COMPOUNDS AND METHODS FOR TREATMENT AND DIAGNOSIS OF MYCOBACTERIAL INFECTIONS

Abstract: The present invention provides polypeptides comprising an immunogenic portion of a M. vaccae protein and DNA molecules encoding such polypeptides, together with methods for their use in the diagnosis and treatment of mycobacterial infection. Methods for enhancing the immune response to an antigen including administration of M. vaccae culture filtrate or delipidated M. vaccae cells are also provided.

Description: COMPOUNDS AND METHODS FOR TREATMENT AND DIAGNOSIS OF MYCOBACTERIAL INFECTIONS Technical Field The present invention relates generally to the detection, treatment and prevention of infectious diseases. In particular, the invention is related to compounds and methods for the treatment of mycobacteπal infections including Mycobacterium tuberculosis and Mycobacterium avium The invention is further related to compounds that function as non-specific immune response amplifiers, and the use of such non-specific immune response amplifiers as adjuvants in vaccination or lmmunotherapy against infectious disease, and in certain treatments for immune disorders and cancer. Background of the Invention Tuberculosis is a chronic, infectious disease, that is caused by infection with Mycobacterium tuberculosis (M tuberculosis) It is a major disease in developing countries, as well as an increasing problem in developed areas of the world, with about 8 million new cases and 3 million deaths each year. Although the infection may be asymptomatic for a considerable period of time, the disease is most commonly manifested as a chronic inflammation of the lungs, resulting in fever and respiratory symptoms. If left untreated, significant morbidity and death may result. Although tuberculosis can generally be controlled using extended antibiotic therapy, such treatment is not sufficient to prevent the spread of the disease. Infected individuals may be asymptomatic, but contagious, for some time In addition, although compliance with the treatment regimen is critical, patient behaviour is difficult to monitor. Some patients do not complete the course of treatment, which can lead to ineffective treatment and the development of drug resistant mycobacteπa Inhibiting the spread of tuberculosis requires effective vaccination and accurate, early diagnosis of the disease. Currently, vaccination with live bacteria is the most efficient method for inducing protective immunity. The most common mycobacterium employed for this purpose is Bacillus Calmette-Gueπn (BCG), an avirulent strain of Mycobacterium bovis. However, the safety and efficacy of BCG is a source of controversy and some countries, such as the United States, do not vaccinate the general public. Diagnosis of M. tuberculosis infection is commonly achieved using a skin test, which involves intradermal exposure to tuberculin PPD (protein-purified derivative). Antigen-specific T cell responses result in measurable induration at the injection site by 48-72 hours after injection, thereby indicating exposure to mycobacterial antigens. Sensitivity and specificity have, however, been a problem with this test, and individuals vaccinated with BCG cannot be distinguished from infected individuals. A less well-known mycobacterium that has been used for immunotherapy for tuberculosis, and also leprosy, is Mycobacterium vaccae, which is non-pathogenic in humans. However, there is less information on the efficacy of M. vaccae compared with BCG, and it has not been used widely to vaccinate the general public. M. bovis BCG and M. vaccae are believed to contain antigenic compounds that are recognised by the immune system of individuals exposed to infection with M. tuberculosis. There thus remains a need in the art for effective compounds and methods for preventing, treating and detecting tuberculosis. Summary of the Invention Briefly stated, the present invention provides compounds and methods for the prevention, treatment and diagnosis of mycobacterial infection, together with adjuvants Tor use in vaccines or immunotherapy of infectious diseases and cancers. In a first aspect, polypeptides derived from Mycobacterium vaccae are provided comprising an immunogenic portion of an antigen, or a variant of such an antigen. In one embodiment, the antigen includes an amino acid sequence selected from the group consisting of: (a) sequences recited in SEQ ID NOS: 1-4, 9-16, 18- 21, 23, 25, 26, 28, 29, 44, 45, 47, 52-55, 63, 64, 70, 75, 89, 94, 98, 100-105, 109, 110, 112, 1 14, 1 17, 1 18, 121, 124, 125, 134, 135, 140 and 141 ; and (b) sequences having at least about a 99% probability of being the same as a sequence recited in SEQ ID NOS: 1-4, 9-16, 18-21, 23, 25, 26, 28, 29, 44, 45, 47, 52-55, 63, 64, 70, 75, 89, 94, 98, 100-105, 109, 1 10, 1 12, 1 14. 1 17, 1 18, 121. 124. 125, 134. 135, 140 and 141 as measured by the computer algorithm BLASTP. In a second aspect, the invention provides polypeptides comprising an immunogenic portion of an M. vaccae antigen wherein the antigen comprises an amino acid sequence encoded by a DNA molecule selected from the group consisting of: (a) sequences recited in SEQ ID NOS: 40-42, 46, 48-51 , 74, 88, 93, 97, 99, 106- 108, 1 1 1 , 1 13, 1 15, 1 16, 120, 122, 123, 132, 133 and 136-138; (b) complements of the sequences recited in SEQ ID NOS: 40-42, 46, 48-51, 74, 88, 93, 97, 99, 106-108, 1 1 1, 1 13, 115, 1 16, 120, 122, 123, 132, 133 and 136-138; and (c) sequences having at least about a 99% probability of being the same as a sequence of (a) or (b) as measured by the computer algorithm FASTA. DNA sequences encoding the inventive polypeptides, expression vectors comprising these DNA sequences, and host cells transformed or transfected with such expression vectors are also provided. In another aspect, the present invention provides fusion proteins comprising a first and a second inventive poiypeptide or, alternatively, an inventive poiypeptide and a known M. tuberculosis antigen. Within other aspects, the present invention provides pharmaceutical compositions that comprise at least one of the inventive polypeptides, or a DNA molecule encoding such a poiypeptide, and a physiologically acceptable carrier. The invention also provides vaccines comprising at least one of the above polypeptides and a nonspecific immune response amplifier, together with vaccines comprising at least one DNA sequence encoding such polypeptides and a non-specific immune response amplifier. In yet another aspect, methods are provided for inducing protective immunity in a patient, comprising administering to a patient an effective amount of one or more of the above polypeptides together with an immune response amplifier. In further aspects of this invention, methods and diagnostic kits are provided for detecting tuberculosis in a patient. In a first embodiment, the method comprises contacting dermal cells of a patient with one or more of the above polypeptides and detecting an immune response on the patient's skin. In a second embodiment, the method comprises contacting a biological sample with at least one of the above polypeptides; and detecting in the sample the presence of antibodies that bind to the poiypeptide or polypeptides, thereby detecting M. tuberculosis infection in the biological sample. Suitable biological samples include whole blood, sputum, serum, plasma, saliva, cerebrospinal fluid and urine. Diagnostic kits comprising one or more of the above polypeptides in combination with an apparatus sufficient to contact the poiypeptide with the dermal cells of a patient are provided. The present invention also provides diagnostic kits comprising one or more of the inventive polypeptides in combination with a detection reagent. In yet another aspect, the present invention provides antibodies, both polyclonal and monoclonal, that bind to the polypeptides described above, as well as methods for their use in the detection of M. tuberculosis infection. The present invention also provides methods for enhancing a non-specific immune response to an antigen. In one embodiment, such methods comprise administering a composition comprising a component selected from the group consisting of : (a) delipidated M. vaccae cells, (b) deglycosylated M. vaccae cells; (c) delipidated and deglycosylated M. vaccae cells and (d) M. vaccae culture filtrate. In a second embodiment, such methods comprise administering a poiypeptide, the poiypeptide comprising an immunogenic portion of an antigen, wherein said antigen includes a sequence selected from the group consisting of: (a) sequences recited in SEQ ID NOS: 114, 1 17 and 118; and (b) sequences having at least about 97% identity to a sequence recited in SEQ ID NOS: 114, 1 17 and 118. In yet a further aspect, compositions comprising a component selected from the group consisting of delipidated M. vaccae cells, deglycosylated M. vaccae cells, and delipidated and deglycosylated M. vaccae cells are provided, together with vaccines comprising such components and methods of using such compositions and vaccines to induce protective immunity in a patient. 