Cys-Gly sequence may be attached to the amino terminus of the peptide to provide a method of conjugation, binding to an immobilized surface, or labeling of the peptide. Cleavage of the peptides from the solid support may be carried out using the following cleavage mixture: trifluoroacetic acid:ethanedithiol:thioanisole:water:phenol (40:1:2:2:3). After cleaving for 2 hours, the peptides may be precipitated in cold methyl-t-butyl-ether. The peptide pellets may then be dissolved in water containing 0.1% trifluoroacetic acid (TFA) and lyophilized prior to purification by C18 reverse phase HPLC. A gradient of 0%-60%> acetonitrile (containing 0.1%) TFA) in water (containing 0.1% TFA) may be used to elute the peptides. Following lyophilization of the pure fractions, the peptides may be characterized using electrospray or other types of mass spectrometry and by amino acid analysis. From the foregoing it will be appreciated that, although specific embodiments of the invention have been described herein for purposes of illustration, various modifications may be made without deviating from the spirit and scope of the invention. Accordingly, the invention is not limited except as by the appended claims. TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 579 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 29200 292 1 247-100-0-0-J15.sTl -1 182 3 29201 292 247-100-0-0-J15.S1 I 5 " 232 2 29202 294 247-87-0-0-C21.S1 I 3 306 1 29203 296 247-93-0-0-F12.r1 - 2 204 1 29204 "" 297 247-37-0-0D10.S1 857 1240 29205 297 247-37-0-0D10.S1 3 I " 1071 1241 29206 298 247-60-0-0L24.S1 1 1297 1497 29207 298 247-60-0-0L24.S1 2 662 , 14 _98 | 29208 298 247-60-6-0L24.S1 -1 " 460 29209 r 298 247-60-0-0L24.S1 -2 168 1 29210 298 247-60-0-0L24.S1 -3 311 3 29211 299 247-41 -0-2119.r1 1 ■ 793 1149 29212 299 247-41 -0-2119.r1 -3 " 250 2 TABLE 3 - Propiβnibacierium Acnes Open Reading Frames Page 1 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 300 1 247-121-0-0-I16.S1 478 723 301 1 247-121-0-0-116.s1 949 1185 302 247-121-0-0-116.s1 1210 1482 303 247-121-0-0-I16.S1 1717 1947 304 1 247-121-0-0-I16.S1 1951 2226 305 247-121-0-0-I16.S1 2530 2826 306 247-121-0-0-I16.S1 2830 3330 307 247-121-0-0-I16.S1 3334 3606 308 247-121-0-0-I16.S1 4039 4197 309 247-121-0-0-I16.S1 4390 4650 310 247-121-0-0-I16.S1 4654 4824 311 I 247-121-0-0-I16.S1 6184 6384 312 247-121-0-0-I16.S1 6631 6894 313 I 247-121-0-0-I16.S1 7018 7371 314 I 247-121-0-0-I16.S1 7417 7608 315 247-121-0-0-I16.S1 7885 8055 316 247-121-0-0-116.s1 8476 8805 317 I 247-121-0-0-I16.S1 9007 9222 318 247-121-0-0-116.s1 9361 11514 319 247-121-0-0-116.s1 11518 12114 320 I 247-121-0-0-I16.S1 12577 12759 321 I 247-121-0-0-I16.S1 12904 13116 322 • ' I 247-121-0-0-116.s1 13120 13401 323 I 247-121-0-0-I16.S1 13483 13725 324 I 247-121-0-0-I16.S1 13840 14304 325 I 247-121-0-0-I16.S1 14506 14697 326 ! 247-121-0-0-116.s1 14824 15003 327 I 247-121-0-0-116.s1 15016 15297 328 I 247-121-0-0-116.s1 15826 16281 329 I 247-121-0-0-I16.S1 16285 16449 330 I 247-121-0-0-116.s1 16738 16953 331 I 247-121-0-0-116.s1 17080 17595 332 f 247-121-0-0-I16.S1 2 293 487 333 1 247-121-0-0-116.s1 2 875 1042 334 1 247-121-0-0-I16.S1 2 1412 1624 335 1 247-121-0-0-I16.S1 2 1670 1849 336 1 247-121-0-0-I16.S1 2 2066 2383 337 ! 247-121-0-0-I16.S1 2 2489 3643 338 1 247-121-0-0-I16.S1 2 3800 3952 339 1 247-121-0-0-I16.S1 2 4118 4297 340 I 247-121-0-0-116.s1 2 4523 6184 341 1 247-121-0-0-I16.S1 2 6464 6721 342 1 247-121-0-0-116.S1 2 6875 7438 343 I 247-121-0-0-116.s1 2 7856 8011 344 1 247-121-0-0-116.S1 2 8015 8422 345 1 247-121-0-0-116.S1 2 8426 8668 346 1 247-121-0-0-116.s1 2 8696 8917 347 1 247-121-0-0-116.S1 2 8921 9085 348 1 247-121-0-0-116.s1 2 9791 10549 349 1 247-121-0-0-116.S1 2 11066 11332 TABLE 3 - Propionibacterium Acnes Open Reading ϊ g rf t-rames Page 2 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 350 1 247-121-0-0-I16.S1 2 11348 11599 351 1 247-121-0-0-I16.S1 2 11993 12325 352 247-121-0-0-I16.S1 2 12473 12631 353 247-121-0-0-I16.S1 2 14006 14185 354 247-121-0-0-116.s1 2 14477 14740 355 247-121-0-0-I16.S1 2 14978 15160 356 247-121-0-0-I16.S1 2 15164 15331 357 247-121-0-0-I16.S1 2 15473 15742 358 247-121-0-0-I16.S1 2 15893 16243 359 247-121-0-0-I16.S1 2 16247 16429 360 247-121-0-0-116.s1 2 16484 16882 361 247-121-0-0-116.s1 2 16886 17071 362 I 247-121-0-0-116.s1 2 17156 17329 363 247-121-0-0-116.s1 2 17486 17695 364 I 247-121-0-0-I16.S1 3 333 1151 365 I 247-121-0-0-116.s1 3 1194 1721 366 I 247-121-0-0-116.s1 3 1863 2420 367 I 247-121-0-0-116.s1 3 2424 2975 368 I 247-121-0-0-116.s1 3 2979 3236 369 I 247-121-0-0-116.s1 3 3363 4523 370 I 247-121-0-0-116.s1 3 4611 4838 371 I 247-121-0-0-116.s1 3 4890 5081 372 1 247-121-0-0-116.s1 3 5085 5798 373 I 247-121-0-0-116.s1 3 6108 7532 374 1 247-121-0-0-116.S1 3 7536 9314 375 1 247-121-0-0-116.s1 3 9546 9869 376 I 247-121-0-0-116.s1 3 10101 10304 377 1 247-121-0-0-116.S1 3 10683 10916 378 1 247-121-0-0-I16.S1 3 10920 11093 379 I 247-121-0-0-116.s1 3 11235 11474 380 1 247-121-0-0-116.s1 3 11478 11699 381 1 247-121-0-0-I16.S1 3 11796 12062 382 1 247-121-0-0-I16.S1 3 12354 13592 383 1 247-121-0-0-116.s1 3 13596 14159 384 1 247-121-0-0-116.s1 3 14163 14606 385 1 247-121-0-0-!16.S1 3 14610 15044 386 1 247-121-0-0-116.s1 3 15048 15218 387 1 247-121-0-0-I16.S1 3 15288 15686 388 1 247-121-0-0-I16.S1 -1 17622 17440 389 1 247-121-0-0-116.S1 -1 17397 17152 390 1 247-121-0-0-116.S1 -1 17103 15667 391 1 247-121-0-0-116.S1 -1 15528 15283 392 1 247-121-0-0-I16.S1 -1 14898 14728 393 1 247-121-0-0-116.s1 -1 13821 13666 394 1 247-121-0-0-116.s1 -1 13080 12835 395 1 247-121-0-0-116.S1 -1 12468 12163 396 1 247-121-0-0-I16.S1 -1 11628 11332 397 1 247-121-0-0-116.s1 -1 11319 11065 398 1 247-121-0-0-116.s1 -1 10950 9706 399 1 247-121-0-0-116.S1 -1 9570 9238 TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 3 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 400 247-121-0-0-116.S1 _"| 8433 8284 401 247-121-0-0-116.s1 -1 7887 7729 402 247-121-0-0-116.s1 -1 7725 7333 403 247-121-0-0-116.S1 -1 6498 6301 404 I 247-121-0-0-I16.S1 -1 6042 5773 405 247-121-0-0-116.S1 -1 5337 5182 406 247-121-0-0-116.s1 -1 4956 4705 407 247-121-0-0-I16.S1 -1 4470 4318 408 247-121-0-0-I16.S1 -1 3678 3430 409 247-121-0-0-116.s1 -1 3153 2914 410 247-121-0-0-I16.S1 -1 1998 1747 411 247-121-0-0-I16.S1 -1 1023 832 412 247-121-0-0-I16.S1 -1 471 292 413 I 247-121-0-0-116.s1 -1 285 52 414 247-121-0-0-I16.S1 -2 17594 17370 415 I 247-121-0-0-116.s1 -2 17366 17199 416 I 247-121-0-0-I16.S1 -2 17171 16956 417 I 247-121-0-0-116.S1 -2 16574 16386 418 I 247-121-0-0-I16.S1 -2 15668 14736 419 I 247-121-0-0-116.s1 -2 14732 14526 420 I 247-121-0-0-116.s1 -2 14522 14328 421 I 247-121-0-0-116.S1 -2 14303 14058 422 I 247-121-0-0-I16.S1 -2 14054 13806 423 I 247-121-0-0-116.s1 -2 13736 12816 424 I 247-121-0-0-I16.S1 -2 12812 12417 425 I 247-121-0-0-116.s1 -2 12413 12243 426 I 247-121-0-0-I16.S1 -2 12137 11937 427 1 247-121-0-0-116.s1 -2 11495 11142 428 ! 247-121-0-0-I16.S1 -2 10715 10155 429 I 247-121-0-0-I16.S1 -2 9923 9597 430 1 247-121-0-0-116.s1 -2 9548 9324 431 1 247-121-0-0-116.S1 -2 9320 8391 432 1 247-121-0-0-116.S1 -2 8387 7944 433 1 247-121-0-0-I16.S1 -2 7880 7263 434 1 247-121-0-0-116.S1 -2 7259 7053 435 l 247-121-0-0-116.s1 -2 6905 6570 436 1 247-121-0-0-116.S1 -2 6479 6024 437 1 247-121-0-0-I16.S1 -2 5906 5754 438 1 247-121-0-0-116.S1 -2 4982 4833 439 1 247-121-0-0-116.S1 -2 4670 3996 440 1 247-121-0-0-116.s1 -2 3992 3756 441 1 247-121-0-0-116.S1 -2 3008 2844 442 I 247-121-0-0-116.s1 -2 2570 2391 443 1 247-121-0-0-116.S1 -2 2261 1950 444 1 247-121-0-0-I16.S1 -2 1757 969 445 l 247-121-0-0-I16.S1 -2 965 750 446 I 247-121-0-0-116.s1 -2 704 459 447 1 247-121-0-0-116.s1 -2 455 255 448 I 247-121-0-0-116.s1 -3 17773 17609 449 I 247-121-0-0-116.s1 -3 17473 17291 TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 4 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 450 247-121-0-0-I16.S1 -3 17182 16976 451 247-121-0-0-116.S1 -3 16456 16229 452 247-121-0-0-I16.S1 -3 16051 15830 453 247-121-0-0-116.S1 -3 15826 15662 454 247-121-0-0-I16.S1 -3 15520 15257 455 247-121-0-0-116.S1 -3 15205 15047 456 247-121-0-0-I16.S1 -3 14842 14225 457 I 247-121-0-0-116.S1 -3 14158 13982 458 I 247-121-0-0-116.s1 -3 13912 13637 459 I 247-121-0-0-116.s1 -3 13060 12884 460 I 247-121-0-0-116.S1 -3 12880 12656 461 I 247-121-0-0-116.s1 -3 12502 11966 462 ! 247-121-0-0-116.S1 -3 11686 11510 463 I 247-121-0-0-116.s1 -3 11467 11183 464 I 247-121-0-0-116.S1 -3 11155 10907 465 I 247-121-0-0-I16.S1 -3 10726 10325 466 I 247-121-0-0-116.s1 -3 10015 9659 467 I 247-121-0-0-116.S1 -3 9412 9254 468 I 247-121-0-0-116.S1 -3 9127 8819 469 1 247-121-0-0-116.S1 -3 8689 8504 470 1 247-121-0-0-I16.S1 -3 8500 8270 471 1 247-121-0-0-116.S1 -3 8266 8003 472 1 247-121-0-0-116.S1 -3 7798 7622 473 1 247-121-0-0-116.S1 -3 7618 7430 474 1 247-121-0-0-116.S1 -3 7348 6959 475 1 247-121-0-0-116.S1 -3 6955 6581 476 1 247-121-0-0-116.S1 -3 6409 5717 477 1 247-121-0-0-116.S1 -3 5713 5516 478 1 247-121-0-0-116.s1 -3 5512 5291 479 1 247-121-0-0-I16.S1 -3 5278 5021 480 1 247-121-0-0-116.S1 -3 4837 4610 481 1 247-121-0-0-I16.S1 -3 4606 4088 482 1 247-121-0-0-116.S1 -3 4072 3740 483 1 247-121-0-0-I16.S1 -3 3709 3305 484 1 247-121-0-0-116.s1 -3 3172 2936 485 1 247-121-0-0-116.S1 -3 2932 2438 486 1 247-121-0-0-116.s1 -3 2434 2105 487 1 247-121-0-0-116.S1 -3 1606 1445 488 1 247-121-0-0-116.S1 -3 1288 1097 489 1 247-121-0-0-116.S1 -3 1093 923 490 1 247-121-0-0-116.S1 -3 808 530 491 1 247-121-0-0-116.S1 -3 220 29 492 2 247-19-0-2E05.S1 670 1092 493 : 2 247-19-0-2E05.S1 1249 1458 494 2 247-19-0-2E05.S1 1849 2277 495 2 247-19-0-2E05.S1 2281 2517 496 2 247-19-0-2E05.S1 2665 2910 497 2 247-19-0-2E05.S1 3172 3408 498 2 247-19-0-2E05.S1 3715 4050 499 2 247-19-0-2E05.S1 4141 4389 cn oi oi Ci oi oi ui cji υi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi υi oi oi oi Oi oi oi oi oi oi oi Oi oi oi Oi oi oi CΛ Cji oi oi υ^ n w tB C s σ) w *^ ωw ^o <o ∞ ro oι j^ ω w - ι o*a ∞ *vi σ) CΛ ^ ωw ^ θ (D Co co cn ^ω M -i θ*s ω 2o w ^ » rπ O D o — M N M M M M N N3 M N M M M N M M M N M M N M M M M M M N M M N N M M M M M M M 3 σ cδ ' 2 O N M M ( N3 l*0 M M M M N M NI M (O M I M M IO M IO N t l"0 CD OO 0000 -NI σ> σ> σ> oi 4^ 4=- co co co ιo IΌ _ o O co oo CO -4 σ> D ro cn 4^ O O NI IΌ O CO 00 00 0000 -si -si σ> CD l l 4^ 4S. 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Ol <D 00 o (l N O tO lD O tO CO S O O Ji C!) 0> ω CO N3 © 0 -sJ O Ψ' Cβ -ι W * sl CO O -ι* N ^ (D ω i\) 00 4- ->• Ol CO CO -> ■ IO Ol CD 00 4=- Oi O O -4 3 tO IO CO * s| 0 -sl C0 4-. 0) tO TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 7 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 600 2 247-19-0-2E05.S1 2 28418 28630 601 2 247-19-0-2E05.S1 2 29234 29437 602 2 247-19-0-2E05.S1 2 29666 29842 603 2 247-19-0-2E05.S1 3 717 890 604 2 247-19-0-2E05.S1 3 894 1241 605 2 247-19-0-2E05.S1 3 1392 2168 606 2 247-19-0-2E05.s1 3 2172 2321 607 2 247-19-0-2E05.s1 3 2661 3221 608 2 247-19-0-2E05.S1 3 3471 3620 609 2 247-19-0-2E05.S1 3 3642 3929 610 2 247-19-0-2E05.S1 3 4215 4394 611 2 247-19-0-2E05.S1 3 4398 4571 612 2 247-19-0-2E05.S1 3 5814 5987 613 2. 247-19-0-2E05.S1 3 6486 6662 614 2 247-19-0-2E05.S1 3 6666 6818 615 2 247-19-0-2E05.S1 3 7233 7448 616 2 247-19-0-2E05.S1 3 8280 8504 617 2 247-19-0-2E05.S1 3 8940 10412 618 2 247-19-0-2E05.S1 3 11409 11618 619 2 247-19-0-2E05.S1 3 11799 11948 620 2 247-19-0-2E05.S1 3 12282 13907 621 2 247-19-0-2E05.S1 3 14016 14204 622 2 247-19-0-2E05.S1 3 14658 14969 623 2 247-19-0-2E05.S1 3 14973 15137 624 2 247-19-0-2E05.S1 3 15249 15968 625 2 247-19-0-2E05.S1 3 15972 16307 626 2 247-19-0-2E05.S1 3 16311 16496 627 2 247-19-0-2E05.S1 3 18159 18350 628 2 247-19-0-2E05.S1 3 18768 18968 629 2 247-19-0-2E05.S1 3 18978 19274 630 2 247-19-0-2E05.S1 3 19953 20195 631 2 247-19-0-2E05.S1 3 20385 20693 632 2 247-19-0-2E05.S1 3 20697 22682 633 2 247-19-0-2E05.S1 3 22686 22877 634 2 247-19-0-2E05.S1 3 22881 23069 635 2 247-19-0-2E05.S1 3 23382 23570 636 2 247-19-0-2E05.S1 3 23574 23768 637 2 247-19-0-2E05.S1 3 23799 24050 638 2 247-19-0-2E05.S1 3 24054 24257 639 2 247-19-0-2E05.S1 3 24465 24689 640 2 247-19-0-2E05.S1 3 24852 25040 641 2 247-19-0-2E05.S1 3 25044 25313 642 2 247-19-0-2E05.S1 3 25437 25712 643 2 247-19-0-2E05.S1 3 25818 26030 644 2 247-19-0-2E05.S1 3 26034 26267 645 2 247-19-0-2E05.S1 3 26406 26621 646 2 247-19-0-2E05.S1 3 26772 26948 647 2 247-19-0-2E05.S1 3 26964 27131 648 2 247-19-0-2E05.S1 3 27147 27344 649 2 247-19-0-2E05.S1 3 27366 27515 ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro cD CD ro ro C0 C0 C0 CD CD C0 CD ∞ C» C» C0 00 00 C» ∞ 00 C» --*sJ -**sl -s| *-*sI ---s| --*sl ---sl -s^ C0 C0 IS W * W W ^ O (000 M C» W * W M -i O *B C0 M C5 Cfl - W M -' O (D » -sl R Ul ^ W M O m 2 τι O ~ CΛ ^ rπ O O NNMMNMNNN MMMMMMMMNNMMNMNNMMMNNJMNMMMMNMNMMM MM § δ CQ ' Z O MMNMM M NN3MMM N3NMNMMM NMMM MMMMMM N MN3MN MM 3MMMN 3MWMM ^ ^ ^ 4^ 4^ ^ 4^ 4^ 4^ ^ 4^ 4^ 4^ ^ ^ ^ 4^ 4^ 4^ 4-» 4^ -. 4^ 4^ ^ 4^ 4^ 4^ ^ ^ - -s4 - s J -4 -^ - s l - s l - s l - s l -4 -i *4 - s l - s l *-J *-4 -sJ *-4 - s | -s4 -sJ - - J *-J -s4 *^ -j -j ^ ^ -^ ^ ^ o o CD CO CO CO CD CO CO CO CO CD CO CD CD CΩ CΩ CO CO CO CD CO CD CO CO CD CD CD CO CD CD CO CD CD CO CD CD CD CO CD CO CD CO CD CD CO CD CO CD CD CD CO 3 ( O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O (Q S tό tO M IO IO tό tO IO IO IO lό lό lO IO M M IO lό IO IO IO IO IO IO IO < * > m rπ m m r oπ m m ra m m iTi m m m m rπ rπ rπ m m ii m iTi m rπ m m o o o o o o o o o o o O o O o o o o o o o O o o o o o O O o o o o O o o o o o o o o o o 0 o o o o Ol Ol Ol Ol l 01 Ol Ol Ol Ol Ol n Oi Ol Ol Ol Ol Ol Ol Ol Ol Ol Oi Ol Ol Ol Ol Ol Oi 01 Ol Ol Ol Ol Ol n Ol cn Ol Ol n Ol Ol cn cn 1 Ol Ol Ol Ol 3 cn en en CO en en cn cn en cn en cn en cn CO en en en en en CO cn cn CO en CO en cn en cn en cn cn cn cn cn cn cn en en cn cn CO CO CO co cn cn CO CO Φ C 00 CO O 00 CO CO CD CO tO IO IO IO IO tO tO IO IO tO tO IO IO IO tO IO IO IO IO IO IO IO IO -Α O OI CO O o o o ->• -=- N W IO C 4=- -|i. Ol CD CD -4 -4 CX> 00 C0 C0 C0 o ~ O~ __, IΌ IΌ CO * O -l O-l O--l O--l -4 -4 -si 0 000 00 00 CD CΩ CD CO CD 00 01 Ol CO Ol CO - ■ >* ■*>■ -4 CO IO 00 4. CΩ CO -- > 4*-» |* D OJ -*. CD -!. 4_. O tO OO o Ol (ύ en n IΌ IΌ cn -si CD CO -i CO cD Oo -i- co oo co o ro C - * . --i 00 -- * . O - * *. * * -D C0 00 IO 4-. C0 Ol 00 4^ ro _-*. Ol Ol — *. CO oo 4*. oo CO CO 00 00 -4 0l |O CD ->- 4->. --- CO o O O 00 -P- CD -si CD CO -=- IO CD C» IO O O CD Ol -»• CO I0 4i. CD C0 4-. O O l OO 00 O -si O Ol -4 CD Ol CO ro Oi GO -4 IΌ IΌ Ol CO CO CD CD CO CD CO O OO 3 -4 00 00 CO CD CO lO tO IO IO IO tO IO IO IO tO IO IO IO tO IO tO IO I IO IO tO IO CD IO 00 O Ol 00 0 0 0 - * . --. -- IO IO IO C0 4--- 4i** CD CD CD -s| --*sI OO OO CO CO CO O 0 -i- lO C C0 4^ 0i Oi oi -4 -4 -4 -si 00 oo oo CO CO CO CO 00 co co co n oi *. -^ Cn -sl O CO (» -^ ro cO CD IO CD 4^ - s 4 CO CO CO --i. CO -i. 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IO co IO CO C0 4i- CO C σ) C;ι j^ J |θ Ul C Ui σi O -4 O O W ffl O W M -si -sj co ω iD -ti ∞ o -si ^ CD IΌ O 00 -4 Oi -si -4 CO -si o Ol IΌ TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 9 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 700 2 247-19-0-2E05.S1 ~"\ 7265 6879 701 2 247-19-0-2E05.S1 -1 6440 6096 702 2 247-19-0-2E05.S1 -1 6086 5751 703 2 247-19-0-2E05.S1 -1 5573 5388 704 2 247-19-0-2E05.S1 -1 5384 4902 705 2 247-19-0-2E05.S1 -1 4898 4740 706 2 247-19-0-2E05.S1 -1 4736 4440 707 2 247-19-0-2E05.S1 -1 4313 4134 708 2 247-19-0-2E05.S1 -1 3884 3615 709 2 247-19-0-2E05.S1 -1 3602 2340 710 2 247-19-0-2E05.s1 -1 2249 498 711 2 247-19-0-2E05.s1 -2 28843 28667 712 2 247-19-0-2E05.S1 -2 28576 28193 713 2 247-19-0-2E05.S1 -2 28111 27914 714 2 247-19-0-2E05.S1 -2 27772 27596 715 2 247-19-0-2E05.S1 -2 27505 27317 716 2 247-19-0-2E05.S1 -2 26920 25220 717 2 247-19-0-2E05.S1 -2 25204 24851 718 2 247-19-0-2E05.S1 -2 24847 24617 719 2 247-19-0-2E05.S1 -2 • 24613 24260 720 2 247-19-0-2E05.S1 -2 24256 23726 721 2 247-19-0-2E05.S1 -2 23332 23084 722 2 247-19-0-2E05.S1 -2 23080 22784 723 2 247-19-0-2E05.S1 -2 22420 22205 724 2 247-19-0-2E05.S1 -2 22114 21713 725 2 247-19-0-2E05.S1 -2 21709 21545 726 2 247-19-0-2E05.S1 -2 21109 20882 727 2 247-19-0-2E05.S1 -2 20803 20099 728 2 247-19-0-2E05.S1 -2 19921 19637 729 2 247-19-0-2E05.S1 -2 19573 18971 730 2 247-19-0-2E05.S1 -2 18967 18710 731 2 247-19-0-2E05.S1 -2 17818 17657 732 2 247-19-0-2E05.S1 -2 17650 17438 733 2 247-19-0-2E05.S1 -2 17125 16976 734 2 247-19-0-2E05.S1 -2 16945 16667 735 2 247-19-0-2E05.S1 -2 16387 16073 736 2 247-19-0-2E05.S1 -2 16051 15248 737 2 247-19-0-2E05.S1 -2 15097 14309 738 2 247-19-0-2E05.S1 -2 14305 14138 739 2 247-19-0-2E05.S1 -2 14047 13871 740 2 247-19-0-2E05.S1 -2 13642 13481 741 2 247-19-0-2E05.S1 -2 13477 13199 742 2 247-19-0-2E05.S1 -2 13114 12809 743 2 247-19-0-2E05.S1 -2 12805 12635 744 2 247-19-0-2E05.S1 -2 12631 12452 745 2 247-19-0-2E05.S1 -2 12139 11984 746 2 247-19-0-2E05.S1 -2 11755 11594 747 2 247-19-0-2E05.S1 -2 10954 10781 748 2 247-19-0-2E05.S1 -2 10432 10259 749 2 247-19-0-2E05.S1 -2 10054 9704 -4 -sI *^ -4 -s| -sl -4 -4 ^ *^ -4 -sl -sl -4 -sl -4 - 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G Ni -x O CD CO -si ro Cn 4- CO IO -x θ 2 Tl D _ D z o O .