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 Figs. 1A and IB illustrate the protective effects of immunizing mice with autoclaved M. vaccae or unfractionated M. vaccae culture filtrates, respectively, prior to infection with live M. tuberculosis H37Rv. Figs. 2A and B show components of M. vaccae and M. tuberculosis culture filtrates, respectively, as analysed by 2-dimensional polyacrylamide gel electrophoresis. Fig. 3 is a comparison of the Antigen 85A protein sequence obtained from M. vaccae with those from M. bovis, M. tuberculosis and M. leprae. Fig. 4A(i) - (iv) illustrate the non-specific immune amplifying effects of 10 μg, XOOμg and lmg autoclaved M. vaccae and 15μg unfractionated culture filtrates of M. vaccae, respectively. Fig. 4B(i) and (ii) illustrate the non-specific immune amplifying effects of autoclaved M. vaccae and delipidated M. vaccae, respectively. Fig. 4C(i) illustrates the non-specific immune amplifying effects of whole autoclaved M. vaccae. Fig. 4C(ii) illustrates the non-specific immune amplifying effects of delipidated M. vaccae from which glycolipids had been removed and the proteins extracted with SDS. Fig. 4C(iii) illustrates that the adjuvant effect of the preparation of Fig. 4C(ii) is destroyed by treatment with the proteolytic enzyme pronase. Fig. 4D illustrates The non-specific immune amplifying effects of heat-killed M. vaccae (Fig. 4D(i)), M. tuberculosis (Fig. 4D(ii)), M. bovis BCG (Fig. 4D(iii)), M. phlei (Fig. 4D(iv)) and M. smegmatis (Fig. 4D(v)). Fig. 5 shows the results of polyacrylamide gel electrophoresis analysis of SDS-extracted proteins derived from delipidated and deglycolipidated M. vaccae. Fig. 6 illustrates the non-specific immune amplifying effects of different molecular weight fractions of SDS-extracted M. vaccae proteins. Fig. 7 illustrates the non-specific immune amplifying effects of different pi fractions of SDS-extracted M. vaccae proteins. Fig. 8 illustrates the induction of IL-12 by heat-killed M. vaccae, lyophilized M. vaccae, delipidated and deglycosylated M. vaccae (referred to as "delipidated M. vaccae") and M. vaccae glycolipids. Fig. 9 illustrates the stimulation of interferon-gamma production by different concentrations of M. vaccae recombinant proteins, heat-killed M. vaccae, delipidated and deglycosylated M. vaccae (referred to as "delipidated M. vaccae"), M. vaccae glycolipids and lipopolysaccharide in C57BL-6 peritoneal macrophages (Fig 9A); BALB/C peritoneal macrophages (Fig 9B); and C3H/HeJ peritoneal macrophages (Fig 9C). Detailed Description of the Invention As noted above, the present invention is generally directed to compositions and methods for preventing, " treating and diagnosing mycobacterial infections, including M. tuberculosis and M. avium infections. Considerable research efforts have been directed towards elucidating the mechanism of immune response to mycobacterial infection, in particular M. tuberculosis infection. While macrophages have been shown to act as the principal effectors of M. tuberculosis immunity, T cells are the predominant inducers of such immunity. The essential role of T cells in protection against M. tuberculosis infection is illustrated by the frequent occurrence of M. tuberculosis in AIDS patients, due to the depletion of CD4 T cells associated with human immunodeficiency virus (HIV) infection. Mycobacterium-reactive CD4 T cells have been shown to be potent producers of gamma-interferon (IFN-γ), which, in turn, has been shown to trigger the anti-myco acterial effects of macrophages in mice. While the role of IFN-γ in humans is less clear, studies have shown that 1,25-dihydroxy-vitamin D3, either alone or in combination with IFN-γ or tumor necrosis factor-alpha, activates human macrophages to inhibit M. tuberculosis infection. Furthermore, it is known that IFN-γ stimulates human macrophages to make 1 ,25-dihydroxy-vitamin D3. Similarly, IL-12 has been shown to play a role in stimulating resistance to M. tuberculosis infection. Another property of CD4" T cells and macrophages is their ability to activate CD8 * cytotoxic T cells which are capable of killing pathogen-infected cells. CD8 * T cells have been shown to kill macrophages and other cells that harbour M. tuberculosis. For a review of the immunology of M. tuberculosis infection see Chan and Kaufmann in Tuberculosis: Pathogenesis, Protection and Control, Bloom (ed.), ASM Press. Washington, DC, 1994. The compositions of the present invention include polypeptides that comprise at least one immunogenic portion of an M. vaccae antigen, or a variant thereof. Such polypeptides stimulate T cell proliferation, and/or, interferon gamma secretion from T cells of individuals exposed to M. tuberculosis. In certain embodiments, the inventive polypeptides comprise at least an immunogenic portion of a soluble M. vaccae antigen. A "soluble M. vaccae antigen" is a protein of M. vaccae origin that is present in M. vaccae culture filtrate. As used herein, the term "poiypeptide" encompasses amino acid chains of any length, including full length proteins (i.e., antigens), wherein the amino acid residues are linked by covalent peptide bonds. Thus, a poiypeptide comprising an immunogenic portion of one of the above antigens may consist entirely of the immunogenic portion, or may contain additional sequences. The additional sequences may be derived from the native M. vaccae antigen or may be heterologous, and such sequences may (but need not) be immunogenic. "Immunogenic," as used herein, refers to the ability to elicit an immune response in a patient, such as a human, or in a biological sample. In particular, immunogenic antigens are capable of stimulating cell proliferation, interleukin-12 production or interferon-γ production in biological samples comprising one or more cells selected from the group of T cells, NK cells, B cells and macrophages, where the cells are derived from an M. tuberculosis-immune individual. Polypeptides comprising at least an immunogenic portion of one or more M. vaccae antigens may generally be used to detect tuberculosis or to induce protective immunity against tuberculosis in a patient. The compositions and methods of this invention also encompass variants of the above polypeptides. As used herein, the term "variant" covers any sequence which exhibits at least about 50%, more preferably at least about 70% and more preferably yet, at least about 90% identity to a sequence of the present invention. Most preferably, a "variant" is any sequence which has at least about a 99% probability of being the same as the inventive sequence. The probability for DNA sequences is measured by the computer algorithm FASTA (version 2.0u4, February 1996; Pearson W. R. et al., Proc. Natl. Acad. Sci., 85:2444-2448, 1988), the probability for translated DNA sequences is measured by the computer algorithm TBLASTX and that for protein sequences is measured by the computer algorithm BLASTP (Altschul, S. F. et al. J. Mol. Biol.. 215:403-410, 1990). The term "variants" thus encompasses sequences wherein the probability of finding a match by chance (smallest sum probability), is less than about 1% as measured by any of the above tests. A poiypeptide of the present invention may be conjugated to 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 poiypeptide may also be conjugated to a linker or other sequence for ease of synthesis, purification or identification of the poiypeptide (e.g., poly-His), or to enhance binding of the poiypeptide to a solid support. For example, a poiypeptide may be conjugated to an immunoglobulin Fc region. In general, M. vaccae antigens, and DNA sequences encoding such antigens, may be prepared using any of a variety of procedures. For example, soluble antigens may be isolated from M. vaccae culture filtrate as described below. Antigens may also be produced recombinantly by inserting a DNA sequence that encodes the antigen into an expression vector and expressing the antigen in an appropriate host. Any of a variety of expression vectors known to those of ordinary skill in the art may be employed. 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 poiypeptide. Suitable host cells include prokaryotes, yeast and higher eukaryotic cells. Preferably, the host cells employed are E. coli, mycobacteria, insect, yeast or a mammalian cell line such as COS or CHO. The DNA sequences expressed in this manner may encode naturally occurring antigens, portions of naturally occurring antigens, or other variants thereof. DNA sequences encoding M. vaccae antigens may be obtained by screening an appropriate M. vaccae cDNA or genomic DNA library for DNA sequences that hybridize to degenerate oligonucleotides derived from partial amino acid sequences of isolated soluble antigens. Suitable degenerate oligonucleotides may be designed and synthesized, and the screen may be performed as described, for example in Maniatis et al., Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratories, Cold Spring Harbor, NY, 1989. As described below, polymerase chain reaction (PCR) may be employed to isolate a nucleic acid probe from a cDNA or genomic DNA library. The library screen may then be performed using the isolated probe. DNA molecules encoding M. vaccae antigens may also be isolated by screening an appropriate M. vaccae expression library with anti-sera (e.g., rabbit or monkey) raised specifically against M. vaccae antigens. Regardless of the method of preparation, the antigens described herein have the ability to induce an immunogenic response. More specifically, the antigens have the ability to induce cell proliferation and/or cytokine production (for example, interferon-γ and/or interleukin-12 production) in T cells, NK cells, B cells or macrophages derived from an M. tuberculosis-immune individual. An M. tuberculosis-immune individual is one who is considered to be resistant to the development of tuberculosis by virtue of having mounted an effective T cell response to M. tuberculosis. Such individuals may be identified based on a strongly positive (i.e., greater than about 10 mm diameter induration) intradermal skin test response to tuberculosis proteins (PPD), and an absence of any symptoms of tuberculosis infection. The selection of cell type for use in evaluating an immunogenic response to an antigen will depend on the desired response. For example, interleukin-12 production is most readily evaluated using preparations containing B cells or macrophages. T cells, NK cells, B cells and macrophages derived from M. tuberculosis-immune individuals may be prepared using methods well known in the art. For example, a preparation of peripheral blood mononuclear cells (PBMCs) may be employed without further separation of component cells. PBMCs may be prepared, for example, using density centrifugation