- rπ o D O3 00 00 O3 O3 O3 00 CO Ci3 00 00 00 C0 00 00 C O C» C» O0 CO 00 O0 O 00 O0 00 O3 00 O0 00 00 O0 O0 O 00 C0 O ∞ CQ ' Z - ^ o ro ro ro cn oι 42- 42- j2- N0 Ni _x CO CO Gύ CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO IO Ni Ni Ni Ni NO Ni Ni ro rO Ni Ni Ni NO IO Ni NO Ni NO -x Tl 00 CJ1 G0 00 CO C0 01 0 J2- - X 01 ro 00 -4 ro ro 01 01 cn 42- 42- C0 C0 Ni N0 Ni -x O O O CD 00 03 03 -4 ■ -4 -4 ro ro ro -t- CO CO NO -x o O CO -I Ni CD CD J- CD CO -x CD J2- tO -4 Ni -x IO -fc- -x CO -sl J2- 00 42- CO -x eO Ol O OO -sJ l -x |O -sl Ol lO * s4 Ol CO CO -sl 42. CD ro 0 -x -4 CO 03 Ol CO o -sI CO Ol CO CO J-*- -s| -s| -*4 CD —x -4 ro ro ro -x ιso co - χ 4- -si c_ cn *si o ro oι ro -4 θ -si ϋι -si oo Ni cn ro CO CD ■ sl GO Ol Ni CO O -sl IO ro -x ro CD -x IO Ol C0 -4 C0 42- O tO 01 N0 J2- 03 03 0i -fc. 0l O -fc- ro -x - -si Ni co co ro co co o oi -x 3 • si ro ro ro 01 01 42- 42- CO Ni -x -x CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO Ni Ni Ni Ni O -4 Ol Ni Ol CO CD Ol 42- Ni CO Ol 03 -si CD ro ro cn cn 42- 42- 42- CO CO Ni NO Ni o o cα oo co oo NooO N-sii N-sOi Ni lO Ni NO NO NO Ni Ni Ni NO Ni fO -si ro ro ro 4_ 42- co iO O CO O CD CD CD CO Ol CO -x CO -4 Ol -x -4 co 0 CO Oi co Oi 00 42- -x CO NO O -sJ Cθ ro cθ -sJ 4- - χ *sl 42- -si -x J2- -x ro CO 42- ro -4 CD CO CD Ol IO -sl CO o 00 CO 00 -fc. CO -4 CO -4 Oi CO 0 -sl Oi CΛ 42- Ni co ro 00 o ro θl 01 CD J2- -4 -4 IO 01 CD cn 01 co co Ni co o 01 ro co co o cn -4 42- CO CO -4 0 00 CO 42- GO O Ni GO -x ■ s| 0 -x 42- -x O O Ol C0 01 IO -4 O CO CO -x 00 01 j- ro ro TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 34 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 1950 8 247-7-2-0D07.S1 2 7007 7234 1951 8 247-7-2-0D07.S1 2 7238 7510 1952 8 247-7-2-0D07.S1 2 7514 8296 1953 8 247-7-2-0D07.S1 2 8339 8647 1954 8 247-7-2-0D07.S1 2 8651 8806 1955 8 247-7-2-0D07.S1 2 8810 9067 1956 8 247-7-2-0D07.S1 2 9071 9241 1957 8 247-7-2-0D07.S1 2 9572 10219 1958 8 247-7-2-0D07.S1 2 10562 10828 1959 8 247-7-2-0D07.S1 2 11615 11824 1960 8 247-7-2-0D07.S1 2 11837 12358 1961 8 247-7-2-0D07.S1 2 12362 12538 1962 8 247-7-2-0D07.S1 2 12647 12811 1963 8 247-7-2-0D07.S1 2 13385 13534 1964 8 247-7-2-0D07.S1 2 13550 13957 1965 8 247-7-2-0D07.S1 2 13961 14185 1966 8 247-7-2-0D07.S1 2 14189 14575 1967 8 247-7-2-0D07.S1 2 14645 14932 1968 8 247-7-2-0D07.S1 2 14960 15802 1969 8 247-7-2-0D07.S1 2 15806 16135 1970 8 247-7-2-0D07.S1 2 16139 16486 1971 8 247-7-2-0D07.S1 2 16490 17161 1972 8 247-7-2-0D07.S1 2 17288 17443 1973 8 247-7-2-0D07.S1 2 18053 19969 1974 8 247-7-2-0D07.S1 2 20012 20161 1975 8 247-7-2-0D07.S1 2 20303 20881 1976 8 247-7-2-0D07.S1 2 20948 21646 1977 8 247-7-2-0D07.S1 2 21650 22192 1978 8 247-7-2-0D07.S1 2 23228 23380 1979 8 247-7-2-0D07.S1 2 23729 23926 1980 8 247-7-2-0D07.S1 2 23930 24250 1981 8 247-7-2-0D07.S1 2 24308 24505 1982 8 247-7-2-0D07.S1 2 24590 24856 1983 8 247-7-2-0D07.S1 2 24860 25156 1984 8 247-7-2-0D07.S1 2 25718 26002 1985 8 247-7-2-0D07.S1 2 26351 26572 1986 8 247-7-2-0D07.S1 2 26720 27298 1987 8 247-7-2-0D07.S1 2 27365 27544 1988 8 247-7-2-0D07.S1 2 27656 27826 1989 8 247-7-2-0D07.S1 2 27965 28408 1990 8 247-7-2-0D07.S1 2 28934 29236 1991 8 247-7-2-0D07.S1 2 29240 29410 1992 8 247-7-2-0D07.S1 2 30239 30436 1993 8 247-7-2-0D07.S1 2 30548 30865 1994 8 247-7-2-0D07.S1 2 30878 31069 1995 8 247-7-2-0D07.S1 2 31073 31528 1996 8 247-7-2-0D07.S1 2 32123 32299 1997 8 247-7-2-0D07.S1 2 32441 32668 1998 8 247-7-2-0D07.S1 2 32738 33397 1999 8 247-7-2-0D07.S1 2 34736 35314 Ni Ni lO IO NO IO W IO NO NO tO Ni Ni W IO IO M NO NO IO W IO rO IO rO tO Ni lO ro rO IO IO W W IO Ni W O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O J_ J_ J_ J_ J_ J_ 4_ 4_ 42- J- CO C C CO CO CO CO OJ CO C Ni Ni Ni Ni Ni Ni J Ni -x -x -x -x -x -^ -^ - i -^ co *si ro cn ^ co -i θ co oo -si ro cn - Co to -χ o co oo -4 ro cn j- co iO - χ o ∞ -4 ro cn j2- ω 2 T 2l o _ CO ,-s rn O O 0 co 00 D Z p C i C (j0 CO CO CO G0 C CO C CO G0 G0 CO C C0 C0 C0 CO C CO C0 CO CO CO C C G0 CO C C0 C C Gύ G0 CO CO G0 03 3 φ Ni Ni Ni Ni NO Ni -■ 42- CO Ni -x -x O CD CD O _O O _O C _D O _l Ol 42- CO Ni Ni Ni -x -x o o o CO CO CD OO OO -4 -4 ro l Ol Ol Ol 42- G IO NO ro iO θo co ro -4 θι o C~D C " O " -4 • 0 —3 Ni CO CO ro <jO -x -4 42. CO Ol p j CoO 0 OI IO OO C0 03 42- -X CD 00 42- O C0 01 -S1 CO CD -SJ 42- 42- O3 00 -x -sI C0 -x O_ O _ Ol OO CD -4 CO Cn -x -x CO O -fc- CD Ul o Mo ro r.i - _sxi ro co ro s o ro ro co oro^ oOo c Jn 2 - -fc- oo yi ^-! _ -si co co co -x -fc- o ro oi iO CO Ol -fc- CO -4 CO Cn OO CD Ol Ol o o 00 to CO r O— s -4i r CDo -4i i Nsii r CO.i _x r O l s -sii w I IΌSJ f i cjo -4 Ni CO 03 00 CO O lO IO IO IO IO IO NO IO tO NO Ni lO NO IO M IO NO IO IO Ni lO IO W tO IO Ni lO ro rO IO tO IO O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O o w co co co cD θ o co ∞ oo e» ∞ θ3 θo ∞ co e» s] -si -4 -si - * --4 * si -si sj * --4 si ro ro ro ro ro ro ro ro ro 2 ππ co ∞ -4 ro c j2. co Ni - χ o cD θo -si ro cn -fc- Go ro - χ o c» -si ro cn 42- co No -^ o o oo -4 ro oι j- co 2 Tl O _ C» 00 Ci3 C» 03 C» *03 C» C» CJ e» C0 <» O3 C0 03 03 Ci3 00 C» ∞ CX> <» NO Ni Ni cf Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni NO Ni ro ro NO Ni NO Ni NO Ni Ni Ni IO Ni tO NO NO Ni tO Ni Ni Ni NO Ni Ni Ni NO NO NO Ni Ni N3 Ni NO 4- 42- 42- fc J2?- 42?- 42- -fc- 4.*. 42- 42- ■fc- 42- J2- J- J .2- -fc- 42- -fc- 42- ■fc- 42- . 42- ■fc- J2- 42- 42- ■fc- 42- -fc- 42- ■fc- 42- 42. 42- 42- 42- J2- J- 42- 42- 4- 42- 42- 42- -4 -4 -4 -4 -4 -4 -4 -4 -4 -4 -4 -sl -4 -s| -4 -4 -4 -4 -4 -4 -4 -4 -4 -4 -si -4 -4 -4 l -4 -4 -4 -4 -sl -4 -4 -4 -sl -4 -sl -4 -4 -4 -4 -4 s j -4 -4 sl o I I -4 -sl -sl -4 -4 sl -4 sJ sl -sl -s| -sl -4 -4 -sJ sj s4 *s| -sl o 7J -4 -sJ sI sj sJ -s| sJ -4 -4 -4 -4 -sl -4 -4 -4 -sl -4 -4 -4 -4 -4 -4 -s| -s| sj -4 -4 -4 sj sj I I 3 C Ni Ni Ni Ni Ni Ni Ni NO Ni Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni to Ni Ni Ni Ni Ni ro Ni NO NO IO Ni Ni NO Ni Ni Ni Ni Ni lO io to to iO No ro ro ro ro io I I IΩ O o o O O o o o o O O o o 66 o o o o O O O O 66 O O O O o o o o o o o 0 0 0 D α D α D D D D D D O D D O D O D O o o O O α D α D o o α o o o α o α o o o o α D o α o o α D o o o o o O O σ O α D o O α o α o o o o 0 α D0 0 O ω z -4 -4 IN -4 -sl ■ -4 -sl -4 -4 -4 -4 -4 -4 -sl -4 -4 ■ -4 -sl -4 -4 -4 -4 -4 sl -sl -4 -J -4 -4 -4 -si o O o α -4 -4 -4 -4 -sl -sl sl 3 CO cn cn CO CO CO CO CO CO en co co cn co co co CO co co en co en cn en cn co cn cn co co co en cn co cn cn co en cn co cn en φ CO CO Gi GO CO CO Gύ CO CO CO CO GO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO OO CO CO GO 03 3 φ Ni Ni Ni CO W CO CO Oi OO CO CO CO CO CO CO OO GO CO O CO CO CO CO CO CO CO CO CO GO CO CO CO CO CO rO Ni M Ni Ni Ni NO M -4 00 CD O O O -x -x Ni C C0 42- J-. 01 01 ro ro -400 -si --4 Cn θl -fc- .fc- J- CO CO CO |O O O CO CO CD CD OO OO OO -4 -sl -4 CD ro ϋl 01 0l 42- oo -si o -x -fc- ro No oo cn o co io oo _χ cn J- i 00 co sj IO CD 42- OO ro tO CO GO O --x -4 ro ■ si . i .O . oo ro iO o ro cn -x co ro -x oo Ni Oo ro -x cD CD 00 42- Oi -x CO tO OO CO CO Ni CD CO j- Ni ro o o o cn O 00 N0 O1 0 _0_ C_D -X -4. O_ 4.2- C _0_ -X 0 :1 C:0 oi -fc- cD co c» -x c» o -si co co oo c» -x -x co o ro -sJ 03 00 0 IO CO C0 42- 01 CO I0 01 -x Ol -x -x 00 CD NO a to co co Ni o -i co iO -fc- io - -fc -- o co oo -fc- co ∞ oo co oi oo Ni co -si -si ro ro 3 IΌ IΌ IΌ IΌ CO CO C ωO CcOo CωO CcOo co co co co co Go co ω co co co co co co co co co co co co co co co co co io NO Ni M NO NO w ■ sl OO OO CΩ O O --x χ --x χ N| NOii NNii ccoo ccoo jj_- jj_- coni ccjnn roro * -ssii oo - - 4 4 --s4i ---44 ϋOil oOιl j J22-. 4422-- 4422-- cCoO cCOo ιNsoO -- χ - χ o o o cD oo eχι ∞ -^ C3i ul -sI 42. Ni -fc. 0 -sl ' O " 0 " 0 ' OO OO CO tO -sJ -fc- Ol CD CD -x CD O CO 42- -x CD CO C —O C ^ O -fc- CD -fc- IO OO ro lO O CD CO -x CD θi - χ ro o θ3 Cn — CO IO CD -fcx -fc- -fc- CD -x -4 IΌ -4 -fc- o oi ro o O Ol GO sl 00 42- O CO O -sl C-O- 4-- -4 -4 00 G0 J- CO CO G0 -SI J- O3 O 00 CQ -si ro C0 CD -x 0 42- 42. 00 CO -SI IO CD CO CO Ni -sl Ol 00 -fc- 01 o -4 IO CO 00 -4 ■ sl O O 03 -x co co oo 42- oι o ro co J2- ro ro co J2. Ul sl 42- CO CD C rO Ni VO 90 CoΛ 0 * *4 * N N O*_ C\l lO N CD 10 _ *a3 CD*r- -* OO O U3 *_ Csl O *_ Ui in -t N *_ o N O N ^ Φ ^ Ui '* ffl τ- O in 't *_ 00 -* S in (0 N C\| CVI <» N O *_ O C 1 .O .I.O .C.O. C.D. , _Is_. „h-..IO,. t. |s. o ιo oo c ro τ- M «j θθ co - ■ 4 * ( θ _ I O „ l O IN σ ) n - -s t C! ) N „ Ω N O _ N roιn ( vi ro N S N. mh- CmD ϊLo m-st cήo wro OO O CO -st CD ts- CM OO CM Is- O C .M„ -_ C ts- -si- o ι-s in o cD ro co co τ- > : s _ : _; c H N 1 i n ιn -* - * Ϊ P i C \| Cvl N Φ ro Φ ∞ S * _ * _ - t -N -s t - s t C C I C V I C \ l - O _ S g S m m ts- rs eD Lo in Lo -*si- c c c o ■ ^ CO C U α. en ε e os o eo -st CO CM CD CO . N- IO CM O CD O CD CO T- OO CD I- O CO O O CM co oo ro CM oo CD !_- CO 'st IO ro U CO CM CM 'st OO Is. T- - Is. oO ro o ■ - O o CM ro LO co co c τ co e E c oD 'st OD co ro o i. -^ oo io c io L <s-f O t- LoM irs-. ocM cco iro- o O CO "t t s o- roc - rcM oc ro 2 α. t s - LO LO LO rt st CO OO CsI CM O ffl O) OO OO N ( fl in <t -f** - p* C£K( NySCM NSre- θSffi 0S0Js LSOij 0gfi05«2SS 00 CS«D JS Oii: ^S CO - o rs. co o co ro co cM Lθ oo τ CM CM CM CM CM CM CM CM CM CM CM S tO lfJ IO U t C C r Cvl - T o v- cM oo 'st io eo is. oo ro o CM CO rf Ui CO N » _ 0 -- Cv| e , * ir3 CD N ∞ 0> O τ- CM tr) 't lΛ _ S Cθ σ) O τ- CM CO -st lO CD Is- C O O O O O O O O O O -Γ- - T- - - CM CM CM CM CM CN CM CM CM CM C C C C OO C CO C CO CO -st t CM CM CM CM C4 CM e CM CM CM CN CM CM CM CM e CN CM CM CM CM e CM CM CM CM CN CM CM CM CM CM eN TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 38 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 2150 8 247-7-2-0D07.S1 -2 38461 37253 2151 8 247-7-2-0D07.S1 -2 37096 36710 2152 8 247-7-2-0D07.S1 -2 36313 36107 2153 8 247-7-2-0D07.S1 -2 35779 35081 2154 8 247-7-2-0D07.S1 -2 , 34852 34190 2155 8 247-7-2-0D07.S1 -2 33688 33314 2156 8 247-7-2-0D07.S1 -2 32743 32486 2157 8 247-7-2-0D07.S1 -2 32323 32132 2158 8 247-7-2-0D07.S1 -2 31909 31001 2159 8 247-7-2-0D07.S1 -2 30997 30734 2160 8 247-7-2-0D07.S1 -2 30730 30560 2161 8 247-7-2-0D07.S1 -2 30103 29825 2162 8 247-7-2-0D07.S1 -2 29728 29579 2163 8 247-7-2-0D07.S1 -2 29479 29258 2164 8 247-7-2-0D07.S1 -2 29026 26183 2165 8 247-7-2-0D07.S1 -2 25525 25352 2166 8 247-7-2-0D07.S1 -2 24715 24488 2167 8 247-7-2-0D07.S1 -2 23479 23330 2168 8 247-7-2-0D07.S1 -2 22894 22739 2169 8 247-7-2-0D07.S1 -2 22735 22544 2170 8 247-7-2-0D07.S1 -2 22153 21992 2171 8 247-7-2-0D07.S1 -2 21988 21764 2172 8 247-7-2-0D07.S1 -2 21760 21401 2173 8 247-7-2-0D07.S1 -2 21343 21065 2174 8 247-7-2-0D07.S1 -2 21061 20588 2175 8 247-7-2-0D07.S1 -2 20584 20186 2176 8 247-7-2-0D07.S1 -2 20182 19985 2177 8 247-7-2-0D07.S1 -2 19504 19304 2178 8 247-7-2-0D07.S1 -2 19288 19079 2179 8 247-7-2-0D07.S1 -2 19075 18203 2180 8 247-7-2-0D07.S1 -2 17092 16646 2181 8 247-7-2-0D07.S1 -2 16615 16391 2182 8 247-7-2-0D07.S1 -2 15907 15539 2183 8 247-7-2-0D07.S1 -2 15412 15233 2184 8 247-7-2-0D07.S1 -2 15043 14879 2185 8 247-7-2-0D07.S1 -2 14776 14576 2186 8 247-7-2-0D07.S1 -2 14059 13796 2187 8 247-7-2-0D07.S1 -2 13747 13295 2188 8 247-7-2-0D07.S1 -2 13078 12911 2189 8 247-7-2-0D07.S1 -2 12895 12713 2190 8 247-7-2-0D07.S1 -2 12382 11591 2191 8 247-7-2-0D07.S1 -2 10945 10598 2192 8 247-7-2-0D07.S1 -2 10306 7085 2193 8 247-7-2-0D07.S1 -2 7081 6812 2194 8 247-7-2-0D07.S1 -2 6808 6623 2195 8 247-7-2-0D07.S1 -2 6619 6152 2196 8 247-7-2-0D07.S1 -2 6148 5993 2197 8 247-7-2-0D07.S1 -2 5677 5426 2198 8 247-7-2-0D07.S1 -2 5422 4103 2199 8 247-7-2-0D07.S1 -2 4084 3875 IO Ni Ni Ni Ni Ni Ni N ._O N._i M.„ N..i. M._ .„ N ._O N .~O N ,«i N ..i. N ..O. M ._ N ..i. N .-i N ._i M ._ N ._i N ._i N ._i N .-i N ..O. N ..i. N ._O N ..i. N ._i N ._i N .-i N ._i N ._O N ._i N .-i Ni Ni Ni Ni Ni NO N Ni Ni NO Ni Ni Ni Ni Ni NO Ni Ni NO NNO MNi NNOi NNii Ni NNii NNii NNOi NNii NNOO NNii MNi NNii NNii NNii NNii Ni NNii NNii NNii NNOi NNOi NNii NNii NNOO NNii NNii NNii NNOO NNii NNii NO NO Ni Ni NO NO Ni Ni Ni Ni Ni NO O CΛ j χ ^ ^ χ jχ ^ χ 4 j - -jfc- .jfcx- eCri Cω Wω CωO ωC Cω Cω Cω CωO CωO NM ^N3 NMi NNo3 ^ii NMi Nr3) NN3i r^ ivO3 -----x rt- χ -rt χ rt-i _- χ x rt-ι. .-_i- rt- χ -_ ._. o O O O O O O O O Oo m co ∞ -si ro oι -fc- co to - χ o co -si ro cj s 4^ Go to - χ o cD ∞ -si ro cn 42. Go ιo -^ o cD θo * si ro cn o co oo -si ro oi j- co to o τι D Ό z o CO C33 00 03 ∞ 03 00 CO OO CO C» Ci3 Ci3 C» C» OO OO OO OO OO OO O CO OO CO OO OO C» 00 00 00 00 00 00 00 ∞ IO Ni Ni NO NO Ni Ni Ni Ni Ni Ni Ni Ni NO Ni Ni Ni CO CO CO GO CO CO CO CO CO CO CO CO CO CO J- Ol Ol D ■ si -4 -si . o .o. c .o co cΩ co o σ - χ - χ ro -fc. .fc. Ol Ol Ui ro -4 -sl C0 00 CD CO CO CO 4_ 42- Ol Ol CD -sl -4 . m -x ro ro co co Tl Ni co co ro co co o - c -o - ro - -x -sj to o3 Co o3 ϋι si ro j- -4 -x j2- -4 CO IO 00 CO .fc. O1 00 o co ro -fc- CD to ro O CD -x CO -4 s: S co ω si co ca ■fc- oi to cD -j ro oi oo oi o oi to -si o ■fc- O -x -fc- IO -x lO -sJ IO Cn -4 CO CD O -4 CO O -x CD 42- CD CO __ __ Ni 00 Ol -x o o co ro oo o oo oo No oo cn ro co io oi co 4- -x Ol CD -x -fc- --I co sj co co oo ro o ro o cD ■ si oo IΌ oi oo ro oi CO rt* -x CO rt* -x o oo ro -x 3 NO Ni Ni M NO Ni Ni M Ni ^ NO Ni Ni Ni Ni Ni Ni CO CO CO CO CO CO CO CO CO CO CO CO co co 4_ oi oi ro ro -s| sj si oo oo co co o o -x _x ro io J2- -fc. Ol oi ro -4 -si i Q3 00 CO o _x CO 00 42- J- cn cn -4 -4 Ni CO GO O CD •si - χ oo θ 4- iO J2. -4 co oo - χ io - χ ro iO cn - χ *si cn -4 ■fc- ro o ro co co co ro — _ o -fc- 03 03 CO -fc" 03 cn si _x Ol O Ol i cn -fc. H ■fc- 00 Sl oi o o to Ni ro ro co NO Ni -si oo oo ro oi co cn 42- CD CO GO Ni CO NO -fcx NO CO oo CD -4 CO Ol 42- o ro co ro j-. cn -fc. NO cn J2. Ol o 00 -si O -x 0l θ ro --. J2. -4 -*4 00 CD C0 I C0 IO CD 0l J- Ni _x -4 CO Ol J^. 00 -x ■fc- Ni CO o — l CO 42- -x co ro CO 42- CO -4 NO Ni Ni Ni Ni Ni Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni NO Ni Ni Ni Ni NO Ni Ni Ni NO Ni Ni Ni Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni NO Ni Ni Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni Ni NO Ni NO NO NO Ni NO Ni Ni Ni Ni Ni NO Ni Ni Ni NO Ni Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni CD CO CD CO CD CO CD CO CD CD 00 00 00 00 00 00 CO 00 00 00 -4 -4 -sl -4 -sl -sl -4 -sl -sl -4 ro CD CD CD ro CD CD CD CD CD Ol Ol Ol Ol Ol Ol Ol Ol Ol l CO 00 -4 ro Ol 42- CO Ni _x O CO CO -4 Oi Ol 42- CO ro _x O CO 00 -4 CD oi GO Ni O eo 00 -4 CD Ol •fc- CO Ni O CO 03 -4 ro Ol GO NJ O CO CO CD CO CD co CD CO CD CD CO CO CD CD CD CO CO CD CO 00 00 CO 00 00 03 00 03 00 00 00 oo 00 00 00 00 00 00 00 00 CO 00 00 00 00 00 00 00 00 CO 00 S) ejO Oi CO CO CO CO CO OO CO CO CO CO GO CO CO CO CO CO CO CO CO OO CO CO CO CO CO CO GO OO CO 3 φ C- OO CO -sI sl si ro Ol ϋl ϋl Ol CO CO CO Ni NO - χ - χ ro ro Ni co co co 42- j2- 4- oi ro ro ro -4 sl 00 CO CD CO -4 4- o co ro iO cn -sj c- o3 ->* oi C33 oι -x _x _x | * o Ni ι co - χ cD J^ - χ js . ro -si 4- co cn -4 oo -x o cn ro O O _. 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O o CM CM CM rt rt rt LO LO CO CD CO co N CO CO O CM CM is- ro rt τ- rt CM CO LΩ - 00 00 CC CM 00 00 rt rt lO lO CO |s- rs. |s, ∞ n∞i T- - 1- CM ∞n O∞O rro * ro_ nΞoΞnΞn2ΣM_MΣ--*n-rt2:. co en en cn en en en cn en o o O O O O O O O CM CM CM CM CM CM CM CM CM O O O O O O O O O O O O O O O O O O CM CM CM 00 00 00 I s - |s- N. is. (s is is. is. rt rt rt rt rf rt rt rt rl" CM CM CM CM CM CM CM CM CM ro ro ro ro ro ro ro ro ro 90 z δ α ^^ O -r- < C0 ^ l0 to r-s 00 ro θ -^ < C -* L0 * 3 ∞ CD O ^ CM *^ ^ lO *_3 00 ro O σ L UJ 0 00 0 0 0 0 000 - *r * * τ -r -r -τ -τ -- N * N N C\| N , N N N N N tO C n M n n n n W n 't * ^ '>t -* '* oo oo c oo co oι < ) oo oo c oo oo c c oo o co c co oo oo oo c oo c oo c co oo oo co oo c oo oo oo c oo oo c O (0 O rn oo rt ro ro rf ro ro rt co rf is o o rt o rf co 00 rt |s- rf rt O co rf co rt oo o co rf LO o 00 ro ro |s. o o co 1- 00 O |s- r— ts- o |s- ts. o -r- o [s. 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Is rf rf rt rf rt rt rt rf rt rt rt rt rt rt rf rt rf rf rt rf rt rt rf rt rf rt rf rf rf rf rf rf r C -M CM CM CM CM .o d z oo 9 c CD r CD CD CD CD ro ro ro CD ro r CD ro C o o o CD D CD ro ro CD ro ro ro ro ro ro ro CD ro ro ro ro ro ro ro CD ro ro CD ro ro ro ro CD ro ro ro ro UJ σ O ω 6 90 z 90 9 σ u? o •<— 00 rf ts. 00 o co rt |s- ro IO 00 ro o rf CO is- co ro o co rf . O o LO LO LO IO CD co i os. |s- is- |s- is! |s- is. Is. |s- is. co UJ t 00 oo CO oo 00 00 ro ro ro CD ro ro ro O 00 00 00 oo 00 oo oo 00 co 00 00 oo oo oo co co oo co oo oo co 00 co co 00 co co 00 co co co co o O O O CM TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 43 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 2400 9 247-82-0-0-M20.S1 3 17646 17801 2401 9 247-82-0-0-M20.S1 3 18360 18740 2402 9 247-82-0-0-M20.S1 3 18822 19211 2403 9 247-82-0-0- 20.S1 3 19299 19553 2404 9 247-82-0-0-M20.S1 3 19626 19802 2405 9 247-82-0-0-M20.S1 3 19806 20438 2406 9 247-82-0-0-M20.S1 3 20442 20648 2407 9 247-82-0-0-M20.S1 -1 21099 20809 2408 9 247-82-0-0-M20.S1 -1 20805 20422 2409 9 247-82-0-0-M20.S1 -1 20256 19723 2410 9 247-82-0-0-M20.S1 -1 19491 19153 2411 9 247-82-0-0-M20.S1 -1 18909 18721 2412 9 247-82-0-0- 20.S1 -1 18588 17416 2413 9 247-82-0-0-M20.S1 -1 17412 17143 2414 9 247-82-0-0-M20.S1 -1 16785 16501 2415 9 247-82-0-0-M20.S1 -1 15975 15811 2416 9 247-82-0-0-M20.S1 -1 15351 15202 2417 9 247-82-0-0-M20.S1 -1 14532 12244 2418 9 247-82-0-0-M20.S1 -1 12240 11836 2419 9 247-82-0-0-M20.S1 -1 11832 11467 2420 9 247-82-0-0-M20.S1 -1 11262 10870 2421 9 247-82-0-0-M20.S1 -1 10791 10459 2422 9 247-82-0-0-M20.S1 -1 10446 10294 2423 9 247-82-0-0-M20.S1 -1 10239 9829 2424 9 247-82-0-0- 20.S1 -1 9519 9241 2425 9 247-82-0-0-M20.S1 -1 9237 8917 2426 9 247-82-0-0-M20.S1 -1 8859 8701 2427 9 247-82-0-0-M20.S1 -1 8649 8230 2428 9 247-82-0-0-M20.S1 -1 8193 8038 2429 9 247-82-0-0-M20.S1 -1 7605 7444 2430 9 247-82-0-0-M20.S1 -1 7344 7090 2431 9 247-82-0-0-M20.S1 -1 7050 6850 2432 9 247-82-0-0-M20.S1 -1 6846 6631 2433 9 247-82-0-0-M20.S1 -1 6162 5881 2434 9 247-82-0-0-M20.S1 -1 5706 5530 2435 9 247-82-0-0-M20.S1 -1 4857 4195 2436 9 247-82-0-0-M20.S1 -1 4191 3907 2437 9 247-82-0-0-M20.S1 -1 3636 3460 2438 9 247-82-0-0-M20.S1 -1 3204 2998 2439 9 247-82-0-0-M20.S1 -1 2487 2293 2440 9 247-82-0-0-M20.S1 -1 2289 2092 2441 9 247-82-0-0-M20.S1 -1 2019 1861 2442 9 247-82-0-0-M20.S1 -1 1857 1672 2443 9 247-82-0-0-M20.S1 -1 1662 1435 2444 9 247-82-0-0-M20.S1 -1 603 94 2445 9 247-82-0-0-M20.S1 -2 21431 21255 2446 9 247-82-0-0-M20.S1 -2 20552 20268 2447 9 247-82-0-0-M20.S1 -2 20042 19758 2448 9 247-82-0-0- 20.S1 -2 18572 18348 2449 9 247-82-0-0-M20.S1 -2 18344 18117 TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 44 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 2450 9 247-82-0-0-M20.S1 -2 18113 17808 2451 9 247-82-0-0-M20.S1 -2 17804 17598 2452 9 247-82-0-0-M20.S1 -2 17594 17439 2453 9 247-82-0-0-M20.S1 -2 17270 16782 2454 9 247-82-0-0-M20.S1 -2 16769 16485 2455 9 247-82-0-0-M20.S1 -2 16481 16326 2456 9 247-82-0-0-M20.S1 -2 16040 15867 2457 9 247-82-0-0-M20.S1 -2 15863 15132 2458 9 247-82-0-0-M20.S1 -2 15002 14271 2459 9 247-82-0-0-M20.S1 -2 14264 14100 2460 9 247-82-0-0-M20.S1 -2 14069 13587 2461 9 247-82-0-0-M20.S1 -2 13583 13362 2462 9 247-82-0-0-M20.S1 -2 13352 12837 2463 9 247-82-0-0-M20.S1 -2 12683 12453 2464 9 247-82-0-0-M20.S1 -2 12449 12159 2465 9 247-82-0-0-M20.S1 -2 12080 11898 2466 9 247-82-0-0-M20.S1 -2 11573 11220 2467 9 247-82-0-0-M20.S1 -2 11027 10689 2468 9 247-82-0-0-M20.S1 -2 10640 10326 2469 9 247-82-0-0-M20.S1 -2 9875 9225 2470 9 247-82-0-0-M20.S1 -2 9128 8868 2471 9 247-82-0-0-M20.S1 -2 8615 8427 2472 9 247-82-0-0-M20.S1 -2 8345 8175 2473 9 247-82-0-0-M20.S1 -2 7499 7164 2474 9 247-82-0-0-M20.S1 -2 6758 5580 2475 9 247-82-0-0-M20.S1 -2 5042 4758 2476 9 247-82-0-0-M20.S1 -2 4754 4575 2477 9 247-82-0-0-M20.S1 -2 3278 3114 2478 9 247-82-0-0- 20.S1 -2 2765 2508 2479 9 247-82-0-0-M20.S1 -2 2387 2238 2480 9 247-82-0-0-M20.S1 -2 2132 1956 2481 9 247-82-0-0-M20.S1 -2 1841 1659 2482 9 247-82-0-0-M20.S1 -3 21496 20318 2483 9 247-82-0-0-M20.S1 -3 20248 18656 2484 9 247-82-0-0-M20.S1 -3 17707 17537 2485 9 247-82-0-0-M20.S1 -3 17473 17204 2486 9 247-82-0-0-M20.S1 -3 16999 16727 2487 9 247-82-0-0-M20.S1 -3 16414 15854 2488 9 247-82-0-0-M20.S1 -3 15844 15668 2489 9 247-82-0-0-M20.S1 -3 15157 14903 2490 9 247-82-0-0-M20.S1 -3 14857 14447 2491 9 247-82-0-0-M20.S1 -3 13789 13580 2492 9 247-82-0-0-M20.S1 -3 12394 11474 2493 9 247-82-0-0-M20.S1 -3 11470 11249 2494 9 247-82-0-0-M20.S1 -3 10711 9875 2495 9 247-82-0-0-M20.S1 -3 9532 9383 2496 9 247-82-0-0-M20.S1 -3 9265 9104 2497 9 247-82-0-0-M20.S1 -3 8293 6710 2498 9 247-82-0-0-M20.S1 -3 6508 6317 2499 9 247-82-0-0-M20.S1 -3 6295 6029 tO Ni Ni Ni lO IO O IO Ni W Ni lO Ni lO NO W IO NO IO IO M M M IO W W Ni tO IO Ni lO Ni Ni W C J_-ι cJn_ o4_ι oJ_ι oJ_ι oJ_ι ϋJ_i oJ_ι oJ_ι o4_ι ϋ C i o CO ι o G ι o O ι o GO i ϋe O ι ϋ CO i o CO i ϋ C i o GO i ϋNii oNiι o N ιi oNiι o NO ι oNiι o N iι oNiι oN O ι oι ortι o-_i ϋ_ii o_iι ortι o_iι c--i-iι c3 oι oι oι oι oι oι oi ϋι oι oι o^ o oo -si ro c3i j2- c Ni rt o c33 -si ro cj j2. co Ni rt θ cD θ3 -si ro n -^ c ιθ rt co oo sj ro cn 2- ω z o CO r-s rπ O o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o _ _ _ _ _ _ _ _ ° D 2. = σ CQ ' Z vo o -π 0) 3 NO NO Ni NO Ni NO rt* rt* O O co oo co -si si ro oi oi co co co No iO rt CD CO 00 -4 sl sl CD Ol Ol J2- <J0 Ni Ni -4 Ol CO Tl -4 00 CO Ol GO ro IO Ni CO CO 4- Ol Ol ■ -s| O J2- r t O CO CO OO CD rt* cD CO CO Oo ro C tO ■ si ω co co oi o ro cn o 42- -4 co |\i J_ si CD CO CO CO Ni Ni 42- J2. θ3 4. 