through Ficoll™ (Winthrop Laboratories, NY). T cells for use in the assays described herein may be purified directly from PBMCs. Alternatively, an enriched T cell line reactive against mycobacterial proteins, or T cell clones reactive to individual mycobacterial proteins, may be employed. Such T cell clones may be generated by, for example, culturing PBMCs from M. tuberculosis- immune individuals with mycobacterial proteins for a period of 2-4 weeks. This allows expansion of only the mycobacterial protein-specific T cells, resulting in a line composed solely of such cells. These cells may then be cloned and tested with individual proteins, using methods well known in the art, to more accurately define individual T cell specificity. Assays for cell proliferation or cytokine production in T cells, NK cells, B cells or macrophages may be performed, for example, using the procedures described below. In general, immunogenic antigens are those antigens that stimulate proliferation or cytokine production (i.e. , interferon-γ and or interleukin-12 production) in T cells, NK cells, B cells or macrophages derived from at least about 25% of M. tuberculosis-immune individuals. Among these immunogenic antigens, polypeptides having superior therapeutic properties may be distinguished based on the magnitude of the responses in the above assays and based on the percentage of individuals for which a response is observed. In addition, antigens having superior therapeutic properties will not stimulate cell proliferation or cytokine production in vitro in cells derived from more than about 25% of individuals that are not M. tuberculosis-immune, thereby eliminating responses that are not specifically due to M. tuberculosis-responsive cells. Thus, those antigens that induce a response in a high percentage of T cell, NK cell, B cell or macrophage preparations from M. tuberculosis-immune individuals (with a low incidence of responses in cell preparations from other individuals) have superior therapeutic properties. Antigens with superior therapeutic properties may also be identified based on their ability to diminish the severity of M. tuberculosis infection, or other mycobacterial infection, in experimental animals, when administered as a vaccine. Suitable vaccine preparations for use in experimental animals are described in detail below. Antigens having superior diagnostic properties may generally be identified based on the ability to elicit a response in an intradermal skin test performed on an individual with active tuberculosis, but not in a test performed on an individual who is not infected with M. tuberculosis. Skin tests may generally be performed as described below, with a response of at least about 5 mm induration considered positive. Immunogenic portions of the antigens described herein may be prepared and identified using well known techniques, such as those summarized in Paul, Fundamental Immunology, 3d ed., Raven Press, 1993, pp. 243-247. Such techniques include screening poiypeptide portions of the native antigen for immunogenic properties. The representative proliferation and cytokine production assays described herein may be employed in these screens. An immunogenic portion of a poiypeptide is a portion that, within such representative assays, generates an immune response (e.g. , cell proliferation, interferon-γ production or interleukin-12 production) that is substantially similar to that generated by the full length antigen. In other words, an immunogenic portion of an antigen may generate at least about 20%, preferably about 65%, and most preferably about 100%, of the proliferation induced by the full length antigen in the model proliferation assay described herein. An immunogenic portion may also, or alternatively, stimulate the production of at least about 20%, preferably about 65% and most preferably about 100%, of the interferon-γ and/or interleukin-I2 induced by the full length antigen in the model assay described herein. Portions and other variants of M. vaccae antigens may be generated by synthetic or recombinant means. Synthetic polypeptides having fewer than about 100 amino acids, and generally fewer than about 50 amino acids, may be generated 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 BioSystems, Inc. (Foster City, CA), and may be operated according to the manufacturer's instructions. Variants of a native antigen may be prepared using standard mutagenesis techniques, such as oligonucleotide-directed site-specific mutagenesis. Sections of the DNA sequence may also be removed using standard techniques to permit preparation of truncated polypeptides. In general, regardless of the method of preparation, the polypeptides disclosed herein are prepared in substantially pure form. Preferably, the polypeptides are at least about 80% pure, more preferably at least about 90% pure and most preferably at least about 99% pure. In certain preferred embodiments, described in detail below, the substantially pure polypeptides are incorporated into pharmaceutical compositions or vaccines for use in one or more of the methods disclosed herein. The present invention also provides fusion proteins comprising a first and a second inventive poiypeptide or, alternatively, a poiypeptide of the present invention and a known M tuberculosis antigen, such as the 38 kD antigen described in Andersen and Hansen, Infect. Immun. 57:2481-2488. 1989, together with variants of such fusion proteins. The fusion proteins of the present invention may also include a linker peptide between the first and second polypeptides. A DNA sequence encoding a fusion protein of the present invention is constructed using known recombinant DNA techniques to assemble separate DNA sequences encoding the first and second polypeptides into an appropriate expression vector. The 3' end of a DNA sequence encoding the first poiypeptide is ligated, with or without a peptide linker, to the 5' end of a DNA sequence encoding the second poiypeptide so that the reading frames of the sequences are in phase to permit mRNA translation of the two DNA sequences into a single fusion protein that retains the biological activity of both the first and the second polypeptides. A peptide linker sequence may be employed to separate the first and the second polypeptides by a distance sufficient to ensure that each poiypeptide folds into its secondary and tertiary structures. Such a peptide linker sequence is incorporated 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 poiypeptide 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 40:39-4 , 1985; Murphy et al., Proc. Natl. Acad. Sci. USA 55:8258-8262, 1986; U.S. Patent No. 4,935,233 and U.S. Patent No. 4.751 ,180. The linker sequence may be from 1 to about 50 amino acids in length. Peptide 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 encoding the fusion proteins are cloned into suitable expression systems using techniques known to those of ordinary skill in the art. In another aspect, the present invention provides methods for using one or more of the inventive polypeptides or fusion proteins (or DNA molecules encoding such polypeptides or fusion proteins) to induce protective immunity against tuberculosis in a patient. As used herein, a "patient" refers to any warm-blooded animal, preferably a human. A patient may be afflicted with a disease, or may be free of detectable disease or infection. In other words, protective immunity may be induced to prevent or treat tuberculosis. In this aspect, the poiypeptide, fusion protein or DNA molecule is generally present within a pharmaceutical composition or a vaccine. Pharmaceutical compositions may comprise one or more polypeptides, each of which may contain one or more of the above sequences (or variants thereof), and a physiologically acceptable carrier. Vaccines may comprise one or more of the above polypeptides and a non- specific immune response amplifier, such as an adjuvant or a liposome, into which the poiypeptide is incorporated. Such pharmaceutical compositions and vaccines may also contain other mycobacterial antigens, either, as discussed above, incorporated into a fusion protein or present within a separate poiypeptide. Alternatively, a vaccine of the present invention may contain DNA encoding one or more polypeptides as described above, such that the poiypeptide is generated in situ. In such vaccines, 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, bacterial and viral expression systems. Appropriate nucleic acid expression systems contain the necessary DNA sequences for expression in the patient (such as a suitable promoter and terminator signal). Bacterial delivery systems involve the administration of a bacterium (such as Bacillus-Calmette-Guerrin) that expresses an immunogenic portion of the poiypeptide on its cell surface. 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, or defective, replication competent virus. Techniques for incorporating DNA into such expression systems are well known in the art. The DNA may also be "naked," as described, for example, in Ulmer et al., Science 259:1745-1749. 