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CO CO C IO rt- o O _ co_ e_o o_o_ c_33 θ _o. -4 ro ro oι oι oι oι 42.42- co co rt. -_ o o o eo oo co o ro ro oi oi oi co co NO NO rt rt. ro - c ■ o ■ - j - c ' o- ~ OO eD rt- Ni ro OO Ni C " O " C ~D rt CD CD " -t " - • sl CD Ol CD -sl Cj-l rt CO rt. oO CJl CO Ol -sl CO O ro CO D rt t o OO l tO C rt- -i o j-l tO ■ sl Ol j CO CO NO CD C0 42. Ni NO -4 . 4.2- ro _. i .O. O_ O_ Ni O CD tO J2. rt. o 1 Cj-| sj 00 00 4-. OO Oi ro 42- j2- si o ro oo ro ro co ro co θ3 -4 No co ro o -s| Cθ ro tO rt- ϋl |O Ol C0 42- 00 CO CO j * sl J_ J_ CD CJl -sl C0 CD rt. J_ C0 O C0 rθ -4 *- C0 C0 Ol tO rt Ni Oi rt CO tO O Ni OO IO O CO -sl Ol CD CO 3 N0 Ni N3 Ni Ni N3 N3 N0 N0 N0 Ni Ni Ni N0 rt. __ __ __ _- _i. _- __ _. __ __ _. __ ro CJ1 01 01 J2- J- J- CO C C rt _ι O *_ O CD ∞ CO -4 -4 ro cD 01 01 0l 42- j2- J- CO NO rt. rt. o O O CO 00 00 -4 ro ro CJl Ol 42- CO |O Ni rt rt. O —l C " O ■ rt ~D J2- rt. a3 Ci rt co o co io oo j- rt. oo ci co o cD 4- eo ro c oi CO rt OO CO OO Ol sI lsO O 4- -sl C CO Ni O OO Ol 00 4- OO C0 03 4_ CO 00 42- -si CD o ro ej3 θi ro -si Nθ rt _!. oo co ro co ro oo c» o oo rt CD iO Ni 4.2- ro _. o.o. c_o_ rt. co oι oι o r t . CO 42- -sl -- cύ Ol 00 r t __ cD r t 00 Ni Ni O CD NO Ol -4 -rt Ol 01 01 M CO CO eO CO -rt O CD O * sI 4_ j2- 42- * sl Oi ro Cn C -01 CiO C- O-l CD- J-^ ro -J co oo ιo o oo oo oo oι j2. ro 2- oo ro -si TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 51 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 2800 10 247-17-3-0H11 .s1 3 26196 26579 2801 10 247-17-3-0H11 .s1 3 26583 26963 2802 10 247-17-3-OH11 .s1 3 27057 27290 2803 10 247-17-3-0H11 .s1 3 27792 28007 2804 10 247-17-3-0H11 .s1 3 28233 28421 2805 10 247-17-3-0H11 .s1 3 28677 28910 2806 10 247-17-3-OH V .s1 3 29289 29456 2807 10 247-17-3-OH V .s1 3 29766 30005 2808 10 247-17-3-OH V .s1 3 30009 30524 2809 10 247-17-3-OHr .s1 3 30636 30821 2810 10 247-17-3-0H1' .s1 3 30933 31376 2811 10 247-17-3-OH1 ' .s1 3 31380 31643 2812 10 247-17-3-OH V .s1 3 32091 32381 2813 10 247-17-3-0H1- .s1 3 32439 33023 2814 10 247-17-3-OH1' .s1 3 33027 33491 2815 10 247-17-3-0H1' .s1 3 34404 34625 2816 10 247-17-3-0H1' .s1 3 34641 34997 2817 10 247-17-3-0H1" .s1 3 35067 35273 2818 10 247-17-3-OH1 ' .s1 3 35526 35747 2819 10 247-17-3-0H1 ' I.s1 3 35802 36008 2820 10 247-17-3-0H1 ' I.s1 3 36012 36401 2821 10 247-17-3-0H1' I.s1 3 37272 37502 2822 10 247-17-3-0H1'l.s1 3 37671 38033 2823 10 247-17-3-0H1' I.s1 3 38037 38198 2824 10 247-17-3-0H1' I.s1 3 38202 38438 2825 10 247-17-3-0H1 ' I.s1 3 38505 38840 2826 10 247-17-3-OH1 ' I.s1 3 39006 40031 2827 10 247-17-3-OH1-l.s1 3 40035 40304 2828 10 247-17-3-OH1 l.s1 3 40308 40922 2829 10 247-17-3-0H1" I.s1 3 40926 41102 2830 10 247-17-3-0H1" 1.s1 3 41106 41528 2831 10 247-17-3-0H1" I.s1 3 41532 41738 2832 10 247-17-3-0H1"l.s1 3 41742 42170 2833 10 247-17-3-OH1'l.s1 3 42174 42527 2834 10 247-17-3-0H1 ' I.s1 3 42879 43235 2835 10 247-17-3-OH1 1.s1 3 43239 43397 2836 10 247-17-3-0H1 1.s1 3 43401 43568 2837 10 247-17-3-OH1 1.s1 3 43728 43907 2838 10 247-17-3-0H1 1.s1 3 43911 44072 2839 10 247-17-3-OH1 1.s1 3 44223 44390 2840 10 247-17-3-0H1 1.s1 3 44394 44546 2841 10 247-17-3-OH1 1.s1 3 44550 44807 2842 10 247-17-3-OH1 1.s1 3 44811 45092 2843 10 247-17-3-OH1 1.s1 3 45843 46040 2844 10 247-17-3-OH1 1.s1 3 46419 46583 2845 10 247-17-3-OH1 1.s1 3 46587 47372 2846 10 247-17-3-OH1 1.s1 3 47640 47936 2847 10 247-17-3-OH1 1.s1 3 47940 48116 2848 10 247-17-3-OH1 1.s1 3 48165 48470 2849 10 247-17-3-0H1 1.s1 3 48615 49274 O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O cJi ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ci oi oi oi oi oi oi oi oi oi cn c j i ro oi oi oi oi oi ϋi oi oi oi oi oi -t- T| CD o o o N0 Ni Ni 42- 42- CJl Oi ro CD CD Ol Ol J2. J_ Ni Ni Ni rt. r t . o co o c» oo -sj ro ro ro oi ϋi 42- co co co Go iO Ni Ni rt. __ rt. o o eD CD --s Ol oo Ol O CO CD ul -sl Ni -sI O J- Ol CD CO CO O CO CD Ni CD Ol CO rO O C0 O IO 00 ro J2. C0 C0 -4 C0 Ji. |O O CD CD O -sl J_ O -sl J2- C0 tO NO CO Ni -si CD N0 01 CO OO O Oo ej3 NO OO -4 ro rt- cO J2- C N3 -sI CO tO Cjn 42- *OO N0 42- 00 01 -sj ro NO CΛ Ol CO -sl rt _^ 4_ ro cθ -sI C-ι OO O -s| 5 -4 0l 4- ro 42- -4 01 rt. ro co IΌ 4- co rt- isi co si co j- ro co ro _ o '" i -si ro CJl j2. IO rt J_ Ol O Ol -4 Ni O rt __ sJ lsi CJ1 00 42- rt. s4 00 3 c-i oi ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ci oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi Ol Ol 42- eo o o θ rt rt |so ro ro -^ J- cι cι ro ro c _ι. oι oi J422-- cCoO NNoO t NθO N Nii rtrt oo o CD oCD c0i03 C0303 -s4l -M ro _. ro— ro_. c_Λ. o.-ι.4-2-- c.o ω _ ._ ... o O CO -s| CD rt sl o Ol rt 2- -sl Ol CO J^ OO rt. -sI CO ro O Ni C CD CO rt -sI 4_ ro ro ro IΌ -4 ∞ ro rt *sI C IO C0 4-2. |O O C0 01 0 -s| J- 0 -s! 42- 00 rt. CJ1 00 IO -4 CD O CD GJl CO OO -sI rt. ro rt* oo -s co oi o co oo ro oi o _i. o IΌ OI ro co sI 42- -M CO O ro W Cl Ol tO CD O CJl 42- CJl CO -il CJl -4 0l 01 03 U1 0 J2- CO O CD -sl CO CO Ul 42- 03 ro rt Oi o co co co -si cD -4 CO tO Ni 03 Ol j2- o 3 ι θ rt. ro ->- c oo ro -i co co oo rt ^_ o -i o TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 53 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 2900 10 247-17-3-0H11.S1 -1 59357 59193 2901 10 247-17-3-0H11.S1 -1 59087 58902 2902 10 247-17-3-OH11.s1 58874 58614 2903 10 247-17-3-OH11.s1 58520 58371 2904 10 247-17-3-OH11.s1 58232 58056 2905 10 247-17-3-OH11.s1 57968 57240 2906 10 247-17-3-0H11.S1 57194 56940 2907 10 247-17-3-0H11.S1 55742 55053 2908 10 247-17-3-0H11.S1 55031 54477 2909 10 247-17-3-0H11.S1 54359 52617 2910 10 247-17-3-0H11.S1 I 52538 52365 2911 10 247-17-3-0H11.S1 I 51239 51042 2912 10 247-17-3-0H11.S1 I 50996 50796 2913 10 247-17-3-0H11.S1 50285 48726 2914 10 247-17-3-OH11.s1 I 48701 48534 2915 10 247-17-3-OH11.s1 I 48479 48324 2916 10 247-17-3-OH11.s1 I 47477 47052 2917 10 247-17-3-OH11.s1 I 47006 46836 2918 10 247-17-3-OH11.s1 1 46412 46023 2919 10 247-17-3-0H11.S1 1 46019 45777 2920 10 247-17-3-0H11.S1 1 45563 45351 2921 10 247-17-3-OH11.s1 1 45347 44979 2922 10 247-17-3-0H11.S1 1 44171 43761 2923 10 247-17-3-OH11.s1 1 43757 43323 2924 10 247-17-3-0H11.S1 1 43103 42876 2925 10 247-17-3-0H11.S1 1 42725 41727 2926 10 247-17-3-0H11.S1 1 41705 41145 2927 10 247-17-3-OH11.S1 1 41003 38850 2928 10 247-17-3-0H11.S1 1 38765 38571 2929 10 247-17-3-0H11.S1 1 38342 38172 2930 10 247-17-3-0H11.S1 1 38072 37713 2931 10 247-17-3-0H11.S1 1 37412 36909 2932 10 247-17-3-0H11.S1 1 36527 36291 2933 10 247-17-3-0H11.S1 1 36167 35859 2934 10 247-17-3-0H11.S1 1 34751 34575 2935 10 247-17-3-0H11.S1 1 34472 34245 2936 10 247-17-3-0H11.S1 1 34241 33957 2937 10 247-17-3-0H11.S1 1 33578 32901 2938 10 247-17-3-0H11.S1 1 32663 32481 2939 10 247-17-3-OH11.s1 1 32159 31992 2940 10 247-17-3-OH11.s1 1 31694 31023 2941 10 247-17-3-OH11.s1 1 30881 30654 2942 10 247-17-3-0H11.S1 1 30446 29730 2943 10 247-17-3-OH11.s1 1 29693 29457 2944 10 247-17-3-0H11.S1 1 27848 27690 2945 10 247-17-3-0H11.S1 1 26534 26364 2946 10 247-17-3-OH11.s1 1 26069 25875 ' 2947 10 247-17-3-0H11.S1 1 25601 25272 2948 10 247-17-3-0H11.S1 1 25112 24963 2949 10 247-17-3-0H11.S1 1 24959 24756 lO Ni lO IO W NO Ni NO IO tO tO NO lO NO rO IO IO Ni lO IO tO W IO IO tO IO tO Ni NO IO IO Ni Ni N^ CO CD CO CD CO CD CO CD CO CD CD eO CD CD CO CO CD eO CO CO eO CO CD CD CO CD CO CD CO CD CD CD CO eO CO CD CO CD CO CD CD CO CO CO CD eD CO eO CD CO co o co o eo co ∞ c» cio e3 ∞ c o3 C» co σ3 -si s4 sj *si s| sj sj si sj sj ro roro ro ro ro o m co c» -si ro *_i - o M rto *_ oo -4 ro cj-i 4- o iO rto *_ ci3 *si ro ci 42- co ro rto *_ c» J Tl O D z p CO ^^^ m O D o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o _J D CQ Z — — ' o W IO IO Ni lO M IO Ni tO W Ni M IO Ni lO W Ni lO NO IO IO IO IO W NO NJ W Ni NO NJ to Ni NO Ni NO N^ 4_ J_ J_ J_ J2. 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CO N0 N3 rt- rt CD O 03 00 03 --J -si ro θ l O l O l 42- 4-. 42- C0 tO Ni Ni rt __ rt o o o -sl rt. 10 Ni GO CO GO 42- cn cn oi ro ro cxi oo cD ■ π 4_ rt O O O ! lO -4 CO rt 00 ro 42- < Q D3 J2- cD NO o ro co io co oi o ej3 Cn r t . cn -4 Co o cD -^- ro co -4 co 10 -4 10 rt CD G0 42- CD OO C0 42- " CD Ni G ro oι io o o rt _. o ro rt rt. o iO co ro 42- Ol ro o cn o co si oi rt O Ni CO Cl O GO C ~D CO O Ol CO CD Ni O ro -4 00 N0 Ni CO rt rt SJ θ C0tD C0 ω W ffl - M - iO 00 0 42- o -si oo 42- ro co co rt. cn O 42. ro oo ro iO J- o c o co rt 42- Ni -J cn O NO 3 42- 42- 42- 00 Ni Ni rt. rt. __ _i. o o o 0 00 00 -4 -4 ro ro Ol Ol 42- 4- 42- CO CO IO Ni rt _i. rt. .r . . ro _ _o c _ o -si e3 cD ro oo rt io si - oo oi co o oo ro rt. e^j3 J^ cn M Ci3 Cn -si rt oo n o * sj 4^ ro N3 c rt co ro NO CO - r* y 7S4 t i o 2- . oi oi c r oi -4 ■ i ■ O—Oi o- oi co (0 - *4 M _ N3 0 rt sl C0 O O Ni 00 03 ro Ni ro ω C j ι e» 00 -M - s | SS Si! -- n 2. OO CD O Cj-l J2- CO Cji r t - lo ro r t . cO - o*oι 4ιs2- o-ι ιc*roι ocos s-4i rt- ro ro co ro ro co j- CD OO CO CO O -4 Ci3 CD CD NO ro _ -4 00 42- 42. cn ro o c» co co ro io -si io co rt. o -4 co -si oi 0*, < -' ro ro oi ro -si o oo iO -si oi io co ro eo cD TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 60 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3250 1 1 247-114-0-0-L03.M 14659 14820 3251 1 1 247-114-0-0-L03.r1 15016 15270 3252 1 1 247-114-0-0-L03.r1 16075 16236 3253 1 1 247-114-0-0-L03.r1 16684 16932 3254 1 1 247-114-0-0-L03.I-1 16999 17190 3255 1 1 247-114-0-0-L03.r1 17386 18354 3256 1 1 247-114-0-0-L03.r1 18544 18705 3257 1 1 247-114-0-0-L03.r1 18709 18858 3258 1 1 247-114-0-0-l.03.ri 19096 19326 3259 1 1 247-114-0-0-L03.r1 19441 19602 3260 1 1 247-114-0-0-L03.r1 19774 19929 3261 1 1 247-114-0-0-L.03.ii 20371 20739 3262 1 1 247-114-0-0-L03.I-1 20758 20982 3263 1 1 247-114-0-0-L03.r1 22492 22758 3264 1 1 247-114-0-0-l_03.r1 23170 23325 3265 1 1 247-114-0-0-L.03.r1 23992 24351 3266 1 1 247-114-0-0-L03.r1 24355 24537 3267 1 1 247-114-0-0-L03.r1 24781 25290 3268 1 1 247-114-0-0-L03.r1 25294 25452 3269 1 1 247-114-0-0-L03.r1 25477 26022 3270 1 1 247-114-0-0-L03.r1 26026 26190 3271 1 1 247-114-0-0-L03.r1 26194 26355 3272 1 1 247-114-0-0-L03.r1 26359 26703 3273 1 1 247-114-0-0-L03.r1 27121 27282 3274 1 1 247-114-0-0-L03.r1 27286 27456 3275 1 1 247-114-0-0-L03.r1 27901 28128 3276 1 1 247-114-0-0-L03.r1 28132 28323 3277 1 1 247-114-0-0-L03.r1 28450 28848 3278 1 1 247-114-0-0-L03.r1 28894 29070 3279 1 1 247-114-0-0-L03.r1 2 98 292 3280 1 1 247-114-0-0-L03.r1 2 296 577 3281 1 1 247-114-0-0-L03.M 2 581 793 3282 1 1 247-114-0-0-L03.r1 2 1664 1834 3283 1 1 247-114-0-0-L03.r1 2 1982 2311 3284 1 1 247-114-0-0-L03.r1 2 2372 2524 3285 1 1 247-114-0-0-L03.r1 2 2657 2878 3286 1 1 247-114-0-0-L03.r1 2 2921 3235 3287 1 1 247-114-0-0-L03.r1 2 3239 3772 3288 1 1 247-114-0-0-L03.r1 2 4091 4315 3289 1 1 247-114-0-0-L.03.r1 2 4397 6082 3290 1 1 247-114-0-0-L03.r1 2 6086 6238 3291 1 1 247-114-0-0-L.03.r1 2 6284 6463 3292 1 1 247-114-0-0-L03.r1 2 6548 6790 3293 1 1 247-114-0-0-L03. 2 8396 8632 3294 1 1 247-114-0-0-L03.r1 2 8636 8806 3295 1 1 247-114-0-0-L03.r1 2 8840 9010 3296 1 1 247-114-0-0-L03.r1 2 9014 9190 3297 1 1 247-114-0-0-L03.r1 2 9704 10939 3298 1 1 247-114-0-0-L03.r1 2 10997 11263 3299 1 1 247-114-0-0-L03.r1 2 11267 11467 TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 61 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3300 1 1 247-114-0-0-L03.M 2 11615 12088 3301 1 1 247-114-0-0-L03.M 2 12092 12718 3302 1 1 247-114-0-0-L03. 2 12722 13372 3303 1 1 247-114-0-0-L03. 2 13496 13873 3304 1 1 247-114-0-0-L03.r1 2 13964 14425 3305 1 1 247-114-0-0-L03. 2 14594 14782 3306 1 1 247-114-0-0-L03. 2 15137 15421 3307 1 1 247-114-0-0-L03. 2 15482 15814 3308 1 1 247-114-0-0-L03. 2 15866 16105 3309 1 1 247-114-0-0-L03.M 2 16112 16357 3310 1 1 247-114-0-0-L03. 2 16361 16654 3311 1 1 247-114-0-0-L03.r1 2 16658 16990 3312 1 1 247-114-0-0-L03.r1 2 17399 17557 3313 1 1 247-114-0-0-L.03. 2 18209 19294 3314 1 1 247-114-0-0-L03. 2 19913 20548 3315 1 1 247-114-0-0-L03. 2 20777 21667 3316 1 1 247-114-0-0-L03. 2 21791 22204 3317 1 1 247-114-0-0-L03.r1 2 22280 22969 3318 1 1 247-114-0-0-L03.M 2 22973 23200 3319 1 1 247-114-0-0-L03. 2 23204 23758 3320 1 1 247-114-0-0-L03.r1 2 24170 24697 3321 1 1 247-114-0-0-L03. 2 24944 25093 3322 1 1 247-114-0-0-L03. 2 25097 25528 3323 1 1 247-114-0-0-L03. 2 25595 25747 3324 1 1 247-114-0-0-L03. 2 25751 25927 3325 1 1 247-114-0-0-L03. 2 26312 26485 3326 1 1 247-114-0-0-L03.M 2 26723 26953 3327 1 1 247-114-0-0-L03. 2 27098 28180 3328 1 1 247-114-0-0-L03. 2 28424 28852 3329 1 1 247-114-0-0-L03.M 3 735 1127 3330 1 1 247-114-0-0-L.03.r1 3 1131 1349 3331 1 1 247-114-0-0-L03.r1 3 1353 2723 3332 1 1 247-114-0-0-L03.r1 3 2754 2927 3333 1 1 247-114-0-0-L03.r1 3 3060 3296 3334 1 1 247-114-0-0-L03.r1 3 3552 4451 3335 1 1 247-114-0-0-L03. 3 4455 4934 3336 1 1 247-114-0-0-L03.r1 3 4965 5480 3337 1 1 247-114-0-0-L03.r1 3 5484 5978 3338 1 1 247-114-0-0-L03.r1 3 6171 6389 3339 1 1 247-114-0-0-L03.r1 3 6618 6956 3340 1 1 247-114-0-0-L03.r1 3 7062 7235 3341 1 1 247-114-0-0-L03.r1 3 7272 7640 3342 1 1 247-114-0-0-L03.M 3 7644 8303 3343 1 1 247-114-0-0-L03.r1 3 9120 9272 3344 1 1 247-114-0-0-L03.r1 3 9591 9773 3345 1 1 247-114-0-0-L03. 3 9777 10184 3346 1 1 247-114-0-0-L03.r1 3 10242 10664 3347 1 1 247-114-0-0-L03.r1 3 10668 11333 3348 1 1 247-114-0-0-L03.r1 3 11646 11894 3349 1 1 247-114-0-0-L03.r1 3 11907 12137 co co co co co co Go cjo co co co co eo ω co co co oi Oo co eo co co co co co co co co co co co co co co oi co * 0 (D (0 (0 (0 (O CD _ (D _ » „ OJ C» 03 ω M „ CO C» sl M s| sl S M M N M ro θ) 0) C» CO -4 ro Cj-l 42- CO Ni rt θ OO -4 ro CΛ 4_ Cθ rθ rt θ ∞ -j ro Cjι 4_ G NO rt θ O C» -si ro *0^ Ni Ni lO NO Ni lO W tO IO ro rO W IO ro rO M IO IO Ni M Ni IO IO IO Ni rO W IO Ni lO IO IO IO W IO W 4_ J_ J_ J_ 42- 42- 42- J- J- 4_ 4- -t2- J- J- J- J- 42- J- 42. 42- 42- 4- 42- 42- 42- 42- 4- 4- -^ M M *SJ M M M M M N M M N M NI M M S| S 1 N SJ 1 S J * S| S 1 1 M * S1 S1 N S -II 1 SI J_ _ J_ 42. 4_ J_ 4- J- j2- 4- J- J- j2. 42- J_ J- J- J- 42- 42- J2- J2. J_ 4_ J_ J_ J_ J_ J2- J_ J_ J_ 4_ 4_ J_ J2- J2- J2- J-. J_ 4_ O O O OO O OO O OOO O O O O OO O O O O OO O OO OO OO O O OO O O OOO O o si O OO O OO O OO O OO O O O O O OO O OO O OO OO O OO OO O O OO O O OOO r- |— Γ- |— I— |— Γ- |— O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O CO CO CO CO CO CO GO CO OO CO CO OO CO CO CO CJO CO CO CO CO CO OO CO CO CO GO CO CO CO CO OO CO CO CO GO CO GO CO CJJ W CO CO CO CO CO CO CO CO CO CO CO CO CO GO CO CO CO CO CO CO Oi CO CO GO CO CO GO Ni NO Ni Ni Ni Ni Ni Ni lO Ni Ni Ni rO Ni Ni Ni Ni NO Ni NO Ni Ni Ni Ni Ni Ni Ni Ni No rO CO CD IO IO 1O C OI I -4 00 00 CD 00 00 -4 *S1 CD Ol Cn ϋl Ol GO CO NO Ni Ni O O CD CD 00 03 -sJ sl CD CD co cD co oi rt - eo io o Ni Go j- ro o co ro cn o CD 42- 00 O CO -4 -4 Ol O 4- rt 4_ o -4 C0 03 rt* 03 IO 0l G0 CO -sl C0 42. -4 0 00 CO rt θ3 CD 42- tO -4 Cθ ro θi ro CO 00 ro -4 o O O 42- ro si oι oo o o oo ro Ni θι cθ rt rt cn -si rt C ro 2- ro oi rt sj ro co co -si J2- 2- oι -4 42- co oo ro ro oi Ni oι ro iO co co co oι 42- oo oo -4 ro CO GO co cjO Co c eo c ej eo c co cύ co c oi C co eO Co c co cO Co co eo co co c ω J2.42- 42- 42- 42- 42- 4_ 4- 42- 4- J_ J- J- J- J2- .|2- J- 4- J_ -l- 42- 42.42.42. 42.42. 42- 4^ n w 4- J_ J- J_ J- J- J- 4- 4- 4- C CO CO CO CO CO CO C CO CO M IO IO M Ni M Ni tO IO N0 rt rt ._. __ rt _- rt o m CD OO -4 ro ϋl -J CO IO -i O O OO -M ro Cjι J2. CO M rt O O OO -s ro Cn j2- CO N3 rt θ O C33 -4 ro Cil 4^ 3 TlD D z o NO Ni Ni Ni NO Ni Ni Ni Ni N Ni Ni __ _ _. 2. 