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. A DNA vaccine as described above may be administered simultaneously with or sequentially to either a poiypeptide of the present invention or a known mycobacterial antigen, such as the 38 kD antigen described above. For example, administration of DNA encoding a poiypeptide of the present invention, may be followed by administration of an antigen in order to enhance the protective immune effect of the vaccine. Routes and frequency of administration, as well as dosage, will vary from individual to individual and may parallel those currently being used in immunization using BCG. In general, the pharmaceutical compositions and vaccines may be administered by injection (e.g., intradermal, intramuscular, intravenous or subcutaneous), intranasally (e.g., by aspiration) or orally. Between 1 and 3 doses may be administered for a 1-36 week period. Preferably, 3 doses are administered, at intervals " of 3-4 months, and booster vaccinations may be given periodically thereafter. Alternate protocols may be appropriate for individual patients. A suitable dose is an amount of poiypeptide or DNA that, when administered as described above, is capable of raising an immune response in a patient sufficient to protect the patient from mycobacterial infection for at least 1-2 years. In general, the amount of poiypeptide present in a dose (or produced in situ by the DNA in a dose) ranges from about 1 pg to about 100 mg per kg of host, typically from about 10 pg to about 1 mg, and preferably from about 100 pg to about 1 μg. Suitable dose sizes will vary with the size of the patient, but will typically range from about 0.1 mL to about 5 mL. While any suitable carrier known to those of ordinary skill in the art may be employed in the pharmaceutical compositions of this invention, the type of carrier will vary depending on the mode of 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., polylactic galactide) 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 and 5,075,109. Any of a variety of adjuvants may be employed in the vaccines of this invention to non-specifically enhance the immune response. Most adjuvants contain a substance designed to protect the antigen from rapid catabolism, such as aluminum hydroxide or mineral oil, and a non-specific stimulator of immune responses, such as lipid A, Bordetella pertussis, M. tuberculosis, or, as discussed below, M. vaccae. Suitable adjuvants are commercially available as, for example, Freund's Incomplete Adjuvant and Freund's Complete Adjuvant (Difco Laboratories, Detroit, MI), and Merck Adjuvant 65 (Merck and Company, Inc., Rahway, NJ). Other suitable adjuvants include alum, biodegradable microspheres, monophosphoryl lipid A and Quil A. InΕriother aspect, this invention provides methods for using one or more of the polypeptides described above to diagnose tuberculosis using a skin test. As used herein, a "skin test" is any assay performed directly on a patient in which a delayed- type hypersensitivity (DTH) reaction (such as swelling, reddening or dermatitis) is measured following intradermal injection of one or more polypeptides as described above. Preferably, the reaction is measured at least 48 hours after injection, more preferably 48-72 hours. The DTH reaction is a cell-mediated immune response, which is greater in patients that have been exposed previously to the test antigen (i.e., the immunogenic portion of the poiypeptide employed, or a variant thereof). The response may be measured visually, using a ruler. In general, a response that is greater than about 0.5 cm in diameter, preferably greater than about 1.0 cm in diameter, is a positive response, indicative of tuberculosis infection. For use in a skin test, the polypeptides of the present invention are preferably formulated, as pharmaceutical compositions containing a poiypeptide and a physiologically acceptable carrier, as described above. Such compositions typically contain one or more of the above polypeptides in an amount ranging from about 1 μg to about 100 μg, preferably from about 10 μg to about 50 μg in a volume of 0.1 mL. Preferably, the carrier employed in such pharmaceutical compositions is a saline solution with appropriate preservatives, such as phenol and/or Tween 80™. In a preferred embodiment, a poiypeptide employed in a skin test is of sufficient size such that it remains at the site of injection for the duration of the reaction period. In general, a poiypeptide that is at least 9 amino acids in length is sufficient. The poiypeptide is also preferably broken down by macrophages or dendritic cells within hours of injection to allow presentation to T-cells. Such polypeptides may contain repeats of one or more of the above sequences or other immunogenic or nonimmunogenic sequences. In another aspect, methods are provided for detecting mycobacterial infection in a biological sample, using one or more of the above polypeptides, either alone or in combination. In embodiments in which multiple polypeptides are employed, polypeptides other than those specifically described herein, such as the 38 kD antigen described above, may be included. As used herein, a "biological sample" is any antibody-containing sample obtained from a patient. Preferably, the sample is whole blood, sputum, serum, plasma, saliva, cerebrospinal fluid or urine. More preferably, the sample is a blood, serum or plasma sample obtained from a patient or a blood supply. The polypeptide(s) are used in an assay, as described below, to determine the presence or absence of antibodies to the polypeptide(s) in the sample, relative to a predetermined cut-off value. The presence of such antibodies indicates the presence of mycobacterial infection. In embodiments in which more than one poiypeptide is employed, the polypeptides used are preferably complementary (i.e., one component poiypeptide will tend to detect infection in samples where the infection would not be detected by another component poiypeptide). Complementary polypeptides may generally be identified by using each poiypeptide individually to evaluate serum samples obtained from a series of patients known to be infected with a Mycobacterium. After determining which samples test positive (as described below) with each poiypeptide, combinations of two or more polypeptides may be formulated that are capable of detecting infection in most, or all, of the samples tested. For example, approximately 25-30% of sera from tuberculosis-infected individuals are negative for antibodies to any single protein, such as the 38 kD antigen mentioned above. Complementary polypeptides may, therefore, be used in combination with the 38 kD antigen to improve sensitivity of a diagnostic test. A variety of assay formats employing one or more polypeptides to detect antibodies in a sample are well known in the art. See, e.g., Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, 1988. In a preferred embodiment, the assay involves the use of poiypeptide immobilized on a solid support to bind to and remove the antibody from the sample. The bound antibody may then be detected using a detection reagent that contains a reporter group. Suitable detection reagents include antibodies that bind to the antibody/polypeptide complex and free poiypeptide labelled with a reporter group (e.g., in a semi-competitive assay). Alternatively, a competitive assay may be utilized, in which an antibody t at binds to the poiypeptide is labelled with a reporter group and allowed to bind to the immobilized antigen after incubation of the antigen with the sample. The extent to which components of the sample inhibit the binding of the labelled antibody to the poiypeptide is indicative of the reactivity of the sample with the immobilized poiypeptide. The solid support may be any solid material to which the antigen may be attached. Suitable materials are well known in the art. 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 polypeptides may be bound to the solid support using a variety of techniques well known in the art. In the context of the present invention, the term "bound" refers to both noncovalent association, such as adsorption, and covalent attachment, which may be a direct linkage between the antigen and functional groups on the support or a linkage by way of a cross-linking agent. Binding by adsorption to a well in a microtiter plate or to a membrane is preferred. In such cases, adsorption may be achieved by contacting the poiypeptide, 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 1 day. In general, contacting a well of a plastic microtiter plate (such as polystyrene or polyvinylchloride) with an amount of poiypeptide ranging from about 10 ng to about 1 μg, and preferably about 100 ng, is sufficient to bind an adequate amount of antigen. Covalent attachment of poiypeptide 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 poiypeptide. For example, the poiypeptide may be bound 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 poiypeptide (see, e.g., Pierce Immunotechnology Catalog and Handbook, 1991 , at A12-A13). In certain embodiments, the assay is an enzyme-linked immunosorbent assay (ELISA). This assay may be performed by first contacting a poiypeptide antigen that has been immobilized on a solid support, with the sample, such that antibodies to the poiypeptide within the sample are allowed to bind to the immobilized poiypeptide. Unbound sample is then removed from the immobilized poiypeptide and a detection reagent capable of binding to the immobilized antibody-polypeptide complex is added. The amount of detection reagent that remains bound to the solid support is then determined using a method appropriate for the specific detection reagent. More specifically, once the poiypeptide 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) may be employed. The immobilized poiypeptide is then incubated with the sample, and antibody is allowed to bind to the antigen. The sample may be diluted with a suitable diluent, such as phosphate-buffered saline (PBS) prior to incubation. In general, an appropriate contact time, or incubation time, is that period of time that is sufficient to detect the presence of antibody within a M. tuberculosis-infected sample. Preferably, the contact time is sufficient to achieve a level of binding that is at least 95% of that achieved at equilibrium between bound and unbound antibody. 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 be removed by washing the solid support with an appropriate buffer, such as PBS containing 0.1% Tween 20™. Detection reagent may then be added to the solid support. An appropriate detection reagent is any compound that binds to the immobilized antibody-polypeptide complex and that can be detected by any of a variety of means known in the art. Preferably, the detection reagent contains a binding agent (such as, for example, Protein A, Protein G, immunoglobulin, lectin or free antigen) conjugated to a reporter group. Preferred reporter groups include enzymes (such as horseradish peroxidase), substrates, cofactors, inhibitors, dyes, radionuclides, luminescent groups, fluorescent groups and biotin. The conjugation of binding agent to reporter group may be achieved using standard methods known in the art. Common binding agents may also be purchased conjugated to a variety of reporter groups from many commercial sources (e.g., Zymed Laboratories, San Francisco, CA, and Pierce, Rockford, IL). The detection reagent is incubated with the immobilized antibody-polypeptide complex for an amount of time sufficient to detect the bound antibody. An appropriate amount of time may generally be determined from the manufacturer's instructions or 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 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 anti-mycobacterial antibodies in the sample, 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 preferred embodiment, the cut-off value is the average mean signal obtained when the immobilized antigen is incubated with samples from an uninfected patient. In an alternate preferred 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, pp. 106-107. In general, signals higher than the predetermined cut-off value are considered to be positive for mycobacterial infection. The assay may also be performed in a rapid flow-through or strip test format, wherein the antigen is immobilized on a membrane, such as nitrocellulose. In the flow-through test, antibodies within the sample bind to the immobilized poiypeptide as the sample passes through the membrane. A detection reagent (e.g., protein A- colloidal " gold) then binds to the antibody-polypeptide complex as the solution containing the detection reagent flows through the membrane. The detection of bound detection reagent may then be performed as described above. In the strip test format, one end of the membrane to which poiypeptide is bound is immersed in a solution containing the sample. The sample migrates along the membrane through a region containing detection reagent and to the area of immobilized poiypeptide. Concentration of detection reagent at the poiypeptide indicates the presence of anti- mycobacterial antibodies in the sample. Typically, the concentration of detection reagent 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 poiypeptide immobilized on the membrane is selected to generate a visually discernible pattern when the biological sample contains a level of antibodies that would be sufficient to generate a positive signal in an ELISA, as discussed above. Preferably, the amount of poiypeptide immobilized on the membrane ranges from about 25 ng to about 1 μg, and more preferably from about 50 ng to about 500 ng. Such tests can typically be performed with a very small amount (e g , one drop) of patient serum or blood. Numerous other assay protocols exist that are suitable for use with the polypeptides of the present invention. The above descriptions are intended to be exemplary only. The present invention also provides antibodies to the inventive polypeptides. 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 one such technique, an immunogen comprising the antigenic poiypeptide is initially injected into any of a wide variety of mammals (e.g., mice, rats, rabbits, sheep and goats). The immunogen is injected into the animal host, preferably according to a predetermined schedule incorporating one or more booster immunizations, and the animals are bled periodically. Polyclonal antibodies specific for the poiypeptide may then be purified from such antisera by, for example, affinity chromatography using the poiypeptide coupled to a suitable solid support. Monoclonal antibodies specific for the antigenic poiypeptide of interest may be prepared, for example, using the technique of Kohler and Mil stein, Eur. J Immunol. 6:5 \ 1-519, 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 poiypeptide of interest). Such cell lines may be produced, for example, from spleen cells obtained from an animal immunized as described above. The spleen cells may then be immortalized by fusion with a myeloma cell fusion partner, preferably one that is syngeneic with the immunized animal, using one of a variety of techniques well known in the art. Monoclonal antibodies may be isolated from the supernatants of the resulting hybridoma colonies. In addition, various techniques may be employed to enhance the yield, such as injection of the 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. Antibodies may be used in diagnostic tests to detect the presence of mycobacterial antigens using assays similar to those detailed above and other techniques well known to those of skill in the art, thereby providing a method for detecting mycobacterial infection, such as M. tuberculosis infection, in a patient. Diagnostic reagents of the present invention may also comprise DNA sequences encoding one or more of the above polypeptides, or one or more portions thereof. For example, primers comprising at least 10 contiguous oligonucleotides of the subject DNA sequences may be used in polymerase chain reaction (PCR) based tests. Similarly, probes comprising at least 18 contiguous oligonucleotides of the subject DNA sequences may be used for hybridizing to specific sequences. Techniques for both PCR based tests and hybridization tests are well known in the art. Primers or probes may thus be used to detect M. tuberculosis and other mycobacterial infections in biological samples, preferably sputum, blood, serum, saliva, cerebrospinal fluid or urine. DNA probes or primers comprising oligonucleotide sequences described above may be used alone, in combination with each other, or with previously identified sequences, such as the 38 kD antigen discussed above. As discussed above, effective vaccines contain at least two different components. The first is a poiypeptide comprising an antigen, which is processed by macrophages and other antigen-presenting cells and displayed for CD4 + T cells or for CD8 + T cells. This antigen forms the "specific" target of an immune response. The second component of a vaccine is a non-specific immune response amplifier, such as an adjuvant or a liposome, into which the antigen is incorporated. An adjuvant amplifies immune responses to a structurally unrelated compound or poiypeptide. Several adjuvants are prepared from microbes such as Bordetella pertussis, M. tuberculosis and M. bovis BCG. Adjuvants may also contain components designed to protect poiypeptide antigens from degradation, such as aluminum hydroxide or mineral oil. While the antigenic component of a vaccine contains polypeptides that direct the immune attack against a specific pathogen, such as M. tuberculosis, the adjuvant is often capable of broad use in many different vaccine formulations. Certain pathogens, such as M. tuberculosis, as well as certain cancers, are effectively contained by an immune attack directed by T cells, known as cell-mediated immunity. Other pathogens, such as poliovirus, also require antibodies produced by B cells for containment. These different classes of immune attack (T cell or B cell) are controlled by different subpopulations of CD4 + T cells, commonly referred to as Thl and Th2 cells. A desirable property of an adjuvant is the ability to selectively amplify the function of either Thl or Th2 populations of CD4 * T cells. As shown below in Example 6, M. vaccae and a modified form of autoclaved M. vaccae have been found to have adjuvant properties. As used herein, the term "modified M. vaccae" includes delipidated M. vaccae cells, deglycosylated M. vaccae cells and M. vaccae cells that have been both delipidated and deglycosylated (hereinafter referred to as DD-Λ . vaccae). Furthermore, it has been found that M. vaccae produces compounds which amplify the immune response to M. vaccae antigens, as well as to antigens from other sources. The present invention thus provides methods for enhancing immune responses to an antigen comprising administering killed M. vaccae cells, M. vaccae culture filtrate or modified M. vaccae cells. As detailed below, further studies have demonstrated that this non-specific immune amplifying effect is due, at least in part, to an M. vaccae poiypeptide having homology to heat shock protein 65 (GroEL), previously identified in M. tuberculosis. As described below in Example 10, it has also been found that heat-killed M. vaccae and M. vaccae constituents have cytokine stimulation properties. In particular, it has been found that heat-killed M. vaccae, lyophilised M. vaccae and DD- vaccae stimulate the production of interleukin 12 (IL-12) from macrophages. Production of IL-12 from macrophages is known to enhance stimulation of a Thl immune response. The following examples are offered by way of illustration and not by way of limitation. EXAMPLE 1 EFFECT OF IMMUNIZATION OF MICE WITH M VACCAE ON TUBERCULOSIS This example illustrates the effect of immunization with M vaccae or M. vaccae culture filtrate in mice prior to challenge with live M. tuberculosis. M. vaccae (ATCC Number 15483) was cultured in sterile Medium 90 (yeast extract, 2.5 g/1; tryptone, 5 g/1; glucose, 1 g/1) at 37 °C. The cells were harvested by centrifugation, and transferred into sterile Middlebrook 7H9 medium (Difco Laboratories, Detroit, MI, USA) with glucose at 37 °C for one day. The medium was then centrifuged to pellet the bacteria, and the culture filtrate removed. The bacterial pellet was resuspended in phosphate buffered saline at a concentration of 10 mg/ml, equivalent to 10'° M. vaccae organisms per ml. The cell suspension was then autoclaved for 15 min at 120 °C. The culture filtrate was passaged through a 0.45 μM filter into sterile bottles. As shown in Fig.lA, when mice were immunized with 1 