01 ro -4 co co __ o θ rt- ιsi co j_ j- oι oι oι ro -4 l -4 -4 -sI ∞ ∞ O O IO C0 . i ro C I sj 03 00 C0 0 00 r_ ^ r^ Ni Ni NO CO J- 4 rt Ol CD rt O Ni Ol Ol CD Ni J2- NO co ro ro 42- CO Ni 01 01 ro ro o co ro O NO Ol Oo ro CJl sl O CO -sl CO C o co ro cn -4 Ol Ol ■— sl -4 -4 Ol 03 c *_o 0 U0J o ro 01 co o ro cn cn 0 —1 O crto oCDo cNoO 00 C " D -sl CD -■- c o rt CO -4 42- rt 00 rt 00 5 CD O 00 IO CO 00 co oi to co *->• Ni CO O J2- Ol CO CD CO 00 O Ni rt CD -4 ' 0 -0 0- 0 42- 00 10 -4 0 00 cn ro GO 00 NO rt. 3 NO tO Ni Ni Ni NO Ni Ni Ni Ni Ni rt __ rt 10 Ni Ni GO Ol -sj sJ CO CO CXJ CO O rO J2- Ol Oi ro -4 -4 -sl 0303 rt 4_ 00 j- 01 ro ro 00 CO CO j2- ϋl Ol CD -4 -sl 00 C0 OO O CO OO sl CD GO OO N3 rt ^ sI rt. t 4_ θ IO 00 ro Ni 4- CO D 00 rt n CD -sl Ni CO NO -sl -4 42- 00 O r t |o C0 C0 4- 01 s| rt Ol rt Ol C0 4- 0 oo co 42. co co ro o ro c -D- c-o- c-o- ∞- ro 01 01 -I. i 00 GO co 00 rt. o O O (Ω 03 - 03 ->■ O o co cn O Ni ro J2. CD s r t . ro o3 4_ ro rt. co e3 r t * iso oi co -4 O Ul ϋl -sl 0l rt si |o 42- C0 -{- co cn ro -4 co 4- C0 O 01 42- C0 00 N3 O 01 O1 O 00 Ol S| sj -4 0l 042- 0 4- -sl 0l rt |s3 ro i0 TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 64 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3450 1 1 247-114-0-0-L03.r1 -2 15796 14702 3451 1 1 247-114-0-0-L03.r1 -2 14698 13391 3452 1 1 247-114-0-0-L03. -2 13348 13187 3453 1 1 247-114-0-0-L03.M -2 13114 12899 3454 1 1 247-114-0-Q-L03.M -2 12712 11567 3455 1 1 247-114-0-0-L03. -2 11188 11009 3456 1 1 247-114-0-0-L03. -2 10996 10754 3457 1 1 247-114-0-0-L03. -2 10750 10241 3458 1 1 247-114-0-0-L03.M -2 10084 9695 3459 1 1 247-114-0-0-L03. -2 9619 9413 3460 1 1 247-114-0-0-L03.M -2 9268 9116 3461 1 1 247-114-0-0-L03. -2 8812 8582 3462 1 1 247-114-0-0-L03. -2 8410 8054 3463 1 1 247-114-0-0-L03. -2 7531 7349 3464 1 1 247-114-0-0-L03. -2 7345 7052 3465 1 1 247-114-0-0-L03. -2 7048 6665 3466 1 1 247-114-0-0-L03. -2 6661 6419 3467 1 1 247-114-0-0-L03.r1 -2 6106 5573 3468 1 1 247-114-0-0-L03. -2 5395 4829 3469 1 1 247-114-0-0-L03. -2 4825 4670 3470 1 1 247-114-0-0-L03. -2 4435 4226 3471 1 1 247-114-0-0-L03.r1 -2 4222 3971 3472 1 1 247-114-0-0-L03. -2 3931 3758 3473 1 1 247-114-0-0-L03.r1 -2 3688 3479 3474 1 1 247-114-0-0-L03.r1 -2 3475 3008 3475 1 1 247-114-0-0-L03.r1 -2 2782 2582 3476 1 1 247-114-0-0-L03. -2 2443 2279 3477 1 1 247-114-0-0-L03. -2 2275 2015 3478 1 1 247-114-0-0-L03.r1 -2 2011 1673 3479 1 1 247-114-0-0-L03.r1 -2 1669 1358 3480 1 1 247-114-0-0-L03. -2 1348 1097 3481 1 1 247-114-0-0-L03.r1 -2 868 713 3482 1 1 247-114-0-0-L03.r1 -2 613 452 3483 1 1 247-114-0-0-L03.r1 -3 29253 28423 3484 1 1 247-114-0-0-L03.M -3 27984 27694 3485 1 1 247-114-0-0-L03.r1 -3 27477 27325 3486 1 1 247-114-0-0-L03.M -3 27321 27133 3487 1 1 247-114-0-0-L03.r1 -3 26985 26815 3488 1 1 247-114-0-0-L03. -3 26184 26014 3489 1 1 247-114-0-0-L03.M -3 25380 24877 3490 1 1 247-114-0-0-L03.r1 -3 24873 24409 3491 1 1 247-114-0-0-L03.r1 -3 24255 24073 3492 1 1 247-114-0-0-L03. -3 24069 23908 3493 1 1 247-114-0-0-L03.r1 -3 23832 23008 3494 1 1 247-114-0-0-L03.r1 -3 22908 22759 3495 1 1 247-114-0-0-L03.r1 -3 22755 22588 3496 1 1 247-114-0-0-L03.M -3 21990 21781 3497 1 1 247-114-0-0-L03.r1 -3 21456 21211 3498 1 1 247-114-0-0-L03.r1 -3 21183 20974 3499 1 1 247-114-0-0-L03.r1 -3 20874 20401 SO 05 o O rs- lcOo oro c∞o rois- roco CcoM t ^ s - CisO. loO roLo coO O-O L∞O Oro CrsO. 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CO CO lO LO rf rf OO CO CO CM -rt CM 00 CO rf rf TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 66 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3550 12 247-56-0-0M06.S1 6355 6594 3551 12 247-56-0-0M06.S1 6946 7095 3552 12 247-56-0-0M06.S1 7651 8928 3553 12 247-56-0-0M06.S1 9289 9732 3554 12 247-56-0-0M06.S1 10015 10254 3555 12 247-5.6-0-0M06.s1 10258 10794 3556 12 247-56-0-0M06.S1 10798 11013 3557 12 247-56-0-0M06.S1 11116 11340 3558 12 247-56-0-0M06.S1 11767 12381 3559 12 247-56-0-0M06.S1 12385 12648 3560 12 247-56-0-0M06.S1 12652 13128 3561 12 247-56-0-0M06.S1 13858 14139 3562 12 247-56-0-0M06.S1 14359 14604 3563 12 247-56-0-0M06.S1 14803 15141 3564 12 247-56-0-0M06.S1 16114 16410 3565 12 247-56-0-0M06.S1 16465 16659 3566 12 247-56-0-0M06.S1 17020 17313 3567 12 247-56-0-0M06.S1 17560 17727 3568 12 247-56-0-0M06.S1 17755 17976 3569 12 247-56-0-0M06.S1 17980 18270 3570 12 247-56-0-0M06.S1 2 281 475 3571 12 247-56-0-0M06.S1 2 587 1078 3572 12 247-56-0-0M06.S1 2 1109 2047 3573 12 247-56-0-0M06.S1 2 2087 2422 3574 12 247-56-0-0M06.S1 2 2426 2758 3575 12 247-56-0-0M06.S1 2 2783 2971 3576 12 247-56-0-0M06.S1 2 2975 3268 3577 12 247-56-0-0M06.S1 2 3725 4024 3578 12 247-56-0-0M06.S1 2 4193 4537 3579 12 247-56-0-0M06.S1 2 4571 4723 3580 12 247-56-0-0M06.S1 2 4859 5077 3581 12 247-56-0-0M06.S1 2 5651 6016 3582 12 247-56-0-0M06.S1 2 6020 6250 3583 12 247-56-0-0M06.S1 2 6254 6700 3584 12 247-56-0-0M06.S1 2 6704 7669 3585 12 247-56-0-0M06.S1 2 8297 8455 3586 12 247-56-0-0M06.S1 2 8459 8695 3587 12 247-56-0-0M06.S1 2 8975 9229 3588 12 247-56-0-0M06.S1 2 10061 10270 3589 12 247-56-0-0M06.S1. 2 10403 10678 3590 12 247-56-0-0M06.S1 2 10682 10876 3591 12 247-56-0-0M06.S1 2 11003 11572 3592 12 247-56-0-0M06.S1 2 11576 11779 3593 12 247-56-0-0M06.S1 2 11783 11968 3594 12 247-56-0-0M06.S1 2 12200 12421 3595 12 247-56-0-0M06.S1 2 12830 13105 3596 12 247-56-0-0M06.S1 2 13109 13366 3597 12 247-56-0-0M06.S1 2 13370 13537 3598 12 247-56-0-0M06.S1 2 13769 13936 3599 12 247-56-0-0M06.S1 2 14066 14368 co co co co co co co co eO Go co co co ejo ω co co ω co co co co co ejO co ejO Go co co co co co ω ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro cn 4i Ji _ ^ j- 4_ 4.4. j_ 4_ ω ω ω ω ω ω ω c*) ω 3 N3 M W i κι i) W i3 N3 M m 00 -4 ro Cn 42- G0 1O -^ O CX3 * s ro C-l J2- CO Ni -:. 0 00 * si ro Ol 42- C NO -^ O O CO -4 ro Cn 42- CO M - i D 5 z O NO IO IO fO M NO Ni M IO M IO IO tO IO IO Ni lO W IO IO IO NO fO Ni lO IO NO Ni M Ni lO IO IO tO W W Ni NO Ni NO Ni Ni Ni Ni Ni Ni Ni NO Ni Ni IO Ni Ni Ni Ni Ni Ni Ni Ni Ni NO Ni Ni Ni Ni NO Ni NO NO Ni Ni NO NO NO NO Ni Ni IO NO NO Ni Ni Ni Ni Ni 42- 42- 42- 42- 42- J2- J2- 42- 42- 42- 42- 42- 42- 42- 4_ 42- J- J2- 42- 42- 4- 42- 4 sl sl 42. 42- 4- 4- 42- 42- 42- 42- 42- 42- 42- 42- 42- 42- 42- 42- J2- 42- 42- - 42- 4- 4- 42- 42.42- J2- J2. -4 -sl l sl sl -sl -sl -sl -4 -4 -4 -4 -sl sl sl -4 sl -4 sl -4 sj sl sl -4 -si " - l -4 -sl sl -4 -4 -4 -4 sl l l sl s| -4 -4 -sl sl sl sj sl sl o Ol Ol Ol Ol Ol Ol Ol cn cln cn cn oi 01 cn oi Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol cn cn 01 01 (in 01 cln cln Ol Ol Ol Ol cn 01 01 01 o CD CD CD ro CD CD CD ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro CD ro ro ro ro ro CD ro ro ro ro ro ro ro ro CD CD CD CD ro ro ro ro 3 C 0000000000000000000 O O O O O O O O O 000000000000000000000 (Q * ■ _2 ooooooooσoooooooooo O O O O O O O O O O O O O O 0000000000000000 Z 03 0 0 0 O O O O O O 0 0 0 O O O 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ro ro CD CD CD CD CD CD CD ro ro CD CD CD CD ro ro ro ro ro ro ro ro ro ro ro ro D ro CD ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro 3 CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO co CO eo CO co eo eo CO eo CO CO eo eo CO co CO eo eo CO eo CO co CO eo CO CO co eo eo CO CO eo CO ro co co co co co co co co co cji Co co Go co co Go oo co co cjo co co co co co co co co ejO Co co co co co w 3 -si si -si oo oo co si si si ro ro oi ϋi oi co -i- o CO CD CO CO sl si ro ro CD Ol l Ol Ol -l- J- J- CO -i- Ol CD J- sl IO CO IO O CO O OO ro CO O O CO ro 42. co si __ co ro ro sl 42- CO O -sl M -{- OI 01 M (D -ι M O O -» N O ϋI o 00 42. cn j_ Ni i -- co ro C sl MD σι θ σ) -» - i ϋl O NO -i- o iO Oi ϋi oi - j - o co co co o co oo o si cn Ni -■- si 4- Ol o ■-. 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J_ -_ 4- 42- 42- tO Ol TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 68 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3650 12 247-56-0-0M06.S1 _"| 16822 16673 3651 12 247-56-0-0M06.S1 -1 16534 16298 3652 12 247-56-0-0M06.S1 -1 16294 15317 3653 12 247-56-0-0M06.S1 -1 15244 14648 3654 12 247-56-0-0M06.S1 -1 13639 13226 3655 12 247-56-0-0M06.S1 -1 13108 12767 3656 12 247-56-0-0M06.S1 -1 12763 12548 3657 12 247-56-0-0M06.S1 -1 12469 12137 3658 12 247-56-0-0M06.S1 -1 12040 11816 3659 12 247-56-0-0M06.S1 -1 11803 11195 3660 12 247-56-0-0M06.S1 -1 10357 10160 3661 12 247-56-0-0M06.S1 -1 10138 9839 3662 12 247-56-0-0M06.S1 ' -1 9595 9422 3663 12 247-56-0-0M06.S1 -1 9202 8783 3664 12 247-56-0-0M06.S1 -1 8413 8246 3665 12 247-56-0-0M06.S1 -1 8182 7955 3666 12 247-56-0-0M06.S1 -1 7630 6605 3667 12 247-56-0-0M06.S1 -1 6520 6134 3668 12 247-56-0-0M06.S1 -1 5410 5090 3669 12 247-56-0-0M06.S1 -1 4225 3956 3670 12 247-56-0-0M06.S1 -1 3847 3650 3671 12 247-56-0-0M06.S1 -1 2404 2222 3672 12 247-56-0-0M06.S1 -1 2065 1778 3673 12 247-56-0-0M06.S1 -1 1774 1460 3674 12 247-56-0-0M06.S1 -1 1411 1178 3675 12 247-56-0-0M06.S1 -1 1174 968 3676 12 247-56-0-0M06.S1 -1 859 617 3677 12 247-56-0-0M06.S1 -1 568 380 3678 12 247-56-0-0M06.S1 -2 18681 18370 3679 12 247-56-0-0M06.S1 -2 18366 18082 3680 12 247-56-0-0M06.S1 -2 16023 15859 3681 12 247-56-0-0M06.S1 -2 15627 15364 3682 12 247-56-0-0M06.S1 -2 15360 13879 3683 12 247-56-0-0M06.S1 -2 13101 11761 3684 12 247-56-0-0M06.S1 -2 11748 11575 3685 12 247-56-0-0M06.S1 -2 11571 11389 3686 12 247-56-0-0M06.S1 -2 11325 11098 3687 12 247-56-0-0M06.S1 -2 11094 10357 3688 12 247-56-0-0M06.S1 -2 9753 9595 3689 12 247-56-0-0M06.S1 -2 9579 9226 3690 12 247-56-0-0M06.S1 -2 8922 8500 3691 12 247-56-0-0M06.S1 -2 8472 7864 3692 12 247-56-0-0M06.S1 -2 7860 7627 3693 12 247-56-0-0M06.S1 -2 7623 7468 3694 12 247-56-0-0M06.S1 -2 7269 6958 3695 12 247-56-0-0M06.S1 -2 6954 6703 3696 12 247-56-0-0M06.S1 -2 6699 6508 3697 12 247-56-0-0M06.S1 -2 6387 5737 3698 12 247-56-0-0M06.S1 -2 5343 5158 3699 12 247-56-0-0M06.S1 -2 4833 4579 TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 69 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3700 12 247-56-0-0M06.S1 -2 4575 3778 3701 12 247-56-0-0M06.S1 -2 3660 2971 3702 12 247-56-0-0M06.S1 -2 2619 2449 3703 12 247-56-0-0M06.S1 -2 2337 2086 3704 12 247-56-0-0M06.S1 -2 1710 1543 3705 12 247-56-0-0M06.S1 -2 801 451 3706 12 247-56-0-0M06.S1 -3 18512 18324 3707 12 247-56-0-0M06.S1 -3 18242 18057 3708 12 247-56-0-0M06.S1 -3 17996 16185 3709 12 247-56-0-0M06.S1 -3 16175 16011 3710 12 247-56-0-0M06.S1 -3 15083 14931 3711 12 247-56-0-0M06.S1 -3 14927 14775 3712 12 247-56-0-0M06.S1 -3 14561 14391 3713 12 247-56-0-0M06.S1 -3 13787 13587 3714 12 247-56-0-0M06.S1 -3 13370 12957 3715 12 247-56-0-0M06.S1 -3 12785 12594 3716 12 247-56-0-0M06.S1 -3 12257 12048 3717 12 247-56-0-0M06.S1 -3 11912 11616 3718 12 247-56-0-0M06.S1 -3 11111 10956 3719 12 247-56-0-0M06.S1 -3 10952 10788 3720 12 247-56-0-0M06.S1 -3 10784 10446 3721 12 247-56-0-0M06.S1 -3 10253 9921 3722 12 247-56-0-0M06.S1 -3 9917 9729 3723 12 247-56-0-0M06.S1 -3 9725 8979 3724 12 247-56-0-0M06.S1 -3 8975 8766 3725 12 247-56-0-0M06.S1 -3 8648 8073 3726 12 247-56-0-0M06.S1 -3 8069 7809 3727 12 247-56-0-0M06.S1 -3 7805 7590 3728 12 247-56-0-0M06.S1 -3 7586 7422 3729 12 247-56-0-0M06.S1 -3 6593 6345 3730 12 247-56-0-0M06.S1 -3 6098 5664 3731 12 247-56-0-0M06.S1 -3 5633 4410 3732 12 247-56-0-0M06.S1 -3 4403 4152 3733 12 247-56-0-0M06.S1 -3 3998 3831 3734 12 247-56-0-0M06.S1 -3 3827 3600 3735 12 247-56-0-0M06.S1 -3 3482 3279 3736 12 247-56-0-0M06.S1 -3 3038 2571 3737 12 247-56-0-0M06.S1 -3 2567 2298 3738 12 247-56-0-0M06.S1 -3 2159 1767 3739 12 247-56-0-0M06.S1 -3 1631 1464 3740 12 247-56-0-0M06.S1 -3 1460 1269 3741 12 247-56-0-0M06.S1 -3 1265 852 3742 12 247-56-0-0M06.S1 -3 737 498 3743 12 247-56-0-0M06.S1 -3 494 303 3744 13 247-55-0-0L18.S1 97 261 3745 13 247-55-0-0L18.S1 265 447 3746 13 247-55-0-0L18.S1 490 651 3747 13 247-55-0-0L18.S1 655 840 3748 13 247-55-0-0L18.S1 1084 1362 3749 13 247-55-0-0L18.S1 1540 1713 GO CO CO GO GO CO CO CO CO CO CO CO CO CO CO GO CO CO GO CO CO CO CO CO GO GO CO CO CO GO CO CO CO CO CO CO CO GO CO CO CO ω sl N M M M M M M M N M M sI M M l M s| | s| s| l * | M sl *ι| s| -ι| -ιl M M | | s| sl J s| sl N - l * s| -sl sl n w o o o o o oo oo oo o3 θo (x cx3 θo (» co -4 si sj sj sj s4 si s4 sj si ro ro ro ro ro ro ro ro ro ro oι oι oι oι oι oι oι oι oι oι § m c» i ro cn 4- eo ι -i θ co -4 ro c 2- co Nθ -^ o o oo si ro ϋi -^ co tO -^ o o c» si ro ci 42- (jo to -^ 2 τι D _ D Z o O .— rπ o O co co co Go co co co co co co co co co co w co (jj co co <jo Go co co w co co (O co co (jo co |5 CQ " Z ^ o 5- tO fO IO IO IO IO IO IO W IO IO Ni lO IO IO IO IO Ni rO IO Ni Ni NO lO tO tO Ni tO tO tO tO IO IO Ni tO IO Ni Ni lO I IO NO IO IO Ni lO 4- 4- 4- 42- J2- J_ J_ J_ J_ J_ J_ J_ J_ J_ J_ J_ 42. -12- 4- ■12- J_ J- J- J2- J- 4- 4- J2. 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Ni o 42. ro o 3 ro ro ro cn 01 42- 42- CO CO NO Ni co co co co co co co co co co co co co CO CO Ni NO Ni Ni Ni Ni NO Ni Ni NO Ni Ni Ni NO NO Ni Ni NO N CO Ol CO Ol O CD Ni 42- -- Ol IO 03 4- ro θ3 θi ro ϋι oι oι oι -t- 2- co co to Ni --. - ->-- o o cD o cD si si ro ro cn oi j2- j- co co N3 -i- -i- -»- -i* o o cD Oo j- o co si ro co ro j- No co oo O _ O " 4 -2- oo si oi o oo i oo ro - o ro -^ ro -i C33 o o cΛ No ro co *si -- ro - ι * oo ι sj cD sj cn iO si -H co GO ro eo ro J2- Sl J2- CO O CO CO 0 0 0 co Go co to θ! -- co co oι oo ro J2- sI IO sl Ol O G0 01 --. ro iO O Ni ro O CO CO ro OO CD O 0 o o j2- ro ro cn ro No oo io o eo lo ro cii si si ro oi No ro si oi o si j- o co oi j- ro o to -i- TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 73 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 3900 13 247-55-0-0L18.S1 3 6813 6989 3901 13 247-55-0-0L18.S1 3 6993 7184 3902 13 247-55-0-0L18.S1 3 7350 7502 3903 13 247-55-0-0L18.S1 3 7506 7676 3904 13 247-55-0-0L18.S1 3 7698 9653 3905 13 247-55-0-0L18.S1 3 9768 9938 3906 13 247-55-0-0L18.S1 3 ' 9942 10097 3907 13 247-55-0-0L18.S1 3 10101 10253 3908 13 247-55-0-0L18.S1 3 10743 10937 3909 13 247-55-0-0L18.S1 3 11169 11561 3910 13 247-55-0-0L18.S1 3 11565 11747 3911 13 247-55-0-0L18.S1 3 11751 11903 3912 13 247-55-0-0L18.S1 3 12051 12350 3913 13 247-55-0-0L18.S1 3 12393 12560 3914 13 247-55-0-0L18.S1 3 12573 12743 3915 13 247-55-0-0L18.S1 3 13206 13370 3916 13 247-55-0-0L18.S1 3 13434 13613 3917 13 247-55-0-0L18.S1 3 13632 14000 3918 13 247-55-0-0L18.S1 3 14061 14285 3919 13 247-55-0-0L18.S1 3 14682 14849 3920 13 247-55-0-0L18.S1 3 14853 16001 3921 13 247-55-0-0L18.S1 3 16065 16247 3922 13 247-55-0-0L18.S1 3 16257 16925 3923 13 247-55-0-0L18.S1 3 16929 17600 3924 13 247-55-0-0L18.S1 3 17604 18302 3925 13 247-55-0-0L18.S1 3 18726 19313 3926 13 247-55-0-0L18.S1 3 19488 19637 3927 13 247-55-0-0L18.S1 3 19650 19799 3928 13 247-55-0-0L18.S1 3 20577 20768 3929 13 247-55-0-0L18.S1 3 21246 21689 3930 13 247-55-0-0L18.S1 3 21750 21905 3931 13 247-55-0-0L18.S1 3 22014 22268 3932 13 247-55-0-0L18.S1 3 22353 22631 3933 13 247-55-0-0L18.S1 3 23034 23435 3934 13 247-55-0-0L18.S1 3 23439 23666 3935 13 247-55-0-0L18.S1 3 23916 24284 3936 13 247-55-0-0L18.S1 3 25092 25265 3937 13 247-55-0-0L18.S1 3 25269 25418 3938 13 247-55-0-0L18.S1 3 25422 25889 3939 13 247-55-0-0L18.S1 3 25893 26171 3940 13 247-55-0-0L18.S1 3 27597 27782 3941 13 247-55-0-0L18.S1 3 27897 28157 3942 13 247-55-0-0L18.S1 3 28161 28325 3943 13 247-55-0-0L18.S1 3 28329 28562 3944 13 247-55-0-0L18.S1 3 28566 28907 3945 13 247-55-0-0L18.S1 3 29712 31400 3946 13 247-55-0-0L18.S1 3 31425 31754 3947 13 247-55-0-0L18.S1 3 31758 32600 3948 13 247-55-0-0L18.S1 3 33828 34064 3949 13 247-55-0-0L18.S1 3 34194 34352 co co co co co co oo co co co (jo co co co co co (jo co co co co co co cjθ co co co (jo co cjθ Go co co ω v. ω ω c ω ω c O CO O CO O O O O CD CD O CO CO O CO CD O O CO CD CD CD O O O O CD O CO O O CD CD O O CO CD O O OO CCOO CCOO CCDD OO OO CO O CO O CO O o o o o o cio oo ∞ ∞ oo eM co co eis ∞ sj sj si si si si si sj sj sj ro ro ro ro ro ro ro ro ~ ro~ ro — ccnn ooii ooii ooii oi oi oi oi ϋi oi o m oo si ro cjη j- co Ni *^ o o oo si ro cji 4_ Go iO -^ o o co -4 ro oι 42- co iO - i θ (θ si ro ci 4_ Cθ fo CD 00 -4 CD 0l 42- C0 N3 ->- O 73 Tl D D z o CO CO GO GO CO CJO CO CJO CJO CJO GO (JO CO CO CO CO GO (JO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO W N N N J-i J 2 i- J_O NJ_i NJ_i NJ_i NJ_i NO Ni Ni Ni Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni NO NO NO Ni NO Ni Ni NO Ni Ni Ni NO NO Ni Ni Ni NO 4 2 O- N4_i 4-i J-i N N N NO Ni Ni Ni Ni NO 42- 42- 42- J- 4- J2- J2. 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J_ 4_ 4_ J^ 4_ 42- J_ J_ J_ J_ J_ ^ sl sj sl sj s j s j sj s j sj sj sj sj sj sj s j sj sj s l s j sj sj sj sj sj sj sj sj sj s j sj sj sj sl sj sl sj sj sl sl sl sj sj sj sj sj sj sj sj sj sj 0 * Oi Ol Oi Oi Ol Oi Ol Oi Oi Oi Ol Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Oi Ol Oi Oi Oi Oi Ol Oi Oi ϋi Ol Oi Oi Oi Oi Ol Oi Ol ϋl Oi Oi Ol Ol 0 3 C Oi Ol Oi Ol Ol Ol Oi Ol Oi Ol Oi Ol Ol Ol Ol Ol Oi Ol Oi ϋl Oi Ol Oi Ol Oi Oi Oi Oi Ol Oi Oi Oi Oi Ol Oi Oi Oi Oi Oi Ol Ol Oi Oi Ol Oi Oi Oi Oi Ol Ol C O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O _ O OO O OO O OO O O OOO OOO OOO O OO O O O OO OO O OO O OOO O O OO O O O OO OOO O Z o I- r- |— ι— i— ι— ι— r- |— ι— ι— r- !— r- r- i— ι— i— ι— ι— r- r- |— r- i- I- ι— ι— Γ~ I— i— t- r- i— i— ι— r- i- r- !— i— ι— |— ι— |— ι— r- |— |— t— S3 c» 00 00 00 co 00 co 00 00 co 00 co 00 00 00 co 00 co 00 00 00 00 co 00 os 00 ∞ C33 ∞ ∞ ∞ co co c» ∞ ∞ 00 00 ∞ 00 co 00 ∞ 00 ∞ 00 00 00 ∞ os 3 eo cn cn cn cn cn cn cn cn cn cn co eo cn co co co co cn co co co co co ' co co co co co co co co co co co OT ro -π Ni Ni Ni Ni Ni Ni Ni Ni Ni fO Ni Ni Ni Ni NO Ni Ni Ni Ni 3 ro IΌ CJO (^ CO CO CO CO CO CO CO CO CO OO CO CO CO CO GO CO CD O O Ni N Ni Ni GO j_ j_ _ oι oι θι ro ro ro -4 ro co ro Ni co co co j- j- 01 ro s| si sl 00 CO CD eo ■ π • si -i co o co ro o co CO Oi sl O J- sj o NO OO CO 42. 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Ol KΩ KΩ S M OI 00 NO CO CO CO 03 42- CO Ni ->- ro O - i * 42- O CO Ol TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 85 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) 4500 15 247-109-0-0-B18.S1 3 16764 17123 4501 15 247-109-0-0-B18.S1 3 17130 17279 4502 15 247-109-0-0-B18.S1 3 17283 17459 4503 15 247-109-0-0-B18.S1 3 18315 18494 4504 15 247-109-0-0-B18.S1 3 18714 18938 4505 15 247-109-0-0-B18.S1 3 19071 19226 4506 15 247-109-0-0-B18.S1 3 19572 19901 4507 15 247-109-0-0-B18.S1 3 19905 20099 4508 15 247-109-0-0-B18.S1 3 20157 20354 4509 15 247-109-0-0-B18.S1 3 20508 20828 4510 15 247-109-0-0-B18.S1 3 20832 21245 4511 15 247-109-0-0-B18.S1 3 21249 21683 4512 15 247-109-0-0-B18.S1 3 21687 21869 4513 15 247-109-0-0-B18.S1 3 22941 23123 4514 15 247-109-0-0-B18.S1 3 23190 23780 4515 15 247-109-0-0-B18.S1 3 23784 24170 4516 15 247-109-0-0-B18.S1 3 24294 24764 4517 15 247-109-0-0-B18.S1 3 24777 24995 4518 15 247-109-0-0-B18.S1 3 25005 25154 4519 15 247-109-0-0-B18.S1 3 25332 25541 4520 15 247-109-0-0-B18.S1 3 25545 25718 4521 15 247-109-0-0-B18.S1 3 25935 26165 4522 15 247-109-0-0-B18.S1 3 26169 26336 4523 15 247-109-0-0-B18.S1 3 26496 26720 4524 15 247-109-0-0-B18.S1 3 26724 26918 4525 15 247-109-0-0-B18.S1 3 26931 27137 4526 15 247-109-0-0-B18.S1 3 27585 27800 4527 15 247-109-0-0-B18.S1 3 28014 28316 4528 15 247-109-0-0-B18.S1 3 28617 28772 4529 15 247-109-0-0-B18.S1 3 29040 29294 4530 15 247-109-0-0-B18.S1 3 29298 29453 4531 15 247-109-0-0-B18.S1 -1 30216 29803 4532 15 247-109-0-0-B18.S1 -1 29367 29191 4533 15 247-109-0-0-B18.S1 -1 29187 27988 4534 15 247-109-0-0-B18.S1 -1 27984 27745 4535 15 247-109-0-0-B18.S1 -1 27447 27271 4536 15 247-109-0-0-B18.S1 -1 27027 26707 4537 15 247-109-0-0-B18.S1 -1 26499 26323 4538 15 247-109-0-0-B18.S1 -1 25863 24955 4539 15 247-109-0-0-B18.S1 -1 24837 24574 4540 15 247-109-0-0-B18.S1 -1 24570 24379 4541 15 247-109-0-0-B18.S1 -1 24276 24064 4542 15 247-109-0-0-B18.S1 -1 24060 23884 4543 15 247-109-0-0-B18.S1 -1 23880 23617 4544 15 247-109-0-0-B18.S1 -1 23547 23356 4545 15 247-109-0-0-B18.S1 -1 23220 21943 4546 15 247-109-0-0-B18.S1 -1 21936 21727 4547 15 247-109-0-0-B18.S1 -1 21723 21448 4548 15 247-109-0-0-B18.S1 -1 21444 21178 4549 15 247-109-0-0-B18.S1 -1 21174 20887 ^1 [1 '1 ^ \ ^ \ ^1 -^ [1 '1 ^ 1 |\ * \ * [1 |1 -^ [1 * \ '1 ^ \ t^ ^ ^ ^ '1 [1 ^ [1 ^ [1 '1 [1 ' ^ ^ ■^ ^ l*. 