mg, 100 μg or 10 μg of M. vaccae and infected three weeks later with 5x10 s colony forming units (CFU) of live M. tuberculosis H37Rv, significant protection from infection was seen. In this example, spleen, liver and lung tissue was harvested from mice three weeks after infection, and live bacilli determined (expressed as CFU). The reduction in bacilli numbers, when compared to tissue from non-immunized control mice, exceeded 2 logs in liver and lung tissue, and 1 log in spleen tissue. Immunization of mice with heat-killed M. tuberculosis H37Rv had no significant protective effects on mice subsequently infected with live M. tuberculosis H37Rv. Fig.1 B shows that when mice were immunized with 100 μg of M. vaccae culture filtrate, and infected three weeks later with 5x10 5 CFU of M. tuberculosis H37Rv, significant protection was also seen. When spleen, liver and lung tissue was harvested from mice three weeks after infection, and live bacilli numbers (CFU) determined, a 1-2 log reduction in numbers, as compared to non-immunized control mice, was observed. EXAMPLE 2 PURIFICATION AND CHARACTERIZATION OF POLYPEPTIDES FROM M. VACCAE CULTURE FILTRATE This example illustrates the preparation of M. vaccae soluble proteins from culture filtrate. Unless otherwise noted, all percentages in the following example are weight per volume. M. vaccae (ATCC Number 15483) was cultured in sterile Medium 90 at 37 °C. The cells were harvested by centrifugation, and transferred into sterile Middlebrook 7H9 medium with glucose at 37 °C for one day. The medium was then centrifuged (leaving the bulk of the cells) and filtered through a 0.45 μ filter into sterile bottles. The culture filtrate was concentrated by lyophilization, and redissolved in MilliQ water. A small amount of insoluble material was removed by filtration through a 0.45μ membrane. The culture filtrate was desalted by membrane filtration in a 400 ml A icon stirred cell which contained a 3,000 kilodalton molecular weight cut-off (MWCO) membrane. The pressure was maintained at 50 psi using nitrogen gas. The culture filtrate was repeatedly concentrated by membrane filtration and diluted with water until the conductivity of the sample was less than 1.0 mS. This procedure reduced the 20 I volume to approximately 50 ml. Protein concentrations were determined by the Bradford protein assay (Bio-Rad, Hercules, CA, USA). The " esalted culture filtrate was fractionated by ion exchange chromatography on a column of Q-Sepharose (Pharmacia Biotech, Uppsala, Sweden) (16 X 100 mm) equilibrated with lOmM Tris HCl buffer pH 8.0. Polypeptides were eluted with a linear gradient of NaCl from 0 to 1.0 M in the above buffer system. The column eluent was monitored at a wavelength of 280 nm. The pool of polypeptides eluting from the ion exchange column was concentrated in a 400 ml Amicon stirred cell which contained a 3,000 MWCO membrane. The pressure was maintained at 50 psi using nitrogen gas. The polypeptides were repeatedly concentrated by membrane filtration and diluted with 1% glycine until the conductivity of the sample was less than 0.1 mS. The purified polypeptides were then fractionated by preparative isoelectric focusing in a Rotofor device (Bio-Rad, Hercules, CA, USA). The pH gradient was established with a mixture of Ampholytes (Pharmacia Biotech) comprising 1.6% pH 3.5-5.0 Ampholytes and 0.4% pH 5.0 - 7.0 Ampholytes. Acetic acid (0.5 M) was used as the anolyte, and 0.5 M ethanolamine as the catholyte. Isoelectric focusing was carried out at 12W constant power for 6 hours, following the manufacturer's instructions. Twenty fractions were obtained. Fractions from isoelectric focusing were combined, and the polypeptides were purified on a Vydac C4 column (Separations Group, Hesperia, CA, USA) 300 Angstrom pore size, 5 micron particle size (10 x 250 mm). The polypeptides were eluted from the column with a linear gradient of acetonitrile (0-80% v/v) in 0.05% (v/v) trifluoroacetic acid (TFA). The flow-rate was 2.0 ml/min and the HPLC eluent was monitored at 220 nm. Fractions containing polypeptides were collected to maximize the purity of the individual samples. Relatively abundant poiypeptide fractions were rechromatographed on a Vydac C4 column (Separations Group) 300 Angstrom pore size, 5 micron particle size (4.6 x 250 mm). The polypeptides were eluted from the column with a linear gradient from 20-60% (v/v) of acetonitrile in 0.05% (v/v) TFA at a flow-rate of 1.0 ml/min. The column eluent was monitored at 220 nm. Fractions containing the eluted polypeptides were collected to maximise the purity of the individual samples. Approximately 20 poiypeptide samples were obtained and they were analysed for purity on " a polyacrylamide gel according to the procedure of Laemmli (Laemmli, U. K.. Nature 277:680-685. 1970). The poiypeptide fractions which were shown to contain significant contamination were further purified using a Mono Q column (Pharmacia Biotech) 10 micron particle size (5 x 50 mm) or a Vydac Diphenyl column (Separations Group) 300 Angstrom pore size, 5 micron particle size (4.6 x 250 mm). From a Mono Q column, polypeptides were eluted with a linear gradient from 0-0.5 M NaCl in 10 mM Tris HCl pH 8.0. From a Vydac Diphenyl column, polypeptides were eluted with a linear gradient of acetonitrile (20-60% v/v) in 0.1% TFA. The flow-rate was 1.0 ml/min and the column eluent was monitored at 220 nm for both columns. The poiypeptide peak fractions were collected and analysed for purity on a 15% polyacrylamide gel as described above. For sequencing, the polypeptides were individually dried onto Biobrene™ (Perkin Elmer/Applied BioSystems Division, Foster City, CA)-treated glass fiber filters. The filters with poiypeptide were loaded onto a Perkin Elmer/Applied BioSystems Procise 492 protein sequencer and the polypeptides were sequenced from the amino terminal end using traditional Edman chemistry. The amino acid sequence was determined for each poiypeptide by comparing the retention time of the PTH amino acid derivative to the appropriate PTH derivative standards. Internal sequences were also determined on some antigens by digesting the antigen with the endoprotease Lys-C, or by chemically cleaving the antigen with cyanogen bromide. Peptides resulting from either of these procedures were separated by reversed-phase HPLC on a Vydac C18 column using a mobile phase of 0.05% (v/v) trifluoroacetic acid with a gradient of acetonitrile containing 0.05% (v/v) TFA (1%/min). The eluent was monitored at 214 nm. Major internal peptides were identified by their UV absorbance, and their N-terminal sequences were determined as described above. Using the procedures described above, six soluble M. vaccae antigens, designated GVc-1, GVc-2, GVc-7, GVc-13, GVc-20 and GVc-22, were isolated. Determined N-terminal and internal sequences for GVc-1 are shown in SEQ ID NOS. 1, 2 and 3, respectively; the N-terminal sequence for GVc-2 is shown in SEQ ID NO: 4; internal sequences for GVc-7 are shown in SEQ ID NOS: 5-8; internal sequences for GVc-13 are shown in SEQ ID NOS: 9-11; internal sequence for GVc-20 is shown in SEQ ID NO: 12; and N-terminal and internal sequences for GVc-22 are shown in SEQ ID NO:56-59, respectively. Each of the internal peptide sequences provided herein begins with an amino acid residue which is assumed to exist in this position in the poiypeptide, based on the known cleavage specificity of cyanogen bromide (Met) or Lys-C (Lys). Three additional polypeptides, designated GVc-16, GVc-18 and GVc-21, were isolated employing a preparative sodium dodecyl sulfate-poiyacrylamide gel electrophoresis (SDS-PAGE) purification step in addition to the preparative isoelectric focusing procedure described above. Specifically, fractions comprising mixtures of polypeptides from the preparative isoelectric focusing purification step previously described, were purified by preparative SDS-PAGE on a 15% polyacrylamide gel. The samples were dissolved in reducing sample buffer and applied to the gel. The separated proteins were transferred to a polyvinylidene difluoride (PVDF) membrane by electroblotting in 10 mM 3-(cyclohexylamino)-l- propanesulfonic acid (CAPS) buffer pH 1 1 containing 10% (v/v) methanol. The transferred protein bands were identified by staining the PVDF membrane with Coomassie blue. Regions of the PVDF membrane containing the most abundant poiypeptide species were cut out and directly introduced into the sample cartridge of the Perkin Elmer/Applied BioSystems Procise 492 protein sequencer. Protein sequences were determined as described above. The N-terminal sequences for GVc- 16, GVc-18 and GVc-21 are provided in SEQ ID NOS: 13, 14 and 15, respectively. Additional antigens, designated GVc-12, GVc-14, GVc-15, GVc-17 and GVc- 19, were isolated employing a preparative SDS-PAGE purification step in addition to the chromatographic procedures described above. Specifically, fractions comprising a mixture of antigens from the Vydac C4 HPLC purification step previously described were fractionated by preparative SDS-PAGE on a polyacrylamide gel. The samples were dissolved in non-reducing sample buffer and applied to the gel. The separated proteins were transferred to a PVDF membrane by electroblotting in 10 mM CAPS buffer, pH 1 1 containing 10% (v/v) methanol. The transferred protein bands were identified "" by staining the PVDF membrane with Coomassie blue. Regions of the PVDF membrane containing the most abundant poiypeptide species were cut out and directly introduced into the sample cartridge of the Perkin Elmer/ Applied BioSystems Procise 492 protein sequencer. Protein sequences were determined as described above. The determined N-terminal sequences for GVc-12, GVc-14, GVc-15, GVc- 17 and GVc-19 are provided in SEQ ID NOS: 16-20, respectively. All of the above amino acid sequences were compared to known amino acid sequences in the SwissProt data base (version R32) using the GeneAssist system. No significant homologies to the amino acid sequences GVc-2 to GVc-22 were obtained. The amino acid sequence for GVc-1 was found to bear some similarity to sequences previously identified from M. bovis and M. tuberculosis. In particular, GVc-1 was found to have some homology with M. tuberculosis MPT83, a cell surface protein, as well as MPT70. These proteins form part of a protein family (Harboe et al., Scand. J. Immunol. 42:46-51 , 1995). Subsequent studies led to the isolation of DNA sequences for GVc-14 and GVc-22 (SEQ ID NO: 107 and 108, respectively). The corresponding predicted amino acid sequences for GVc-14 and GVc-22 are provided in SEQ ID NO: 109 and 1 10, respectively. Amplifications primers AD86 and AD1 12 (SEQ ID NO: 60 and 61 , respectively) were designed from the amino acid sequence of GVc-1 (SEQ ID NO: 1) and the M. tuberculosis MPT70 gene sequence. Using these primers, a 310 bp fragment was amplified from M. vaccae genomic DNA and cloned into £coRV- digested vector pBluescript (Stratagene) containing added dTTP residues. The sequence of the cloned insert is provided in SEQ ID NO: 62. The purified polypeptides were screened for the ability to induce T-cell proliferation and IFN-γ in peripheral blood cells from immune human donors. These donors were known to be PPD (purified protein derivative from M. tuberculosis) skin test positive and their T cells were shown to proliferate in response to PPD. Donor PBMCs and crude soluble proteins from M. vaccae culture filtrate were cultured in medium comprising RPMI 1640 supplemented with 10% (v/v) autologous serum, penicillin (60 μg/ml), streptomycin (100 μg/ml), and glutamine (2 mM). After " 3 days, 50 μl of medium was removed from each well for the determination of IFN-γ levels, as described below. The plates were cultured for a further 4 days and then pulsed with lμCi/well of tritiated thymidine for a further 18 hours, harvested and tritium uptake determined using a scintillation counter. Fractions that stimulated proliferation in both replicates two-fold greater than the proliferation observed in cells cultured in medium alone were considered positive. IFN-γ was measured using an enzyme-linked immunosorbent assay (ELISA). ELISA plates were coated with a mouse monoclonal antibody directed to human IFN- γ (Endogen, Wobural, MA) 1 μg/ml phosphate-buffered saline (PBS) for 4 hours at 4 °C. Wells were blocked with PBS containing 0.2% Tween 20 for 1 hour at room temperature. The plates were then washed four times in PBS/0.2% Tween 20. and samples diluted 1 :2 in culture medium in the ELISA plates were incubated overnight at room temperature. The plates were again washed, and a biotinylated polyclonal rabbit anti-human IFN-γ serum (Endogen), diluted to 1 μg/ml in PBS, was added to each well. The plates were then incubated for 1 hour at room temperature, washed, and horseradish peroxidase-coupled avidin A (Vector Laboratories, Burlingame, CA) was added at a 1 :4,000 dilution in PBS. After a further 1 hour incubation at room temperature, the plates were washed and orthophenylenediamine (OPD) substrate added. The reaction was stopped after 10 min with 10% (v/v) HCl. The optical density (OD) was determined at 490 nm. Fractions that resulted in both replicates giving an OD two-fold greater than the mean OD from cells cultured in medium alone were considered positive. Examples of polypeptides containing sequences that stimulate peripheral blood mononuclear cells (PBMC) T cells to proliferate and produce IFN-γ are shown in Table 1, wherein (-) indicates a lack of activity, (+/-) indicates polypeptides having a result less than twice higher than background activity of control media, (+) indicates polypeptides having activity two to four times above background, and (++) indicates polypeptides having activity greater than four times above background. EXAMPLE 3 PURIFICATION AND CHARACTERISATION OF POLYPEPTIDES FROM M. VACCAE CULTURE FILTRATE BY 2-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS M. vaccae soluble proteins were isolated from culture filtrate using 2- dimensional polyacrylamide gel electrophoresis as described below. Unless otherwise noted, all percentages in the following example are weight per volume. M. vaccae (ATCC Number 15483) was cultured in sterile Medium 90 at 37 °C. M. tuberculosis strain H37Rv (ATCC number 27294) was cultured in sterile Middlebrook 7H9 medium with Tween 80 and oleic acid/albumin/dextrose/catalase additive (Difco Laboratories, Detroit, Michigan). The cells were harvested by centrifugation, and transferred into sterile Middlebrook 7H9 medium with glucose at 37 °C for one day. The medium was then centrifuged (leaving the bulk of the cells) and filtered through a 0.45 μ filter into sterile bottles. The culture filtrate was concentrated by lyophilisation, and redissolved in MilliQ water. A small amount of insoluble material was removed by filtration through a 0.45μ membrane filter. The culture filtrate was desalted by membrane filtration in a 400 ml Amicon stirred cell which contained a 3,000 MWCO membrane. The pressure was maintained at 60 psi using nitrogen gas. The culture filtrate was repeatedly concentrated by membrane filtration and diluted with water until the conductivity of the sample was less than 1.0 mS. This procedure reduced the 20 L volume to approximately 50 mL. Protein concentrations were determined by the Bradford protein assay (Bio-Rad, Hercules, CA, USA). The desalted culture filtrate was fractionated by ion exchange chromatography on a column of Q-Sepharose (Pharmacia Biotech) (16 x 100 mm) equilibrated with lOmM TrisHCL buffer pH 8.0. Polypeptides were eluted with a linear gradient of NaCl from 0 to 1.0 M in the above buffer system. The column eluent was monitored at a wavelength of 280 nm. The pool of polypeptides eluting from the ion exchange column were fractionated by preparative 2D gel electrophoresis. Samples containing 200-500 ug of poiypeptide were made 8M in urea and applied to polyacrylamide isoelectric focusing rod gels (diameter 2mm, length 150 mm, pH 5-7). After the isoelectric focusing step, the first dimension gels were equilibrated with reducing buffer and applied to second dimension gels (16% polyacrylamide). Figs. 2A and 2B are the 2-D gel patterns observed with M. vaccae culture filtrate and M. tuberculosis H37Rv culture filtrate, respectively. Polypeptides from the second dimension separation were transferred to PVDF membranes by electroblotting in lOmM CAPS buffer pH 11 containing 10% (v/v) methanol. The PVDF membranes were stained for protein with Coomassie blue. Regions of PVDF containing polypeptides of interest were cut out and directly introduced into the sample cartridge of the Perkin Elmer/ Applied BioSystems Procise 492 protein sequencer. The polypeptides were sequenced from the amino terminal end using traditional Edman chemistry. The amino acid sequence was determined for each poiypeptide by comparing the retention time of the PTH amino acid derivative to the appropriate PTH derivative standards. Using these procedures, eleven polypeptides, designated GVs-1 , GVs-3, GVs-4, GVs-5, GVs-6, GVs-8, GVs-9, GVs- 10, GVs-1 1, GV-34 and GV-35 were isolated. The determined N-terminal sequences for these polypeptides are shown in SEQ ID NOS: 21-29, 63 and 64, respectively. Using the purification procedure described above, more protein was purified to extend the amino acid sequence previously obtained for GVs-9. The extended amino acid sequence for GVs-9 is provided in SEQ ID NO:65. Further studies resulted in the isolation of the DNA sequence for GVs-9 (SEQ ID NO: 111). The corresponding predicted amino acid sequence is provided in SEQ ID NO: 1 12. All of these amino acid sequences were compared to known amino acid sequences in the SwissProt data base (version R32) using the GeneAssist system. No significant homologies were obtained, with the exceptions of GVs-3, GVs-4, GVs-5 and GVs-9. GVs-9 was found to bear some homology to two previously identified M. tuberculosis proteins, namely M. tuberculosis cutinase precursor and an M. tuberculosis hypothetical 22.6 kD protein. GVs-3, GVs-4 and GVs-5 were found to bear some similarity to the antigen 85A and 85B proteins from M. leprae (SEQ ID NOS: 30 and 31, respectively), M. tuberculosis (SEQ ID NOS: 32 and 33, respectively) and M. bovis (SEQ ID NOS: 34 and 35, respectively), and the antigen 85C proteins from M. leprae (SEQ ID NO: 36) and M. tuberculosis (SEQ ID NO: 37). A comparison of the inventive antigen 85A protein from M. vaccae with those from M. tuberculosis. M. bovis and M. leprae, is presented in Fig. 3. EXAMPLE 4 DNA CLONING STRATEGY FOR THE M. VACCAE ANTIGEN 85 SERIES Probes for antigens 85A, 85B, and 85C (SEQ ID NOS: 38 and 39) were prepared by the polymerase chain reaction (PCR) using degenerate oligonucleotides designed to regions of antigen 85 genomic sequence that are conserved between family members in a given mycobacterial species, and between mycobacterial species. These oligonucleotides were used under reduced stringency conditions to amplify target sequences from M. vaccae genomic DNA. An appropriately-sized 0.5kb band was identified, purified, and cloned into T-tailed p Bluescript II SK (Stratagene, La Jolla, CA). Twenty-four individual colonies were screened at random for the presence of the antigen 85 PCR product, then sequenced using the Perkin Elmer/Applied Biosystems Model 377 automated sequencer and the M13-based primers, T3 and T7. Homology searches of the GenBank databases showed that twenty-three clones contained insert with significant homology to published antigen 85 genes from M. tuberculosis ' and M. bovis. Approximately half were most homologous to antigen 85C gene sequences, with the remainder being more similar to antigen 85B sequences. In addition, these two putative M. vaccae antigen 85 genomic sequences were 80% homologous to one another. Because of this high similarity, the antigen 85C PCR fragment was chosen to