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Ni Ni NO tO Ni NJ NO Ni Ni Ni Ni Ni Ni Ni NJ Ni IO Ni Ni NO NO Ni sl S s| S s| S S S S S S S -4 S S s| S S S S S S S S S -4 s| S Js. js. js. Js- js. Js- Js. Js. Js. JS. -is. 42. 42. 42. 42. 42. Js. js. Js- -fc. S S S sj S -4 S S S -4 S S S -4 S S S sl S S s JS- j ss- o o C O O O O O O O O O O O O O O O O O O O O O O O O O O O O oi Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol CJl CJl 3 l l l l l l l l l l l l l l I l l l l l l l l l l l l l O P P O O O O O O O O O O o o o o o o ep o o ►sJ O O O O O O O O O O O O O O O O O O O O O O O O O O O O i i ι (O oe l i l i t i l l l i l t i i i i i l i i l l i l i l i i rO Ni Ni NO Ni Ni Ni Ni Ni Ni Ni Ni NO NO Ni NO ro ro o ιό NO Ni p p p p p p p p p p p p p p p o o o p o o o p o p o p p i^ πη rπ m m m m m m m m m m m m m m m m m m m z o o o o o o o o o o o o o o o o o 03 222o2o2o2o_o2o?_o2o22o£o2o_22o2o o2o2o_o22o2o2o_o_22o_o_ JS. J. -fc. J. J2- JS. J2. JS. js- JS- JS- JS- J2- Js. Js- 3 o o o22o o2c°o 2CO C°O co co co co co co co co co co CO CO CO CO CO CO CO CO ro ■ π 03 CO CO GO CO CO CO CO CO CO CO Ni Ni NJ Ni NO Ni Ni Ni Ni Ni NJ Ni 3 ro NO Ni -s ■-. O O o o o oo s s s ro ro ro cji j- js- co co co ro Ni -s CD O CJl -s Ol CO o s -fc- oi oo oi - i . o Oi co ro co co o s o cn ->. s cn CO -s CO !. o --i. cn oo o J2- s- oo CO 00 NO -s O O O Ol Ol 00 O -fc -. -fc -. ro s ro co -_ o -- ro -s o s NO s Ni CO Ol _- o o Js. o s s s oι ro Js- -ι. to ro co S S S sl S S sl S S S S S S S S S S S S S S S S S S S S S S S S S S S S S sJ S S S S S S S sl S S S S sl o o o o o o o o o o ex co oo ex co oo oo co oo ex s s s s s s s s s s ro ro ro cD ro ro ro cD ro ro cJi oi oi oi oi oi oi oi oi oi m o <x s ro cn -fc- GO Ni -^ o o oo s ro eji js- co M -s o o co s ro oi -fc. co to -s o o cx s ro oi -fc- co io -s o o co s ro oi Js co io -i. o 2 Tl D _ CA __. rn O O W M IO IO fO NJ W tO NO IO W IO IO lO NJ NJ tO IO IO M IO Ni W rO IO IO IO W tO Ni lO Ni NJ M 9. J_ i 42. -fc. J^ J_. 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J^ S sl S sl s S sl S S S sj s S S S S S S S S -sl S S S S S S sl S S S S sl S S S S sl S S -sl S S sj S S S -sl S sl o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o 3 _s> o o o o o o o o o o o ό o o o o o o o o o o o o o o o 6 o o o o o o o o o o o o o o o o o o o o o o co' oe Uι o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o όό όόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόό 01 3 o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o lO Ni Ni Ni NO NO Ni Ni NO NO Ni Ni NO Ni Ni Ni NO NO Ni NO Ni Ni NO NO Ni Ni NO NO Ni Ni Ni Ni Ni Ni 3 ro Ni N S sj ro Ol Ol J- Js. CO IO Ni -i- -i. O o o ex oo s ro ro ro oi cn -fc. js. js. co co ro ro -s Ni N Ni T| o o o o -fc- oo -s- o o ro ro iO o oi ro si o o CJl CO -i- S O S Ol -i. co ro - ex ro -s GO -s o ~ oO ~ o o co oo s ro ro oi oi -fc- co r oo -s o -s o ro s s o oi s. j-. ro ro s • o -o ro _ e -x ■ ci cji -s co o ro -s o --fcs. o ofc- -ss o cn -s cn co o_o_ c-o o -si o ro ex o s o -s ro -s x cn ro o cn ro co o o js- ro -s ro — e —x o ro co ro co o cD o ro o -_ I J2- S -s -s - * . O IO S Ni O -s oi co o oo s ro o oo co co e cn *- oi o co ro 42. 42. O CO Ol 00 o 3 o o oo oo s ro ro ro cjι cι 4s. j_ _ co co to ιo rO N0 N3 IO N0 Ni -s -i- -i. -i. _s -i. _. -- __. -_. S S S ro oi Ol 42.42. CO tO -->. --- s Js- CO __. __. -_. O O O O CO OO S CD ro Ol 42. CO O CD O O S O 4s- -. N3 00 004s- -i. f _ sjs-. o—, to io co oi co ex iO o s co ro co co ro o js. 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J_- J2- J__. -^ sl S S S S s| S S S S S S sl sl S S s| S S S S S S S S S S S S S S -sl S S s| S S s l S s l S s l S sl S sl S s l S S o o o e_o co Go co co co co co co co co co GO Go co co oo co 0000000 3 c co co oo co co co co co co co co GO o o o O O O OO O OO O O O OOO O OOO oooooooooooooo oooooooo o o oooo O O OOO O O OO O OO O (θ' O OO OOO O OO oooooooooooooo OO OO O OO OOO O O OO O O O O oooooooo z C_ C_ C_ C_ C_ C_ (_. _. _- c__ <__ e__ c_ <__ e__ e m ιτι m rπ rτι rπ rπ ιτι rπ rπ rτι rπ rπ r 0) to to to N NO Ni NO Ni Ni ro ro Ni ro Ni Ni ro ro ro _s __ π rπ rπ r Ni Ni to to _π_. 3 co co CO CO CO GO GO co co 0 0 0 0 0 O 0 0 0 0 0 0 0 0 0 0 0 O O ro CO CO eo eo CO CO CO CO eo eo CO CO CO CO CO eo CO eo CO CO eo CO CO CO CO CO CO eo co eo CO CO CO co eo co co eo eo CO CO CO CO O Ni 03 co Go co co co co to ro ro 3 ro ro CD Ol Js- CO CO CO IO Ni Ni -s -s O O O o o oι -_ o ro s js. -- ro ro -s oι o ex cjι -- co -s co oo o Ni co cn -i S -s co oi o co oi c roo -s o oi io oo ro iO o ro -s ex cD O -. si ro -fc- co ro roji -coi c-tx. coos roco c O CO C CO IO IO IO NO cx c -fco. coo roro irOo -ss -cos -os ooo 4s- f l 5δ 0 r < ' OO S S OI JS. r s ro -fc. o o js. o s -s s NO 00 Ni Ol CO Ol Ol s Ni O CO Ni -S n f ?S? o o oi -s co -fc- oo cn iO O -s ro o oo cji -s Nj cn •fc. ro Js. iO io o c > O~ O -- 0 -0- -s -s S S S « S g|^ « _ M _ O Ni ro ro to 2. c j- cn o -1. O OO CJl NO S O NO Ol CO OO js. ro -s NJ -fc. O O O co o Js. ro cn ■fc. S Ol 00 s- 00 s eo eo O J •fc. NJ CO Ol CD Ol O ro s cn Ni S Ni S S S S S sI S S S S S S sJ S S S S S S S S S S S S S S S S S S S S S S S S S S S S S sl s S S S S S sJ S o So So oS So So So So So So Soo Soo s ooJ Sco Sco Sco Soo oSo Sco Sco Ss Ss Ss Ss Ss Ss Ss s sJi Ss Ss Sro Sro Sro roS rosl Sro Sro Sro roS Sro Scji Scji ϋSi oSi oSi Sϋi Soi Soi Soi ϋSi m o ex s ro cn Js. w io -~- o o co s ro cn -fc- W Ni -s o o oo s ro cn j- co iO --^ o o co s ro cji j- Go io -s o o oo s ro cn j- co Ni --s o 3 Tl O _ to io io ro iO fo io Ni iO to io ro io io fo Nj ro ro iO io io io ro io iO ro io iO ro iO io io io w o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o M M M M M M M N3 M N3 3 N3 M M M M M M N3 N3 N N3 M N3 M M N M M M J2- J_- J2- _fc- J_. J_- _fc- J2- J2- J_ ^ J_- _fc. J2- J_. J2. -fc. 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J2- Js •fc- Js. ■fc- Js. cn cn cn cn cn cn cn Ol Ol cn cn cn cn cn Ol ro ro cn l cn cn cn cn cn cn cn CJl M NO NO NO Ni Ni Ni Ni NO NO Ni NO NO Ni NO Ni NO 3 U o o o o O O O OOO O OOO OO oooooooooooooo p o oooooooooooooooo IΩ o o o O O o o o O o Ni Ni Ni NJ Ni Ni NO Ni NJ NO NJ Ni Ni Ni NJ Ni Ni x x X X X >o >o > 03 o CO CO CO GO GO CO CO CO Js- JS- J - Ni lO jO IO tO jO IO IO IO JO tO IO IO NJ Ni NJ tO 3 co co co co co co co co co co co co co CO CO CO CO CO CO CO CO CO CO CO CO co co co co co co co co co co co co co co co co ro GO Go rO Ni Ni Ni Ni Ni Ni 03 CO CO NJ Ni Ni CO CO CO OO co co Go ejo co co co co co co co co co co co Go co 3 ro CO NO NJ ro to -, Ni NJ -s o ro co Nj ^ to -j -s -s Ni Ni Ni co Go js. j_- j_- cn cn oi ro Ni CD CO O vij Oulι O»_j e^x-, cκn erxrι tiosj J_s-. S f _: 0u0j c_n ro . rosj rou coj — - O °? Ol O -s IΌ js. ro oo -fc- ro -s ro o js- s o io O Ol CO Ni 00 Js. o ro o js- s o i ro ex o -fc- fo -s o ro o Js. O l Js. 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" CO C CO CO CO CO GO C CO tO tO Ni tO NJ fP Ni tO fO Ni -s -s -s - -s O O O O O O O O O O O rπ o oo s ro cn js- ω M -s θ o oo s ro cn j2. co -s o o oo s ro cι J2. co ιo -ι. o o oo s cD ϋι JS- CO NO o o co s ro oi Js- Go iO -s o 2 τι O ~ " "" σ z O CΛ — rn o O ω ω ω ω ω ω ω ω co ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω co ω ω ω ω ω cΛ i ω ω ω ω ω c ω ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro cD 3 D CQ Z "-' o ω ω ω ω ω co ω ω ω ω ω ω co ω ω ω ω ω co co co co co Ni io w iO io NJ io iO tO NJ fO Ni iO fo Ni M Ni iO iO N^ αi 3 ro o oo oo oo s s si s ro ro ro cji 42. _fc- _fc- GO O CO fO -s Ni Ni Ni Ni -s -s oi to o ro co o si . oi N -i o_ ex ro ιo ro 42- -s -s s CD JS. s ro -s o s -4 ro cn ro ro cn ui js. Go iO Ni -s O O o o o oo ex s ro cn IΌ -fc. cn 00 to O OO O Ol O O NJ O -s fO CO O O l CO t .O . O -l O .l C .O S O CD JS- IO 00 01 O 0-0 " o ro ro GO 00 -fc. 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S CD 01 01 IO O j s o os ex ci oo o ro cn ϋi o js- ro o o ro o ωωooωoωωooωoωoωωoωooωoωoo oo ooooooooooooooooooooooo 4_ 4_ 4_ 4_ 4_ 4_ 4_ 4_ 4_ 4_ CO GOωCθωo ωωCOwCθωωωoooωooooooo CO CωO CO NcΛisωNi Nωi MωNωJ MωNωi NωiωNi Mω-ωsω-s -ω- -wsω- ωωωωωωωωωwωwωωw n w i -s _s _s _s _i θ O O O O O O O O O rπ o ∞ s ro cjι ^ co to -s o o *-3 si ro oι 4s- co to -s o o <χ si ro c.n j- co No _s o o ex s ro oι -fc. co No -s o o oo s ro c-n j- 2 Tl O _ CΛ -s m o o o e ω — s * 3es * 3ωsωsωsωswsjωsωsωsωsωsωsswωrororowωroωroroωωroωrowroωroωroro(rf ωrorocoωroωroωroωrowroωrowroωroωroωroωroωroωroroωrowωroωrowrororororo 3 σ CQ '" z o tO Ni tO IO Ni lO tO tO Ni Ni NO Ni lO NJ fO Ni NJ NJ NJ NJ NJ NJ Ni Ni N Ni NO NJ Ni Ni Ni Ni Ni Ni fO Ni Ni Ni Ni Ni Ni Ni Ni NO NJ J_ J2- J_ J2- J2. J_ j2- J2- J_. J_- J_. J2- J_- J_. Ji J_- J2- _fc- Js- Js- Js- js- J2- 42- 42- S- J2- J2- - J2- J2- i J. JS. Js. js. J2- J2S J23. rJo2- Js J2- J_- J2- J2- Js Ji. S S S S S S S S S S S S S S S S S S S s s s S S S S S sl S sl sj S S s s s s s s S S S S S sj S o cn i Ol Ol Ol Ol O O O O O O O O O O J_π o.fci. oJ_i 4_ J_ J2- J2- cb άi n cn ύi ύi ύi όi όi cn cn CJl Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol Ol o o o o O J_ cJn2- oJ_ cJn2- c -fc- -fc- -fc. Js. 4_- J2. 42- 42- Js. JS- Js. J. Js. J2- -fc. J2s J2- -fc- _fc- J2- j s . Js. Js. 3 •fc- J. Uι J J_ J2. J_ J_ J_ J2- J2- J_ J_ J2. 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CO 01 O NO JS. S Φ. CD S C0 03 O Js. NO O CD O OoJs.oOoO IO O COoOcJoS.e0x0 Js. CJl Ni O CO O -s C0 -fc. o ro CD N0 Js. -fc. o SoSoSoSoSoSo-sJoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSoSosloSosjoSosloSoSoSoSoSoSoSoSoS 42s 4s. 4s. 4S. J-. Js. j2- J_. j2. J-. CO C ω CO CO C CO CJ GO Cθ rθ Ni Ni M Ni M Ni Ni Ni f -^ -s -s -^ o m o oo s ro ei js. co -s o o o3 si ro cn -fc- co Ni -s o o oo s ro ci js- co io -s o o ex s ro cn -fc. Go iO -^ o o oo s ro ro -fc- co io 2 T| Ω σ z o ω ω ω ω ω e-i ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω c ω ω c ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω oo cx oo oo oo co oo oo oo oo oo oo oo co oo co ∞ oo ex cx cx cx cx cx co cx cx oo ex ex cx oo cx cx co cx co cx co co co oo co co ex ∞ 03 3 ro CO GO CO CO CO GO CO CO GO CO CO CO Go rO Ni Ni Ni Ni Ni NO NO Ni Ni Ni NO Ni Ni Ni Ni o s ro ro cn ci 4s. co ιo Ni Ni -s o o (x oo oo co s s ro ro js. ^ CO Ni Ni O O O CO OO S ro CD CJl Ul 42. J- CO fO Ni Ni -s -s O O t S __ __ oi -s oo -s ex oi js. o o si ro co cx s o s cji o ro js. o o s -s -s S J2. Ol O ro C0 M -s O tO 00 JS. S O C0 C0 Js. |O ro N0 CJl N0 S fi -T ro ro O 4s. 4s- O JS. J2s Ol 00 O O Ni S C0 O JS. S Ol -s 00 -s -s ro s Ni O Ni cn s oo o o fo co o js. fO Go -s o Ni cn o cn ro __ __ o rO i iO θi ro o sj co o ιo co o o co co iO θ oo iO ro J2. co ex Ni -s -s o ro o Js Js. o s o oo No co co co o -s o o co ro cn -s ^ oo 3 Js. eX C 00 O3 CO CO CO Cύ CO CO CO G0 CO Ni Ni N0 Ni IO Ni N0 IO Ni N3 rθ Ni Ni Ni Ni O sj ro CD C_n Js. J2. G0 IO Ni -s -s O O 00 C0 00 00 S S ro oi Js. j2. 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S ro O ex 42- Oi JS. __. 3 o os to js- co ro io co oi co ro s 03 oo ro cn o co NO o O Ol o NO 00 S J. O CJl JS. O NO Js o co cn O s ro n S. 3 " " s s ro cn js- js. ro cn Ol l Ol CJl cn cn J. J. J. JS- Js. JS. J js. JS- Js. -fc. •fc. -fc. js. J. J- ro ro ro cn oi Js j- j- j- co co co to co CO Ni M o CO eo 00 S s oi CD Ol Ol Js. Js. Js. co CO Ni M _-s O o s ro to ex -s co cι co o ro js. o s o CO Js. co s o 00 Js. J. Ol Js. O -s J2. t0 O 01 C0 03 S -s JS ex ro cn si -s ro s. o cn O o ro 42. 0 O . O -j n co co oi Ni NJ O Ni l CD o s 00 S J . 00 CO _-. Oi cn o o 1 to ro o s -s o si co o oi j- io o o o -s c cn 00or 3 S JS. sl 42s 00 ro CO ro — s -4 CJl ro O CO CO — — o o oo O sl CO oi O CJ s o J O s o _-. 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J_ CO CO CO CO CO CO GO CO GO tO Ni NO NO NJ fP Ni Ni Ni NO NJ NJ NO NO Ni Ni Ni ro ro ro oi oi oi 42- 42- 42. CO IO NJ _i _i _s o o o o o oo oo s s s o o o o oo oo s s ro ro -fcs co co iO o o O OS OS s s Tl O CO cn co S CO o 00 00 cn s CD co o ro o ro o s No ro co -s ro o oι fo ro o s j2. s JS. JS. S CO -S O1 CO -S -fc. Js. 00 o o 00 ro JS. OO CO CO Ol O -s CO JS- GO -s OO IO O CO CD -s ro ex ro o cx -fc- ji- s < c° Js. O Ol -s Ol Ni CO Ol CO ■fc .- S 42- ro n ■ j_s*. ■ ro NJ oi o IΌ co o -s NO CO NO Js. O CJl -s o cn ro o ro to -s o ro to oi iO s ro o s IO O NJ Ni Js. S Js. -fc. 01 IO IO - I . !O - S O -s S ro cji -s s to s 3 J-. J_. J J_. J_ J_ J- J- J-. 4-. eLO CO CO CO CO CO CO CO N0 Ni N0 Ni IO IO Ni lO tO IO N3 tO N0 N0 IO NO 10 s ro ro ro cn cn 01 Js. j _s_. C-_O. N..i. -s -s -s o o o o co oo co s s s o o o o co s s s ro ro js- co ro -s -s O o o 0000 s s o ro co o cn co o ro w o co co o s ro -^ O NO o to o ro iO cn co o co oo cn io ro cx ro co ro _. o_ Ol -fc.00 Ol GO fc. o co o - co ro o 10 " o S CO S CO s - •fc -. o ~ 0 " 0 " 00 O 03 S JS. -S -S |O Ol 4S- -s -_ CO -fc- CD -s ' 0" n 1 — - ron r0n0 ____ n ono ssi ro oo ro sj co Go ro 00 ro ro s - o o oo o co oi oo s -s ro iO -s co ro •fc. lO Oi oi oo ro oi -s o co oo o fp co co o cn 03 00 00 O ro -s ro j2. cn js. oo s O ~ Ϊ JS. CO O CO O S o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o cx cx oo co oo os oo oo co ∞ oo co co co oo co co ∞ ex ex ex cx ex cx oo ex co co oo ex cx ex cx cx ex co co co co oo co co oo co co ex cx ex cx ∞ o o o o o o o o o o ex oo ex cx co cx ex cx oo ex s s s s s s s s s s ro ro ro ro ro cD ro ro ro ro cji cn oi oi oi oi oi oi oi oi m o co s ro -oi j- co NO -s o o oo s ro cn js. co No -s o o oo s ro cji j_ co ro -s o o ex s ro cn j_ co M -s o o cx si ro cn js. eO M 2 T 1 o _ " D z O CΛ - co co co co co ω co co co co co ex ω Go ex ω oi ex co co cAi co co co cjo co cjO CO Gi Co co co co Go ω os o rπ oo oo ∞ ex co oo oo oo cx oo oo co oo oo co co oo co co oo oo co σi co oo oo co oo co oo co co oo cx co oo cx cx oo ex ex ex ∞ § 5 KΩ '" z O Ni Js. s o O O 7os CO CO ro — — s — s _s —s _i Oi Oi Oi Ol Ol Oi Oi Oi Oi Js. J- J_ j_ J2. j_ 42. o o si s ro CJI oi 4S. -fc- GO CO Ni Ni Ni o o o o o o oo ex ex ro ro oi oi - o _ ro _. CO CO Js. O S CO -s c o. s r o js O s _ c . Ni -s s . r -O- -O- S S NO o-o- ro- -S to js. Ni CD o oo co oo co co ro oo c - _o_ r n J .s. c -_ - n 4S - o -s cn c -f o 0 o s ro o oo ro -s o s CO Ni o oO o-si -s O O NO co o ro c f O O o s ji. O rO O O CO C -fc. NO -s έ§^ cn s CO^ Js. OS o o o js. ro o o oo co js. c ι oo ϋi o co ro co ro s ro s s -s o -s o ro co j-s -fc. to - --f^ r cπocoooo ro co CO Ol oi ro to o cn oos cns to ro ro o o s 3 NO NO Oi J2. J_ J_ J- Js. J_ o o oo s ro cji e-n oi j- co co io Ni Ni NO -s -s o o o o o o ex oo ro ro oi oi oi j- j- f _... .. Oi Oi Oi Oi Oi Ol Oi Oi Oi P^ NO Ni NO Ni -. -s O O O OO CX CX S S cn -s co co iO oo j2. -s oi oo iO O si co -s oo ro ro -fc. -s CO NJ O eX CJl S NO S -ls- O CX Ni - _fc_- Ol CO •fc. o o ro co oi oi -s s -s io -s co cn -s oi co oi c iO O IO -s O O -s OO IO O Ni 42- 00 -fc. -s o oi co o j2. o <x s -fc. -s ro co o oo j_ ro co ro s No ro js. o o oo _s ro s oo oi j- ro iO NJ O CO S Ni CO O -sJ O S ro o IΌ o Ni co Js. CO S SJ 42. S --. OO O O GO CO S Ni O js. ro si oι js. o o ro *^- cn j_ s o oo si o oooo oooooooooo J_ J- OoOooO OoOooOoOoOoOoO m oo o oo ro 2 Tl o * ■ ' -s rπ o o co co co co co co co co co oo co co co co co co co co 00 co co co co o ex 00 oo ex oo 00 oo 00 ex 00 00 00 ex oo ex co 00 00 00 oo 00 00 00 00 03 00 00 00 00 oo co 00 00 00 00 00 00 03 03 00 03 03 00 03 3 D z O Ni to Ni ro Ni Ni Ni ro Ni ro IΌ Ni NJ ro to Ni to Ni to to to to IΌ to IΌ ro IO Ni fc S. fc c 42. fc 42- Js. fc JS. fc s 42. Js fc J fc s s S s s s s 5 s_ to ro f s s s s s s s s s s s s s s s s s s s s s] s s s s s s s s s s s s s s s s sl s s s s o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o υ C o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o CQ Ul Ui o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o oe r; 7s 7s 7s 7*-: 7s TC TC TC 7s TC 7s 7s 7s TC 7s TC TC 7s 7s TC TC 7s 7 * . 7s 7s TC C TC TC TC 7s 7s 7s TC 7s TC 7s TC 7s 7s Ts Ts Ts TC Ts C 7s 7*; C o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o co co co co co co co co 3 ro co co w co ω co co co co co Go co co co co co GO Go co ex Go co ejo co co co co co co oo co Go co co co co co ω 03 3 ro Ol cn cn CJI Ol CJl -fc- 42- S- 42- J-s J2. J2. .fc. -fc- Js J_- J_. J_. 4_. CO CO CO CO CO CjO GO CO CO CO CO CO CO CO CO CO CO GO CO CO CO CO Co rO Ni NO Ni Ni Ni IO to to Ni o o OS 00 ex s ro ro n js. GO CO IO O o "o o~s ~ oo s s ro ro oi oi js- j-. J2- Js. GO CO CO Ni Ni Ni . o _ o —i js. js- co ro o — o e» s Oi to Ol — - Oi CO S cn o oi o NO o o S Ol o oo S CO o oi o ro co o oi o_ ro- Js IO 00 .fc- -s 00 Js -s Js. ro s ro co oi ex ro O CO co J oo NJ O 00 s -s NO -*• o o O O ro ro s s o co o CD ro -s s - ro - C -D Ni o ~ _s cn ro o cn oo _n o_ 00 O -fc. O CO CO CO ro o o sl CJI o o 42. 00 O o cn ■fc. O Ni S -s O o o cn o - j - o ro o Js NO Ni Ol CO O O O 00 _s -s Ni oo s s s NO Ni Oi ro ro s 3 Ol Ol Ol Oi Ol Oi Ol J- J-. J_. Js. J s . 42- J_ JS. JS. J_ Js J_ co Cjo ω co co ex co ex eji e^ co co co ex eji co co co co co co co oo co io NO Ni NO Ni Ni o to Ni -s o o o o ex oo oo o cn co co NJ o oo oo s s ro ro ro cn c ι j2. j2. j- js. co co co ro Ni Ni -s -s o o cn js. co co -s o CJl O S Js S s s s ro r IΌ ro iO O — s - o_o. cχ j- cχ j- -s s cn ex ro -fc. o cD -ts o s Js. -s co j-s o ro js. ro o o o cx s .o_orosO .o O _sl _ c_nO .o_i l O .ro ' _. s - s s -s js- o to oo . oi ro o oo ro co -fc- Ni oi io c roD ss ro cx o o ro o s ro -fc- -s cD O J2- js. js. js --s ro js. ro oo cD co o co GO Ni Ul S C0 S S 0l J2. Ni CD l C0 tO O 00 C0 C0 S - — C —Jl Cn θ sl -s -s |O O 03 O tO -s |θ σi sJ J_. S -s C0 C0 f C0 00 C0 CD CX rθ o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o ex 03 00 00 oo 00 ex oo o 00 sl ro cn 42. 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J_- J2- Js cn C» CX O O O M M M C0 C0 C0 J- Js. ι ro 00 O O o_ι rr _ O f0 c_ on rc-o_ eoo cc _ -s ._ N._0 Ni G0 C n c0o Jjss.. Jjss.. Ccnn θolι Oθlι Ooιl CroD Ce_DD SS SS etX C0 C N s r x co cXo Oo --^s --ss ioj roro ss co o o o o — CoO — i no fjj rn — i ύ si e o- > r _jni. nc-.oo. roro_. i _ _-__>i roni oooo rcoo iNsii _J_s_.. o iisOi sSi iNsii ssi —- ss rc_o3 ecnn ron ιrsoι 4j_s-. coj ssi c o_. ifsoi ssi _-fc__-. __s_-. rron rron —-ss co_ni s js. ro o to O O CO o -_ C_JI. o_- s - o«o- j -s. ro — -ro- Js. <-n co o co ci Ni Ni CO J- ro -s ro ro co ci oo oi iO js- ro co co js- ro oi ro co js- ex s -fc- -fc- ro -fc. ex s lO Ni co o co ro oi o NJ Co co -s ro ro cx o ro ci o o o co ϋi o No o co o - - o -_ ro j2- o ro oo fo oi ro cn oo ftO Ni oi oooooooooooooooooooooooooooooooooooooooooooooooooo CA 0 oooooooooooooooooooooooooooooooooooooooooooooooooo A3 m J_ 2- ^ j2. J2- J_ 42- 42- Js J2. 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JS Js Js 4i Ji 4i -fc- 4s 4s 42- 4s. 42. s js js js js js js js js js js js js js js 4s 42- 4s js 4i js 42- 4s. ji Js. js J 2. σ CΩ z o cn ro ro s s cx oo o o Ni Ni S IΌ OI IΌ JS CO S O CO r oo os _os -Nsi c_ns _ss t-o. ι con ccon -ofc. Jjss c-ns ro-s or s s cn oo co ro co co o oo i s iso sjs o c-os cox o-s oio os O C0 00 IO 01 O1 4-S - S O (X -s js o js s ro ro o Js -s oo ro cn ro o o s s co s ro Ol S -i O IO O O CO -s -s Cύ Js OO O CO -s tO Ni O CO IO 4s. cn oi ro ro s s oo ex o to ro ro ro ro ro to ro ro ro ro ro ro ro iO to ro ro io co cn o 4s. oo ιo o co s cn o o o *_. -_ -- -_ to co co 4s 4s cπ ro s s s s co co o o o Ni Nθ co co Gθ 4s oι oι ro s si ex oo o •fc. -s io --s ex s co co .fc. O CO S O C0 01 S -- S - S S 1O 0 42. 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S 00 Cn S O G0 CD f0 CD S CD O C_04S. CD eX 0l S O -s |O Ol o --s js co o o o ro 8 00 fc CD 00 IΌ S Ol s -s o oι s iO co co 4s ro co js o s ro -s s ro -s io cπ oo oo -s cn co js -s co s co 4s. cx c S O O CD 00 o o w iO si cD ro -fc. -si s ro o ro cD ro ro cχ js o fP Co co co ϋι iO No cn cι ro ro Ni θ3 ro oι -s oι o 3 ro s si 0000 o o Ni Ni Ni Ni Ni Ni NO NO NO Ni NO Ni Ni Ni NO NO Ni Ni NO NO CO CO CO CO GO CO o o cn m θ io Nj ω co s 4s cn ro ro ro s ex cx o o o o NJ Ni Ni -fc. Js 42. Ol Ol cn ro ro r s 000 eo CO 0 0 0 O -s to GO ro s -s IΌ - _ N3 O 3 JS 0) -. C 00 -i ■fc- CD CO S tO -fc- Ni ϋl CO Ol CO Cn S -s ϋl CO 0 Js 00 -s Js o CO s 000 CO J ro IΌ Oi 00 -s 00 IΌ sj r - ro N o s CO s s — ro -s 0 Js o Si S Ni n Kj co -Jfe - - Q _ _ J.s s oo ex o ro co -s -s -fc- oi o oi s s oo cπ M s 0 co cn Oi cn c S CO O Js ro S -fc. 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CO ιo -s o o co si ro cD Js- co iO -. o o co s ro cn 45- co Nj -s o o oo s ro cn 4s ex iO -s o o oo s cD cn 4s- co ιo o Tl o α z o CΛ ,-s rn O Ω JS Js 4s Js Js Js Js Js Js Js Js 4s Js 4S 4s Js 4s Js Js Js Js Js 4s 4S 4s 4S Js Js Js Js 4s 4s 4s 4s Js 4s Js 4s Js 4s 4s Js Js Js Js Js Js Js Js Js 00 00 00 C0 C0 00 C0 C» CO 03 00 CO C» CO OS C» 00 00 C» CX CO CX CX CX CX (X 00 00 CO 00 00 eX CX 00 03 00 00 00 CO 00 00 00 00 03 00 00 00 00 00 CX ID CΩ ' Z o Ni Ni NO Ni ro ro to io ro to co co co co Go co co GO Go co -s Ni NJ CO js js ro si -4 O NO -fc- Js- cn cn ro CD ro si io co co co Js Js cn Ol CD S OO O o i OO CO GO Js Js cπ ro Tl CO CO 00 03 •fc. o or -s o lO o fp si ro o - cn o si Js CO s cn -s js CD p ro ro <x -j. --s cn js ro -s -s lO NJ fO N O CD S C CD O CO -sl o rO Ol S -s sl s cn co co iO CsO Ooil O W ro io ro c -s Cn NJ Co ro W - S js r coj. fS e r_nπn C rrθnn J n r ronsn mmoo co J Ss -Ps θ isiι _ro NJ co -s o NO N j o ro co ro o oo CjOs . c r^nn oN moJ cJ ros.i o ecno j rons c- J fcos- o r∞n S V° ro σi S e_π - —i s S ι~o ≤ js S ui ω> ro. co ro co - to _ Oi oJ CO N isji 5 co o js s co co ro oo ro co iO ϋi s -s 3 CΛ O Ω Js js Js Js js 4s 4s 4s 4S js Js Js Js js Js Js js js 4s 4s js 4s 4s Js js js js Js Js 4s 4s Js Js Js js Js js Js js Js Js Js Js js Js Js 4s 4s Js Js o — o o o o o o o o ex ex cx cx cx oo oo co oo oo cx oo co co co co cx cx oo co co cx oo oo oo co oo cx oo co co oo oo cx co oo oo oo co rø 5. σ CΩ ' Z "-" O o vo ω ω u ω ω ω u ω ω ω ω ω ω ω ω ω ω ω ω ω ω j ω ω ω c ω ω ω ω ijj ω ω ω w ω ω ω ω ω w ω 03 3 ro co co ro Ni Ni l r isi -— Ni Ni CO CO CO js js s oi oi oi ro ro s s o o __ _s -_- _s _s _s _s _s _s _-v -_ _s _s _s _s _s _s _s _s __. _s K s rso rO Js -s D ro Js _s rs r^ o o ro o co ro -s js oo o oι o _s s _s o o ro o o o o -s iO Ni Co co co js cn oi or s s s s o o o o o -s ex o ro s -s -s js oi ro o iO js cD Co cn co o ro cn co co cji s co s o GO Go o cn o Js cD o co ro o co co js js co ro s. si |sj C r N) ^* j_. j_, __ ζ - js s co ro o ex s NJ Oi o oo oi No -s -s co o co o -s ro ro o s s ro si co cn ro ro o cD Go oo - s o js ro ro js o ro o eji oi s oi O Go s si js co ro s ro o NJ Go oo 3 Js GO CO NJ Ni N r s sl O o ro o o ro js oo Ol sl NO Ni CO GO CO Js Js cn cn oi ro o ex co s ■ o — J o O O O -s Ni NJ CO co co 4s cn oι ro ro s s s s o o o o -s CO s o to S CO Ni O O CD O S O c-o- o-o -ro ro coJ roJJ ro co cn — - ro s o *_J o •— * sj - -iιs_- c sni io j ■+s— ro o Js s -s oi Ni to co o JS - S s ex en ro en s " ro _ s cn s cn rή rn o rTi c rn.i c rxή o *— ' U to o co Ni o -s o ex ro ro cji o S _ S-. K_. r_^. r_.n. NO Cn JrS CO ro CO -s O CD S IO NJ O S OO CO Cn O OI O 1O G0 CD O 4S O O s co -s co cn co oo ro o cn ro ex Ω 00 CO 00 o cn oo s ro j s s s Js Js Js J Js Js Js J J. Js J J Js Js Js Js Js Js Js Js Js Js Js Js Js Js Js JS Js Js Js Js Js Js S Js J s Js Js . 4s Js Js Js Js O O O O o 0 0 0 0 0 0 0 O 0 0 0 0 O 0 O 0 0 0 0 0 O 0 0 0 0 0 O 0 0 0 O O Ni Ni Ni ro Ni NJ Ni ro ro NO ro ro 10 ro Ni Ni Ni Ni ro Ni to Ni Ni NO O to Ni to to Ni to to ro NJ ro ro Ni to Js JS Js Js J Js s Js fc - s Js J fc Js JS Js JS Js J Js Js Js Js Js J -p. Js fc Js Js Js J Js -fc. fc Js fc Js Js Js JS fc -fc. Js fc 45- fc s S S S s S s S S s s sl S s s S S S S s S s s S s S s s S sj S S S S S s s s s S s S s s s S si S S O ro ro ro Oi ro ro ro ro CD CD ro ro ro ro CD ro ro ro ro CD ro ro ro ro ro ro ro ro ro ro ro ro O ro ro ro ro ro ro ro ro ro ro CD ro ro ro ro ro ro ro ro ro ro CD ro Oi ro ro ro ro ro ro ro ro ro ro ro ro 3 o o o o o o O o o 0 0 O 0 O 0 O 0 O 0 0 0 0 O 0 0 0 0 O O 0 0 O 0 0 0 0 0 O 0 0 0 0 0 0 0 O 0 O 0 0 (O 6 _ ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό ό 6 ό ό ό ό ό ό ό 6 ό ό ό oooooooooooooooooooooooooooooooooooooooooooooooooo z 3 eo eo CO CO eo CO CO eo CO CO CO CO CO CO CO CO en CO CO CO CO CO CO CO CO CO CO CO CO co CO CO CO CO CO CO CO CO CO eo CO CO CO CO CO CO CO CO CO CO ro Tl CO NJ NO Ni Ni Ni NJ Ni Ni Ni NO Ni NO Ni Ni NO NJ Ni NJ NJ NJ Ni NJ Ni NJ NO Ni NJ Ni fP Ni fP 3 3 ro CO j Ni N sji — - - —s . O _ u- O O s el 01 Ol -fc. Js C0 C0 tO Ni N0 N3 f M O -J 1 - 1 co o ro ro o o o o oo oo oo s s ro ro ro oi oi — e -Ts O - r —ή reX -ή S - i S S - 0-0- — oo co o ro co s co o s oi io o -i fl oι _- o 4s. to s -fc. o ro co ro co W rn s i 1Ϊ 1 ri r.i en c -n' j +s-- ■ —- co ro ro *i co j. -s o co --s o ro ro o iO -s SJ ^J g g ^ g r c o oo s ro oro sseroxooro COroCOroJsclosOcOosCX _ -ts c_nπ _-p_- c_o_ ito ^ ro° -*s 3 σ ϋ 3 i s oOi o ϋ1 o c Oi -s s o ro oo ro -s co o o ro co CΛ Go co co co co co co ω cx co co cx co co co co co co co ex ex w co Gύ Go Go ω co co Go co co co co co co co co ω O cn oi oi ro oi oi oi oi oi ϋi oi oi oi oi ϋi oi oi ϋi oi oi oi oi oi oi oi oi oi oi oi oi oi oi oi CD CD CD ϋi oi oi CD cn oi oi oi ϋi oi oi oi oi oi -n m o o o o o o o o o o ex ex ex co co co co ex ex oo s s s s s si s s s s cD ro ro ro ro ro ro ro ro ro cn oi oi Oi oi oi oi oi oi oi ^ D o oo s ro cn s. co Nj -s o o ex s ro cn ji Co ιo -s o o oo s ro cn -fc. co Ni -s o o cx s ro cD 4s co No ^ o o co s ro oι 45- co NJ -^. o sU CΛ -s rn O Ω 4s js 4s js js js 4s 4s js 4s js js js js js js js js js 4s 4s js s 4s js 4s. js js js js js 4s 45- js js js js js js js js j^ ^ -fc. js js 4s js s js o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o § 5 CΩ ' Z fc? cf ro Ni ro ro ro NO to ro NO NO NO NO Ni Ni NO NO NO NO NO Ni NO NO Ni NO Ni Ni Ni ro NO to Ni ro ro ro ro ro ro NO Ni IO NJ Ni Js Js? J Js -fc- Js ■fc- Js Js Js Js Js Js Js Js Js Js Js Js Js Js 42. J. Js J Js Js J-s js J JS Js Js Js Js JS S J fcs? J fcs 3 fc fc fc Js? fc JS 3 Js Js J Js Js JS Js S sl S sl s s s s s s s S S s s S S S S •si s sl S sl S S S S S sl S S sl sl s s| s sl S sl sj S sj s| S s s sl S S o ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro CD ro ro ro ro ro ro ro ro ro ro ro ro 0 ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro CD ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro 3 o o 66 O O O OOO O OO O OO O OOOO o o o o O O O o o o o O O O O O O O o o o ep ep o o o o o to o o O O o o o o o o o o o o o o o o o o O O O O O O O o o o o O O O O O o o o o 66 o o o o o o o o O O O o o O o o o o O o o Q o o O o o o o z 03 3 Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ ro T| ro ro NO ro co co co co cx co ex ex co co co co co co co co GO Go Go co co co co co co s 3 ro i ■_s_Jι O Ni S Go co co co Go co co co co co ex co ω co co ex co co co ω co co co co ω co co co co co co co co co Go co ω o to ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro σ m j. ^ 4s 4_ ι_ j- j. ^ 4s j> c ω ω ω ω ω ω « ω ω M M M N3 M M M i>o M -ι -i j -ι -ι -' ^ -' -» -i θ θ o o o o o o o o Ϊ o ∞ s ro cjι s co M -s o o cx s ro cD Js. co ιo -s o o oo s ro cn Js co N -s o o ex s CT cn Js co M -s o o oo s ro oi Js. co iO -s o T2l Ω __ 4s js js js j- js js js js js js js js js 4s 4s js js js js js 4s 4s s js js 4s 4s js 4s js js js js js js 4i js 4s 45. ji j^ 45. 4s js js 4s ^ O O O O O O O O O O O O O O O O O CO O O O O CD O O O O O O O O O O O O O O O O O O O O O O O O O O O 03 CO CO CO CO GO GO GO CO ω CO CO CO CO CO CO CO CO CO GO CO CO GO eX CO CO GO CO CO tO Ni NO NJ NJ NJ M NJ NJ NJ Ni NJ fP NJ N^ 3 ro j Nsi Nroi Noi ccoo cooo jios cooi soi rooo s s . e_x e_x c-x -o . o . - js js cπ oi ro ro oo oo o o o o -s Cn S NJ O l lO S O CD O rn o ex oi oo -s J o o s- - -- .- . o 010S0 oJ s o O C ro 00 s o co o oi -s js co ex ex io oi ro o co oi js ro co ro to o o o 00 o sl o to co si Ni S 3 Ni NO Ni No co co oi cn cn ro s s co co o o O fO Ol S Js. O -s 4s OO O -ts OO IO S O CD O ■fc. -s cn oi 4s ro ex -s co cD J- CD S s cD Js. s S si oo j- o -s e -x- c-n ro- c-o o-- n ro ex to co co cx co co co co co co Go co co co co co co co co cx co co co co co co co co co co co co co ex co Go ex Go co co G ex n to ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro ro o o o o o o o o o o ex ex tx co co cx ex cx cx co s s s s s s s s s s ro ro ro ro ro ro ro ro ro ro cji cn oi oi oi oi oi oi oi oi o os s ro eji -fc. co M -s o o oo s ro e-n js co iO -s o o ex s ro cn js co iO -s o o <x -s4 ro cn 45. ex Nj -s o o o3 -si ro cji js GO Nj -s o 2 τι D __ CΛ -s rn O Ω cn cn cn cn oi oi oi oi oi oi ro oi ϋi oi oi oi cji cn oi cn eji cn oi oi oi oi ϋi ϋi oi oi ϋi oi oi oi ro oi oi oi ϋi oi oi oi oi oi oi oi oi s js js o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o § 5 CΩ Z o Ni Ni Ni Ni Ni Ni NJ NJ NO NO Ni NJ Ni Ni Ni NJ NJ NJ Ni Ni NO Ni Ni NJ Ni Ni Ni NJ Ni Ni NO Ni ro NO NO NO Ni NJ ro ro NO Ni ro Ni Ni Js J- Js Js Js Js Js Js Js JS js Js Js JS Js Js Js js . Js Js Js J Js Js -fc. -fc. Js Js Js Js JS JS Js js Js 45. J Js fc J? fc Js? fc J 3 fc Js? J Js J J J S sl s s sl S s s S sl sl S s s S f Js sj c s| S 5 sj s| S sl S S S S S S s| sl sl S S sl sl s| SI sl S sj S sj S S sl S S S sl Ol Oi cn oi cn cln Ol Ol CJI cn cn cn cn oi CJl CJl cn Ol cπ cn cn cn Ol Ol cn cn cn cn cn Ol CJl cn cn CJl Ol CJl CJl CJl CJl CJl όl JI CJl CJl Ol CJl Ol ro ro ro o o o o o o o o o o o o o o o o o o o O cp Ω o o O O o o o O o o o o O O O O O O o ep ro ro ro 3 o o o o o o 66 o o O O O O O O o O 66 o o o o o o O O O O O O O O O O O O O O OOOO OOO O OO (O o o o o o o o o o o o o o o o o o o 66 o o o o O O O O O o o O o o o o o o o o o o o O O O O O O O Q i Ni r oo o Ni o NJ o NO o ro o ro o Ni o Ni o Ni o Ni o Ni o Ni o o Q O O Ni NJ NJ Ni t Ni IO Ni Ni NJ Ni NJ NJ Ni Ni ro ro r oo o NO ro ro Ni Ni ro ro ro to Ni Ni o Ni N oJ o NJ o 03 N Ni 3 φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ φ ro CO CO CO CO CO Ni Ni fP Ni NJ Ni NJ Ni Ni Ni NJ Ni Ni NO Ni Ni NO Ni Ni Ni NO 01 GO CO CO 3 ro con co co co ci Co co co co co co co co co co co co ex co co co ex co co co co co co co co ω co co co co co co co co co co ω O CA S S sI S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S sl S S S S S S S 4s Ji 4S 4s Js Js Js Js Js Js CO CO CO CO GO CO CO CO CO CO N Ni Ni Ni NO Ni Ni NO N -s -s -s --s -s _s _s _s __ -_. o θ O O O O O 73 m Ω o ∞ s ro cD js co ro -s o o oo s ro cn js e^ Nj - s o o oo s ro cD -fc. ω to -s o o <x -sj ro cn js co Nj -s o o cx s ro cD . Go iO -^ Tl ϋol Ool Ool Ool Ool CoD CoD Ool Ool Ool Ool Ool Ooi rooOol Ool Ool Ool Ool OoI Ool ϋol CoD Ool CoDoCnoOloϋloOl OoloOloOl OoloOloOi roσOoloOloOl Ool Ool OoloϋloOl OoloOloOloOl OoloOl ro o IO NO Ni Ni NO Ni Ni Js Js JS. Js JS Js Js Js Js cf J?s sl sl sl S S sl sj S CJI όi cn 01 dπ CJI Ol l CJI cn o o o o ep o o o o o o o o 66 o o o o o o o o 66 o o o o o IO N oO o Ni o Ni o Ni o NJ N3o Ni Ni o Ni φ φ φ φ φ φ φ φ φ φ Tl CO CO CO CO CO CO GO CO GO GO CO CO CO GO CO GO CO CO CO CO CO 3 3 ro co co co js oi ro ro ro s s s s cx ex oo o o o oo oo s ro ro ro ro cn Js Js CO co NO NO Tl cn s o j- ex -s s s o iO Oi o io ro o to oo 0 -s -s -s tO C J5. 45. 0l Ol cS S sl cD IO s cn os -fc cn -s o oo oo iO S O o co ro -s cn ex s ro -s s o ro — ~ n ~ ~ ∞ o s o -s cn io o o ro UJ tcoπ cCO ~ 2 o -l "- s c ∞ — ro - ro s oo t s —_nπ & i rIΛ.i OmJ 1 ^ ώ -- - icnn r sό ro co υ n l ssi rυn rv-. r.i ro n soi crx.i j- o cn -s o -fc. - ι uj w ιu υι si yj \ -s o ro co o ro θ -s G0 IO Ji CD Ji Cn -s 4S. CD O O Js Js S co o -s to -s o s ro ro co co f - s iS - '^ σi -'s.∞co o ooe-n s oo - o IΌ S ro 3 co Go co js oi oi ro ro ro s s s ex cx ex cx o o o ex cx cx s ro ro ro ro cn oi js co co co Nj co cn s o co oo ro Js. si o co s o s s o oi oo ro co co js js oi s s si ro ro -s o Oo Js co cji cn s -s ex cx oi cn co o -s o oi co o ro o co o cn — - o H ro ex cn ex s o Js CD o o cn ex ro co -s ro o Js o co cn J jSs. ccoo cx cD __. θ 45. -s -s ro js o co o J5. o oι --s ro cπ oι -s ro ro s ex ro s o o ro ro ex s oo js co cn S 4S. O Js Ni ro S C JS O S -s 4s ro O o co cn s o o oi o ro co -s co s cn -s co ro o o cn ro o ro cn js co io js s oi o s 13799 13978 A co co co CO co co co co co co co co co co O C s s s s s s s s s s s s s s s s s s S s s s s s s s s s s s s s s sj s s s s s s s s rn o o o o o o o o ex ex 00 ex oo (X ex 00 s s s S s s s s s s ro ro ro ro ro ro ro ro cn cn Ol cn cn cn cn Ol Ol Ol 73 D s ro cn •fc. o o ex s ro cn J. co ro o o 00 s CD cn J. ro o ex s ro cn JS o o 00 s ro cn l s co to o T 6 z o CA m o D cn cn cπ Ol cn cn cn cn cn cn Ol cn cn cn cn cn Ol cn Ol Ol cn cn Ol cn cn cn cn cn Ol cn cπ cn cn cn cn cn n cn Ol cn cn n cn Ol Ol Ol Ω o o o o o o o o o o o o o o o o o o o o o o o O O o o o o O o o o o o o o o o o o o o o o o o o o 3 6 CΩ' Z o ro NO Ni Ni to NJ Ni Ni to to IO to to Ni Ni NO NO to to to Ni to NO ro ro Ni Ni Ni Ni Ni to to ro Js 4S fc fc Js Js Js Js Js fc Js Js Js fc Js Js Js fc JS Js Js fc Js Js J fc J -fc. Js fc JS fc fc s Js fc fc J J Js Js Js Js Js s s s s s T 1 s s s s s s s s s s s S S s s S s s s s S s s S s S s s sl s s s 5 s S s s S S s s s s s o Ol Ol Ol cn Ol Ol cn cn cn Ol Ol cn cn cn cn cπ Ol Ol Ol cn cn Ol Ol Ol cn cn cn cn cn Ol Ol cn Ol cn oi cπ cn cn cn cn Ol Ol Ol Ol cn cn Ol Ol Ol cn o o o o o o o o o o o o o o o o o o O o o o o o o o o o o o o o o o o o o o o o O o o o o o o 3 o o o o o o o o o o o o o o o o o σ O o o O o O o 6 o o o O o o o o o o o o o o o o o O o o o o o o CQ άόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόόδόόόόόόόόόόόόόόό OOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOO z rO IO IO IO rO M N3 IO Ni lo rO Ni N3 IO W ro iO IO IO rO tO tO NO NO N3 Ni NO Ni Ni N3 NJ N3 N^ 3 CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO CO eo CO eo CO eo CO CO eo CO CO eo CO CO CO eo CO eo CO CO eo CO CO CO CO CO CO CO CO CO CO ro ro co co js js oi oi cπ s s C0 orCn o00 Oco js i0o0 JJss Ooo oIO 45. cn o ex NJ co lo c uo co j -*—s j ->-s. j ■ »+s— cN —n 3 i cc • _nn/ 1 rooo sw si oo s/o j ro - t-o o cn SM-. rwn ^ _ N_J_. 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CO CO NJ NJ Ni CO CO js Js Js cn f_i fn ~si CO Cn CO O OO -s Cn s s co ro ex co Js oo co __ o i ro co o -A o o CD cπ Js oo CD to o S -A O 00 r o js s o S _ _ M 03 Ol N3 W -i ■ j+s_ —_A ' o Ss| ( ojoi ucni Wco Wco ro /ro. c o j° o s cn ro oo o ex s ex ro o co ro s o oi js Js o o +- ui iv w UJ j i j yj i Nvj uroi cn e uxj o v_/ _- r. s cn -s ro co co N W W (D M W S W N3 0 -A js cD js js cχ js co co => oι co oo co ∞ _s o ro js cn oo - μ ' co ro O N3 0) U1 0 0, ω oo co js co o -s o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o n to s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s s o o o o o o o o o o co exoo exexcxexex cx ex s s s s s s s s s s roro ro rororo ro rororo oi ϋi oi oi oi oi oi oi oi ϋi 5 O o oo s ro cn -fc. co ιo -s o o c» s ro cD -fc. co iO -s o o co s ro e-π js co ro -s o o co s ro cn -fc. co fo -s o o oo s ro cn js cύ ro -s o Tl _ D Z O CΛ — m o o oo cx cx co co oo oo co co oo cx co co co cx ex cx oo oo ex cx co os oo oo co ex cx oo cx oo oo oo ∞ oo cx co co cx ex co oo oo cx co ∞ co co oo ex ex cx oo cx cx oo ex cx oo co co ex cx co co cx oo co ex oo ex cx co co co cx oo co s s s s s s s s s s s si s si s s s si § 5 CΩ z o M M M M M M M M M M M M M Js to NI M NI M M M M Ni Ni M M Ni M Ni M NJ NI M 45. 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247-15-0-2L19.r1 -1 3330 3034 20721 98 247-15-0-2L.19.r1 -1 2370 2131 20722 98 247-15-0-2L19.r1 -1 2031 1552 20723 98 247-15-0-2L19.r1 -1 1548 1063 20724 98 247-15-0-2L19.r1 -1 945 598 20725 98 247-15-0-2L19.r1 -2 4097 3924 20726 98 247-15-0-2L19.r1 -2 3719 3558 20727 98 247-15-0-2L19.r1 -2 3119 2874 20728 98 247-15-0-2L19.r1 -2 2480 2304 20729 98 247-15-0-2L19.r1 -2 2144 1983 20730 98 247-15-0-2L19.r1 -2 1727 1569 20731 98 247-15-0-2L19.r1 -2 377 90 20732 98 247-15-0-2L19.M -3 4096 3917 20733 98 247-15-0-2L19.r1 -3 3667 2153 20734 98 247-15-0-2L19.r1 -3 2101 521 20735 99 247-57-0-0N10.S1 1 210 20736 99 247-57-0-0N10.S1 214 477 20737 99 247-57-0-0N10.S1 580 1068 20738 99 247-57-0-0N10.S1 1105 1305 20739 99 247-57-0-0N10.S1 1417 1611 20740 99 247-57-0-0N10.S1 1756 2139 20741 99 247-57-0-0IM10.S1 2161 2409 20742 99 247-57-0-0N10.S1 2497 2712 20743 99 247-57-0-0N10.S1 3226 3429 20744 99 247-57-0-0N10.S1 3871 4053 20745 99 247-57-0-0N10.S1 4093 4947 20746 99 247-57-0-0N10.S1 5065 5244 20747 99 247-57-0-0N10.S1 5257 5580 20748 99 247-57-0-0N10.S1 2 188 415 20749 99 247-57-0-0N10.S1 2 602 763 M NJ IO IO NO tO IO NJ IO lO IO NJ NJ IO IO ro rO IO IO NJ lO IO M IO NJ IO NO lO oIO NoJ NoJ IO N sooO IO IO O O O O O O O O O O O O O O O O O O O O O O O O O O O O o OOO O OO o o o o o o o o o o n to S S S S S S -4 S S S S S S S S S S S S S S S S S S S S S s s s s s s s s ss ss ro ors sro sro ros sro sro s s s ro rosros cn CD s CD C s s s s s s s o o o o o o o o o o ex ex ex ex oo ex cx cx ex ex D Ol Ol cn cn cn cn 2 o ex s ro o-i js co Ni -s o o cx s ro cD js co ro -A O o ex s ro cn ji CO No -s o o oo s ro oι j. co ro -A θ o 00 s ro Ol Js CO NJ o Tl Ω* ■ ' "" D Z O oooooooooooooooooooooooooooooooooooooooooooooooooo ooooooooooooooooooooooooooooooooooooooooooooooooo CO CO CO CO GO GO GO GO IO NJ NJ NJ IO Ni Ni NJ Ni NJ CO CO CO OO CO CO GO CO CO CO IO NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ Ni 3 ro co co JS JS 4S CD CD -S -— IO N0 Ni CX eX 4s CD __ fo -s -— NO NJ Js Cn cn js Js Js co CO CO NO -A -A cn oi oi oi Js Js js co io NJ -s -A _s -A S cn O tO -01 -s CD -s CO NJ -fc. -sl o ro eχ .- Ol r^ r rθ ro GO S OO CO S S Js - 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CD cn oo j5 . - A o o o oi ro ro ro os Ni -s o o os oi s s _s _s oo s s ro ro oi cπ oι js co co to -A -A θ o o o ro ro cn oi Ni Ni fO NJ NJ NJ Ni NJ Ni N3 -s -s -s -s _s JS CO GJ NO Ni ]O o ro o oι o J5. s cn -A Js e Jxs o CD s O ro to cn ro co S Js js co co ιso to -A -s _s o o o o o oo s ro ro co o -A ro to <χ js Js Js o CD S Ol Ni s o cD NJ Oo ro co ro -fcs o cD io o ro s JSs lO Js co o co cn o iO o o to ro -A Co js NO Js ro s ro to Js NJ o s co o co o ro ro s _s _s CO O CO S CO tO CO Js -A _A .fc. cD -A θ Cπ CO <X IO o ex c-n js cx s s -A o ro Ni co rp os to ro rp js s oi -A -s o io oi o ro -s ro ro o Js oi ro o o NJ Ni NJ NJ NJ M NJ M NJ NJ NJ NJ NJ Ni fO NJ NJ NJ NJ NJ NJ NJ NJ fO NJ NJ NJ NJ NO NJ Ni NO NJ NJ NJ NJ NJ NJ M fO rO IO Ni NJ n to ω ω ω ω ω ω ω ω ω ω u ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω ω c ω w ω ω ω ω ω ω ω ω ω ω ω ω ω c cΛ w ω ω ω o o o o o o o o o o ex oo oo os cx ex oo ex ex oo s s s s s s s s s s ro ro ro ro ro ro ro ro ro ro cD CD CD Oi cn oi oi oi oi oi o oo s ro oi js co M -s o o ∞ s ro cD js co rP -A O O oo s ro cD js co Nj -s o o ex s ro e-π js co ro -s o o oo s ro oi js co iO -s o 2 Tl Ω _ o z O CO r— rπ O Ω o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o o cx w co co co co co co co ω co ω co co co co co co co co co co co co ω co ω Go ex co co co co co co co ω ω co ω co w 15 CQ Z o CO CO CO CO GO GO CO CO GO CO GO 03 3 φ js cn oi ro ■ -fci—. 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ss s S S s s s S sl sl sl s| S s s s s S S S sl si s| 7^ S S s s sl S S S S sJ S S sl S S S O CO GO GO O CO o O O cb eb cb CO 00 ex co ex co co do ex ro ro ro ro ro ro ro ro ro J Js Js o eb 00 00 J oi o J JS Js Js js o <_n ύι cn όι όι cι όι ύι cn oi o o o o o ex ex oo cx co co oo oo oo oo ex 3 CD Ol Ol CD CD Js Js Js s JS Js s JS J js Js s Js Js Js σ o o © o © 00© 0000 ©0 ©000© 0 ©00000 © 00 © 00000 o o o o o o o o o o o o O O O (Ω oe O O σ o o o o oooooooooooooooooooooooooooooo o o o o o o o o o o X X X z o o o z o o z o o o o o z O ooo o o o z Z O oo O NJ N oJ o NJ NJ NJ o NJo NJo NJo NJ o o o o o o ooo o o P o o o 00 00 00 00 00 o fo o o o o o o NJ NJ NJ Ni NJ NJ NJ NJ NJ NJ cπ cn Ol Ol Ol Ol oi o cπ o o cn CD CD NJ NJ NJ NJ Ni NJ NJ NJ NJ CO GO CO CO CO CO CO CO CO CO CO 3 Φ s s s φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ co co eo co co co co co CO CO CO NJ NJ NJ co co co co ro CO CO NJ NO CO NJ NJ ro NO co ro NJ co CO CO to GO GO CO CO NJ NO CO CO CO NJ 3 Φ ex co o -s co CD s GO to CD CD s ro s -A ro co co s ro -A ro NJ co o CO O tO tO -A NJ OO CO CD ______ o S Ol NJ ro CO M JS s M 00 cπ js oo -A -A JS cπ _o oi co . __ co cso Jex- oJS o ex io ex o si co to CD O to NJ CO CO co cn js oo r o to ro co js I © o CO o S 00 -IS o cπ oi o co o s ro co CO O - co ro ex ro s 3 o cn GO e CD co con so oi s cn s Js JS -s CO CD S CD O CO -A -A cπ s ro s oo js CD O cn S CD Js S Ol co o to cjsn cooi roro o co cn oo S S 00 NJ NJ Ni CO CD SI CO S OO IΌ CD IΌ S Ni o ro i sl sl Ni o cπ ro -^ - N co NJ NJ NJ 00 03 g 00 GO -A Ol NJ 00 CO Js O o o S -fc- O CO O J- Ol O S NJ S NJ CD CO CD CΛ ss rπ O D rO NJ NJ NJ M NJ NJ NJ NJ NJ NJ NJ NJ NJ M NJ NJ M NJ fP NJ fO IO NJ NJ NJ M NJ M M NJ IO M M NJ M NJ M NJ W W NO M CD -fc- Js Js Js Js Js Js Js Js Js Js Js Js cύ CO CO CO CO CO CO CO CO CO CO GO eX C IO NJ NJ M NJ fP NO NJ M NJ NJ NJ f -A -A -A -^ C aQ 5 Z * -' o ^ NJ NJ Ni NJ NJ NJ NO NJ fJ NO NJ NJ NJ NJ M NJ NJ M NJ M NJ NJ NJ NJ NJ NJ NJ NJ NJ M Ni Ni M Ni NJ fO M NJ NJ NJ NJ S s js js js js js js j- Js js js js js js js js js js js js js js js js js js js js js js js js js s js js js j- Js ^ js js js j- Js js ^ i S sl S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S sJ S S sl S sI S o O * IO NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ O O O O O O O O O O O O -S -A _S _S -A _S _S _ S _S _ A __ _ S __ , C0 C0 C0 C0 C0 C0 G0 C0 C0 o o O O O O O O O O O O O O O CO CO CO CO GO GO CO CO CO CO CO CO CO CO S si S S sl S sI S S S S S S CD Cn CD CJ-l Ol Ol Ol Ol Ol 3 r* ό O O O O O O O O O O O O O O O O O O O O O O O O O O O NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ O O O O O O O O O CQ σ oe O IO NJ NJ NJ NJ Ni NJ Ni Ni Ni Ni NJ NJ O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O O si z 9 > > > > > > > > > > > -. ^- - ! - J- --- __ -_ _- -- -- -- _- -- _- O O O O O O O O X X X X X X X X X OS r^ ^0 M N 3 M Ivl M M ^J M ^3 •A - l ■ - - - J _ J J ^ ■ _ - i _ o O O O O O O O O O O O O O O O O O O O O ■■■A jO to NJ NJ NJ NJ NO NJ NJ NJ NJ ro ro p O O p p O O O p O p O O c^ i-^ cπ CD Ol Ol Ol Ol Oi ro 3 9° φ φ φ φ φ φ φ φ φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ Φ s s s s s s s s s s s s 's s s s s s s s s φ T| CO GO ro NJ GO GO CO NJ NJ CO CO CO NJ NJ NJ co co ro -A CO CO ro NJ NJ CO CO CO NJ NO NJ CO CO NJ NJ NJ CO GO CO 3 3 Φ fP M NO rO NJ M NJ M NJ NJ NJ NJ NO NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NJ NO rO NJ NJ NO NJ NJ NJ NJ i Ni Ni NO Ni Ni NO to NJ NJ NJ S -4 sl s sJ S S S S sl S S S S S S S sl S S sJ S S S S S S S S S S -sl s S js js js js js js js js Js js js js js js js js js js js js js js js js js s J . s s J . ssJ . ssJs s JS s N J- sJs sJs sJs s Js Js Js JS J. 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So TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 571 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 572 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 573 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) J W M M NJ M M M M M M M M M M M M M M M M M M M M Isl M M M I M W C_O CO C» 00 03 CO C» 00 00 03 03 I30 C» 00 ∞ C» C» <DO OD OO OO OO C» OO OO CO OO CO CO ∞ CD l-D ^O CD CD CO CD CO CO CD CD CO CD CO CD CC ) CD CD CD (D eD CD tD CD CD CD CD CD (o eD (D (D tD CO ΪD CD CD CD CD CD eD CD (D CO (D <D {D CD eD CD o CΛ ■* D *X> CD *X> CO CD * * D *-D CD * > C» C» OO OO C» CO OO C» OO OO S S S S S S S S S S OJ |-_D l_n O> i3} Cn cn 73 m * D θcι i o) tn j> ω M -' θ co t. i o) en j ω ι -k θ θ3 co i '_) eji ω M -i θ (D C» * i o) eιi J> ω D σ z o TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 575 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 577 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) TABLE 3 - Propionibacterium Acnes Open Reading Frames Page 578 of 579 SEQ ID NO: SEQ ID NO: Contig Name Frame From To (ORF) (Contig) a e : an ene ar nayss o . acnes s Pagel of 333 Table 4: BLAST an GeneMark Analysis of P. acnes ORFs Page 2 of 333 a e : an ene ar nayss o . acnes s Page 3 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 4 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 5 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 6 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 7 of 333 Ta e 4: BLAST and GeneMark Analysis of P. acnes s Page 8 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 9 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 10 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 11 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 12 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes OVKΨS " Page 13 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 14 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 15 of 333 Table 4 BLAST and GeneMark Analysis of P acnes URFs Page 16 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 17 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 18 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 19 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 20 of 333 Table 4 BLAST and GeneMark Analysis of P acnes UKFs Page 21 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 22 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 23 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 24 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 25 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 26 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 27 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 28 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 29 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 30 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 31 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 32 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 33 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 34 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 35 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 36 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 37 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 38 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 39 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 40 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 41 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 42 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 43 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 44 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 45 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 46 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 47 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 48 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 49 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 50 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 51 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 52 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 53 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 54 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 55 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 56 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 57 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 58 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 59 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 60 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 61 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 62 of 333 ,<. JI„JI «!i,, ,* • „JI„ $z, ι| ™ iι c;ιι ;;;; Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 63 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 64 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 65 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs"" .:» . » „.4i„ , „,ii„ is;;,.; O O Page 66 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORf--s" ; .ai iu: __&, s „_.„ J ; -ra c;iι . Page 67 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes 'ORFs " r* t-j -i,/ ,.j„ c; ϊo !i Page 68 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes δRF-s ' " Page 69 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 70 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 71 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 72 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 73 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 74 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 75 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 76 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 77 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 78 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 79 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 80 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 81 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 82 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 83 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 84 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 85 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 86 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 87 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 88 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 89 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 90 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 91 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 92 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 93 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 94 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 95 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 96 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 97 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 98 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 99 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 100 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 101 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 102 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 103 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 104 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 105 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 106 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 107 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 108 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 109 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 110 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 111 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 112 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 113 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 114 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 115 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 116 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 117 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 118 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 119 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 120 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 121 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 122 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes Page 123 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 124 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 125 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 126 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 127 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 128 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 129 of.333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 130 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 131 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 132 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 133 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 134 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 135 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 136 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 137 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 138 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 139 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 140 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 141 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 142 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 143 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 144 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 145 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 146 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 147 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 148 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 149 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 150 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 151 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 152 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 153 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 154 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 155 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 156 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 157 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 158 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 159 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 160 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 161 of 333 Table 4 BLAST and GeneMark Analyεiε of P acnes ORFs Page 162 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 163 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 164 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 165 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 166 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 167 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 168 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 169 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 170 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 171 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 172 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 173 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 174 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 175 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 176 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 177 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 178 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 179 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 180 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 181 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 182 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 183 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 184 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 185 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 186 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 187 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ι .i.ε::s!c Page 188 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 189 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 190 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 191 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 192 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 193 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 194 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 195 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 196 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 197 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 198 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 199 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 200 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 201 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 202 of 333 Table 4 BLAST and GeneMark Analysis of P acnes ORFs Page 203 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes 'ORPs"' ..ui,. ii,,,,, *i,„j! i);,;si ; Page 204 of 333 Table 4: . 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DUΛO I emu OBI ItJlvic-i P. rucuydi≥- υi r . α i i Page 248 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 249 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 250 of 333 . j c c )s oτ . ac ec) Page 251 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 252 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFέ" «>' JW ••»„ ,• ■ ,„11„ 1|,„„ Page 253 of 333 Table 4: BLAST and GeneMark Analysiε of P. acnes ORFε Page 254 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 255 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 256 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 257 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 258 of 333 Table 4: BLAST and GeneMark Analysiε of P. acnes ORFs Page 259 of 333 Ta e 4: A an GeneMar Analyss o P. acnes ORFs Page 260 of 333 Table 4: BLAST and GeneMark Analyεiε of P. acnes ORFs Page 261 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 262 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ό ' RFs " «v ■■ „. *• «,«. .. * „.ji,, *,,„ c;ji ii„;)i ; Page 263 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 264 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 265 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 266 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 267 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs 1 '"' ..ιι ιj,,,sι ™ n„ ,.' ■ , K; H I ; Page 268 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 269 of 333 Ta le 4: B AST and GeneMark Analysis o P. acnes s Page 270 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 271 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 272 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes GRF&" »i ! ϋ.,,11 „.«„ ,." «ji„ i!„„ ij ; ι o , Page 273 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 274 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 275 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes U FS Page 276 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 277 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs"' Page 278 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 279 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 280 of 333 Table 4: bLAS I and GeneMark Analysis oτ P. acnes urcrs Page 281 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 282 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes 0RF " ,, Page 283 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 284 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 285 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 286 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 287 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 288 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 289 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 290 of 333 a e . an ene ar naysis o . c - Page 291 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes " ORFs" ' Page 292 of 333 Table 4: BLAST and GeneMark Analysis ot P. acnes urct-s Page 293 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 294 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 295 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 296 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 297 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ' ORFs " Page 298 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 299 of 333 a e ana GeneMark Analysis oτ r. acnes urcrs Page 300 of 333 a e : an ene ar naysis o . acnes - Page 301 of 333 a e : an ene ar naysis of P. acnes uκι-s Page 302 of 333 Ta e : an eneMark Analysis of P. acnes UKI-s Page 303 of 333 a e : an ene ar naysis o . acne - Page 304 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 305 of 333 a e _> oene ar naysis or 1". acnes wrcrs Page 306 of 333 a e : an ene ar naysis o . acn - Page 307 of 333 a e e r naysi o - Page 308 of 333 a e : e r naysi o /*. cnes urcrs Page 309 of 333 Table 4: BLAST and GeneMark Analysis of P. acnes ORFs Page 310 of 333 a e : ano ιsenervιarκ Analysis oτ /-. acnes ursrs Page 311 of 333 a e : and GeneMark Analysis of P. acnes υκι-s Page 312 of 333 a e : an ene ar naysis o . acnes o ι-s"* Page 313 of 333 a e : an ene ar naysis o . acnes - Page 314 of 333 _> . . - Page 315 of 333 a e : an ene ar nayss o . acnes S Page 316 of 333 a e : an ene ar nayss o . ac e - Page 317 of 333 a e an ene ar naysis o acnes S Page 318 of 333 a e : an ene ar nayss o . acnes s Page 319 of 333 is or r. acnβb Page 320 of 333 a e : an ene ar naysis o . acne - Page 321 of 333 a e : an ene ar naysis o . acnes s Page 322 of 333 a e : an ene ar nayss o . acnes s Page 323 of 333 a e _ a ene ar naysis o . a n - Page 324 of 333 -. j . α.ιι-a IΛM O Page 325 of 333 an ene ar naysis o . acnes - Page 326 of 333 a e : an ene ar nayss o . acnes - Page 327 of 333 a e : an ene ar nayss o . acnes Page 328 of 333 a e : - ene ar naysis o . Page 329 of 333 . . Page 330 of 333 a e : an ene ar nayss o . ac e - Page 331 of 333 e : J n ene ar naysis o . a Page 332 of 333 a e : an ene ar naysis o . c - Page 333 of 333

Claims: CLAIMS What is Claimed: 1. An isolated polynucleotide comprising a sequence selected from the group consisting of: (a) sequences provided in SEQ ID NO: 1-299; (b) , complements of he sequences provided in SEQ ID NO: 1-299; (c) sequences encoding a P. acnes protein consisting of at least X contiguous residues of a sequence provided in SEQ ID NO: 1-299, wherein X is selected from the group consisting of 20, 30, 40, 50, 75, 100, 200, 300, 400 and 500; (d) sequences that hybridize to a sequence provided in SEQ ID NO: 1-299 under highly stringent conditions; (e) sequences having at least Y% identity to a sequence of SEQ ID NO: 1-299, determined using the computer algorithm BLAST set to default parameters, wherein Y is selected from the group consisting of 75, 80, 85, 90, 95 and 99; and (f) degenerate variants of a sequence provided in SEQ ID NO: 1-299. 2. An isolated polypeptide comprising an amino acid sequence selected from the group consisting of: (a) sequences encoded by a polynucleotide of claim 1 ; and (b) sequences having at least Y% identity to a sequence encoded by a polynucleotide of claim 1 as determined using the computer algorithm BLASTP set to default parameters, wherein Y is selected from the group consisting of 75, 80, 85, 90, 95 and 99. 3. An isolated polypeptide selected from the group consisting of: (a) P. acnes transferase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 927, 1051, 2084, 2525, 2767, 2891, 3255, 3443, 4287, 5495, 5751, 6133, 6186, 10674, 12113, 12316, 12334, 12347, 12610, 12868, 14234, 14307, 14769, 16001, 16403, 17869, 18690, 20108, 20783, 21258, 22948, 24326, 24787, 25803, 26333, 27012, 27019, 27138, 27141, 27307, 28925, 29085 and 29204; (b) P. acnes enterotoxin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 23419; (c) P. acnes lipoprotein-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 6740, 12271, 15138, 16073, 19399, 19447, 21711, 24622, 26161 and 28123; (d) R acnes membrane-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 1469, 1909, 2482, 2676, 2905, 3081, 3151, 3773, 4114, 4725, 5864, 6515, 7380, 7425, 7576, 7710, 8042, 8324, 8370, 9100, 9782, 10658, 13122, 13897, 15890, 16337, 16713, 17093, 17631, 19021, 19085, 19108, 19154, 19407, 20132, 20207, 20382, 20395, 20512, 21074, 22771, 23809, 24355, 24770, 24800, 24826, 26504, 26798, 27079, 27470, 27475 and 29132; (e) P. acnes permease-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 9383, 9430, 11564, 12052, 12110, 12261, 14484, 14820, 15476, 21154, 21180, 21983, 22019, 22456, 24300, 26784 and 27769; (f) R acnes protease/proteinase-related polypeptides comprising at least an immunogemc fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 10003, 10107, 10197, 17403, 18436, 21368,1585, 2909, 3071, 8768, 10789, 11032, 11033 and 12785; (g) P. acnes protein A-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 23820; (h) R acnes secreted polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consistmg of SEQ ID NOs: 3609, 4118, 6124, 8003, 10273, 11816, 14351, 14514, 16142, 17629, 21155, 22996, 23418 and 24185; (i) P. acnes dismutase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 3608; (j) R acnes adhesin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 17237; (k) R acnes transporter-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 3979, 4157, 4686, 5329, 6589, 6709, 6896, 7028, 7564, 8125, 8126, 8170, 8541, 9004, 9383, 9430, 11564, 11565, 11624, 11682, 12346, 12429, 12563, 12718, 14103, 14484, 14742, 15884, 16279, 16327, 17306, 17307, 18134, 18177, 18245, 19157, 19191, 19359, 19566, 19581, 20311, 20479, 20923, 20926, 21153, 21172, 22819, 23880, 23891, 25720, 26021, 26025, 26281, 26490, 26700, 26784, 26977, 27523, 28116, 28250 and 28385; (1) P. acnes haemolysin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 7017; (m) R acnes penicillin binding-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 10657, 16595 and 25267; (n) P. acnes sialidase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 6710, 16380, 26503 and 27212; (o) P. acnes siderophore-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 6887; (p) P. acnes lipase-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 13402; (q) P. acnes enterobactin receptor-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 5334 and 11075; (r) P. acnes cohemolysin-related polypeptides comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 15127, 25540, 6706, 23076, 8751 and 27533; and (s) sequences having at least Y% identity with a R acnes sequence recited above in (a) - (r), wherein Y is selected from the group consisting of 75, 80, 85, 90, 95 and 99. 4. An isolated polypeptide comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 25131, 25133, 25135, 25163, 25164, 25165, 25166, 25167, 25168, 25169, 25192, 25193, 25215, 25216, 25217, 25218, 7729, 25957, 6884, 7653, 7668, 20966, 20984, 21002, 905, 906, 1008, 5541, 25957, 5527, 5541, 25086, 25088, 25089, 25090, 25103, 25130, 25131, 25133, 25135, 25163, 25164, 25165, 25166, 25167, 25168, 25169, 25192, 25193, 25215, 25216, 25217, 25218, 25922, 25938, 25957, 5527, 5541, 25088, 25089, 25090, 25103, 25131, 25133, 25135, 25163, 25164, 25165, 25166, 25167, 25215, 25216, 25217, 25089, 25103, 25135, 25164, 25165, 25166, 25216, 6695, 5527, 5541, or a polypeptide having having at least Y% identity with a P. acnes sequence recited above, wherein Y is selected from the group consisting of 75, 80, 85, 90, 95 and 99. 5. An isolated polypeptide comprising at least an immunogenic fragment of an amino acid sequence selected from the group consistmg of SEQ ID NOs: 15127, 25540, 6706, 23076, 8751, 27533 or a polypeptide having having at least Y% identity with a P. acnes sequence recited above, wherein Y is selected from the group consisting of 75, 80, 85, 90, 95 and 99. 6. An isolated polypeptide comprising at least an immunogenic fragment of an amino acid sequence selected from the group consisting of SEQ ID NOs: 20036, 19872, 6373, 8769, 5991, 19299, 5011, 12317, 11062, 4958, 6923, 11989, 24369, 21491, 7887, 10447, 3070, 7878, 25103, 6868, 9121 (two matches), 24474, 12029, 20955, 16555, 15237, 20973, 20475, 15259, 6427, 4967, 20100, 10141, 15657, 3608, 16608, 21710, 25380, 4853, 25957, 9071, 3659, 13512, 3697, 7384, 24722, 10674, 1282, 1209, 6501, 3691, 12347, 21762, 15197, 1165, 23091, 6428, 5429, 24758, 3590, 3723, 9106, 12217, 7270, 2913, 1187, 1585, 16537, 24679, 26397, 26691, 7397, 6695, 6892, 19926, 4754, 26692, 15670, 3652, 20510, 3449, 20070, 19245, 20108, 19427, 10564, 10678, 21172, 21780, 3334, 6338, 5379, 11580, 15693, 9994, 24973, 20684, 7865, 16573, 11864, 12324, 20439, 1230, 14278, 3412, 12317, 5991, 6923, 10741, 5373, 19299, 383, 1284, 12228, 26402, 4673, 7887, 9004, 384, 25103, 6373, 12029, 20036, 16555, 17521, 20476, 15237, 24581, 3659, 14031, 9071, 4958, 15259, 12904, 5440, 23560, 3697, 3608, 25957, 7384, 24722, 15863, 8135, 20585, 3691, 12217, 16439, 1645, 5514, 21710, 24895, 4853, 23420, 5437, 1278, 16992, 12126, 20934, 20475, 17970, 20955, 3070, 6564, 9069, 12666, 7864, 18692, 2453, 1209, 20973, 7419, 15197, 23591, 20100, 23065, 6337, 10989, 1585, 17841, 6868, or a polypeptide having having at least Y% identity with a P. acnes sequence recited above, wherein Y is selected from the group consisting of 75, 80, 85, 90, 95 and 99. 7. An expression vector comprising a polynucleotide of claim 1 operably linked to an expression control sequence. 8. A host cell transformed or transfected with an expression vector according to claim 7. 9. An isolated antibody, or antigen-binding fragment thereof, that specifically binds to a polypeptide of any one of claims 2-6. 10. A method for detecting the presence or absence of Propionibacterium acnes in a patient, comprising the steps of: (a) obtaining a biological sample from the patient; (b) contacting the biological sample with a binding agent that binds to the polypeptide of any one of claims 2-6; (c) detecting in the sample an amount of polypeptide that binds to the binding agent; and (d) comparing the amount of polypeptide to a predetermined cut-off value and therefrom determining the presence or absence of Propionibacterium acnes in the patient. 11. A fusion protein comprising at least one polypeptide according to any one of claims 2-6. 12. An oligonucleotide that hybridizes to a sequence recited in SEQ ID NO: 1-299 under highly stringent conditions. 13. A method for stimulating an immune response specific for an Propionibacterium acnes protein, comprising contacting T-cells and or B-cells with at least one component selected from the group consisting of: (a) polypeptides according to any one of claims 2-6; (b) polynucleotides according to claim 1 ; and (c) antigen-presenting cells that express a polypeptide according to any one of claims 2-6, under conditions and for a time sufficient to permit the stimulation and/or expansion of T-cells and/or B-cells. 14. An isolated T cell population, comprising T cells prepared according to the method of claim 13. 15. A composition comprising a first component selected from the group consisting of physiologically acceptable carriers and immunostimulants, and a second component selected from the group consisting of: (a) polypeptides according to any one of claims 2-6; (b) polynucleotides according to claim 1; (c) antibodies according to claim 9; (d) fusion proteins according to claim 11 ; (e) T cell populations according to claim 14; and (f) antigen presenting cells that express a polypeptide according to any one of claims 2-6. 16. A method for stimulating an immune response in a patient, comprising administering to the patient a composition of claim 15. 17. A method for the treatment of an acne in a patient, comprising administering to the patient a composition of claim 15. 18. A method for determining the absence or presence of Propionibacterium acnes in a patient, comprising the steps of: (a) obtaining a biological sample from the patient; (b) contacting the biological sample with an oligonucleotide according to claim 12; (c) detecting in the sample an amount of a polynucleotide that hybridizes to the oligonucleotide; and (d) compare the amount of polynucleotide that hybridizes to the oligonucleotide to a predetermined cut-off value, and therefrom determining the presence or absence of Propionibacterium acnes in the patient. 19. A diagnostic kit comprising at least one oligonucleotide according to claim 12. 20. A diagnostic kit comprising at least one antibody according to claim 9 and a detection reagent, wherein the detection reagent comprises a reporter group. 21. A method for inhibiting the development of Propionibacterium acnes in a patient, comprising the steps of: (a) incubating CD4+ and/or CD8+ T cells isolated from a patient with at least one component selected from the group consisting of: (i) polypeptides according to any one of claims 2-6; (ii) polynucleotides according to claim 1; and (iii) antigen presenting cells that express a polypeptide of any one of claims 2-6, such that T cell proliferate; (b) administering to the patient an effective amount of the proliferated T cells, and thereby inhibiting the development of Propionibacterium acnes in the patient.

Inventors: BHATIA AJAY, CARTER DARRICK, JEN SHYIAN, L MAISONNEUVE JEAN-FRANCOIS, MITCHAM JENNIFER L, PERSING DAVID H, SKEIKY YASIR A W, WANG SIQING STEVEN, ZHANG YANNI, BHATIA, AJAY, CARTER, DARRICK, JEN, SHYIAN, L'MAISONNEUVE, JEAN-FRANCOIS, MITCHAM, JENNIFER, L., PERSING, DAVID, H., SKEIKY, YASIR, A., W., WANG, SIQING, STEVEN, ZHANG, YANNI
Applicants: BHATIA AJAY, CARTER DARRICK, CORIXA CORP, JEN SHYIAN, MAISONNEUVE JEAN FRANCOIS L, MITCHAM JENNIFER L, PERSING DAVID H, SKEIKY YASIR A W, WANG SIQING STEVEN, ZHANG YANNI, BHATIA, AJAY, CARTER, DARRICK, CORIXA CORPORATION, JEN, SHYIAN, L'MAISONNEUVE, JEAN-FRANCOIS, MITCHAM, JENNIFER, L., PERSING, DAVID, H., SKEIKY, YASIR, A., W., WANG, SIQING, STEVEN, ZHANG, YANNI
Application year: 2001
Main classification: C12N15
IPC codes: A61K39, A61K48, A61P17, A61P29, C07K14, C07K16, C07K19, C12N1, C12N5, C12N15, C12Q1, C12R1, G01N33