screen M. vaccae genomic libraries at low stringency for all three antigen 85 genes. An M. vaccae genomic library was created in λ ZapExpress (Stratagene, La Jolla, CA) by cloning BamHl partially-digested M. vaccae genomic DNA into similarly-digested λ vector, with 3.4 x 10 5 independent plaque-forming units resulting. For screening purposes, twenty-seven thousand plaques from this non- amplified library were plated at low density onto eight 100 cm : plates. For each plate, duplicate plaque lifts were taken onto Hybond-N " nylon membrane (Amersham International. United Kingdom), and hybridised under reduced-stringency conditions (55 °C) to the radiolabelled antigen 85C PCR product. Autoradiography demonstrated that seventy-nine plaques consistently hybridised to the antigen 85C probe under these conditions. Thirteen positively-hybridising plaques were selected at random for further analysis and removed from the library plates, with each positive clone being used to generate secondary screening plates containing about two hundred plaques. Duplicate lifts of each plate were taken using Hybond-N + nylon membrane, and hybridised under the conditions used in primary screening. Multiple positively-hybridising plaques were identified on each of the thirteen plates screened. Two well-isolated positive phage from each secondary plate were picked for further analysis. Using in vitro excision, twenty-six plaques were converted into phagemid, and restriction-mapped. It was possible to group clones into four classes on the basis of this mapping. Sequence data from the 5' and 3' ends of inserts from several representatives of each group was obtained using the Perkin Elmer/Applied Biosystems Model 377 automated sequencer and the T3 and T7 primers. Sequence homologies were determined using FASTA analysis of the GenBank databases with the GeneAssist software package. Two of these sets of clones were found to be homologous to M. bovis and M. tuberculosis antigen 85A genes, each containing either the 5' or 3' ends of the M. vaccae gene (this gene was cleaved during library construction as it contains an internal Bam l site). The remaining clones were found to contain sequences homologous to antigens 85B and 85C from a number of mycobacterial species. To determine the remaining nucleotide sequence for each gene, appropriate subclones were constructed and sequenced. Overlapping sequences were aligned using the DNA Strider software. The determined DNA sequences for M. vaccae antigens 85 A, 85B and 85C are shown in SEQ ID NOS: 40-42, respectively, with the predicted amino acid sequences being shown in SEQ ID NOS: 43-45, respectively. The M. vaccae antigens GVc-3 and GVc-5 were expressed and purified as follows. Amplification primers were designed from the insert sequences of GVc-3 and GVc-5 (SEQ ID NO: 40 and 42, respectively) using sequence data downstream from the putative leader sequence and the 3' end of the clone. The sequences of the primers for GVc-3 are provided in SEQ ID NO: 66 and 67. and the sequences of the primers for GVc-5 are provided in SEQ ID NO: 68 and 69. A Xhol restriction site was added to the primers for GVc-3, and EcoRl and Bamlil restriction sites were added to the primers for GVc-5 for cloning convenience. Following amplification from genomic M. vaccae DNA, fragments were cloned into the appropriate site of pProEX HT prokaryotic expression vector (Gibco BRL, Life Technologies, Gaithersburg, MD) and submitted for sequencing to confirm the correct reading frame and orientation. Expression and purification of the recombinant protein was performed according to the manufacturer's protocol. Expression of a fragment of the M. vaccae antigen GVc-4 (antigen 85B homolog) was performed as follows. The primers AD58 and AD59, described above, were used to amplify a 485 bp fragment from M. vaccae genomic DNA. This fragment was gel- purified using standard techniques and cloned into £cσRV-digested pBluescript containing added dTTP residues. The base sequences of inserts from five clones were determined and found to be identical to each other. These inserts had highest homology to Ag85B from M. tuberculosis. The insert from one of the clones was subcloned into the EcoRI/Xhol sites of pProEX HT prokaryotic expression vector (Gibco BRL), expressed and purified according to the manufacturer's protocol. This clone was renamed GVc-4P because only a part of the gene was expressed. The amino aci " and DNA sequences for the partial clone GVc-4P are provided in SEQ ID NO: 70 and 106, respectively. In subsequent studies, using procedures similar to those described above, GVc-3, GVc-4P and GVc-5 were re-cloned into the alternative vector pET16 (Novagen, Madison, WI). The ability of purified recombinant GVc-3, GVc-4P and GVc-5 to stimulate proliferation of T cells and interferon-γ production in human PBL from PPD-positive, healthy donors, was assayed as described above in Example 2. The results of this assay are shown in Table 2, wherein (-) indicates a lack of activity, (+/-) indicates polypeptides having a result less than twice higher than background activity of control media, (+) indicates polypeptides having activity two to four times above background, (++) indicates polypeptides having activity greater than lour times above background, and ND indicates not determined Table 2 EXAMPLE 5 DNA CLONING STRATEGY FOR M VACCAE ANTIGENS An 84 bp probe for the M vaccae antigen GVc-7 was amplified using degenerate oligonucleotides designed to the determined amino acid sequence of GVc- 7 (SEQ ID NOS: 5-8) This probe was used to screen a M vaccae genomic DNA library as described in Example 4. The determined nucleotide sequence fo: GVc-7 is shown in SEQ ID NO 1 46 and predicted amino acid sequence in SEQ ID NO 47 Comparison of these sequences with those in the databank revealed homology to a hypothetical 15.8 kDa membrane protein of M tuberculosis The sequence of SEQ ID NO 46 was used to design amplification primers (provided in SEQ ID NO 71 and 72) for expression cloning of the GVc-7 gene using sequence data downstream from the putative leader sequence A Xhol restriction site was added to the primers for cloning convenience Following amplification from genomic M vaccae DNA, fragments were cloned into the of pProEX HT prokaryotic expression vector (Gibco BRL) and submitted for sequencing to confirm the correct reading frame and orientation. Expression and purification of the fusion protein was performed according to the manufacturer ' s protocol. In subsequent studies, GVc-7 was re-cloned into the vector pET16 (Novagen). The ability of purified recombinant GVc-7 to stimulate proliferation of T-cells and stimulation of interferon-γ production in human PBL, from PPD-positive, healthy donors, was assayed as described previously in Example 2. The results are shown in Table 3, wherein (-) indicates a lack of activity, (+/-) indicates polypeptides having a result less than twice higher than background activity of control media, (+) indicates polypeptides having activity two to four times above background, and (++) indicates polypeptides having activity greater than four times above background. TABLE 3 A redundant oligonucleotide probe was designed to the GVs-8 peptide sequence shown in SEQ ID NO: 6 and used to screen an M. vaccae genomic DNA library as described above. Positive plaques were isolated. Four different genomic clones were identified, hereinafter referred to as GVs- 8A, GVs-8B and GVs-8C and GVs-8D. The determined DNA sequences for the clones GVs-8A, GVs-8B, GVs-8C and GVs-8D are shown in SEQ ID NOS: 48-51, respectively, with the corresponding amino acid sequences being shown in SEQ ID NOS: 52-55, respectively. The clone GVs-8A contains regions showing some similarity to known prokaryotic valyi-tRNA synthetases; GVs-8B shows some similarity to M. smegmatis aspartate semialdehyde dehydrogenase; and GVs-8C shows some similarity to the H. influenza folylpolyglutamate synthase gene. GVs-8D contains an open reading frame which shows some similarity to sequences previously identified in M. tuberculosis and M. leprae, but whose function has not been identified. In subsequent studies, the M. vaccae genomic DNA library constructed in the BamHl -site of lambda ZAP Express vector (Stratagene) was screened with a second redundant oligonucleotide (referred to as MPG15; SEQ ID NO:73) designed from the GVs-8 sequence provided in SEQ ID NO:6. Screening of the library was performed in the presence of tetramethylammonium chloride (TMAC), so that nucleotide base pairs would melt at a standard temperature independent of sequence (i.e. A-T pairs and G-C pairs melt at the same temperature). Hybridisation stringency therefore depended only on the length and degeneracy of the oligonucleotide used as probe (Wood et al. Proc. Nad. Acad. Sci. USA, 52: 1585- 1588,1985). Filters were prepared using standard methods of transfer and pre-hybridised overnight at a temperature -15 °C below the appropriate TMAC wash temperature. Hybridisation was performed overnight in freshly prepared hybridisation solution containing 100 pmol probe. Hybridisation Solution for Oligonucleotides Stock: 1 M NaCl 5 M 0.1 M Tris pH 8 1 M 5X Denhardt's l00X 0.05% NaPPi 5% 0.1% SDS 10% 0. fmg/ml yeast tRNA 10 mg/ml 125 units/ml heparin The filters were washed at a temperature calculated to allow approximately 4 % mismatching in TMAC wash buffer. More specifically, the wash protocol included the following washing steps: 2 x 15 min in 6X SSC, 0.05% NaPPi at room temp; 1 x 15 min in TMAC wash (see below) at room temperature; 2 x 15 min in TMAC wash at the calculated stringent temperature; and 1 x 15 min in 6X SSC, 0.05% NaPPi at room temp. TMAC wash buffer 3 M Tetramethylammonium chloride (TMAC) 50 mM Tris pH 8.0 0.2 mM EDTA Positive plaques were picked and stored in 1 ml SM buffer with 20 μl chloroform. Screening was repeated until plaques were pure following the procedure described above. The pBK-CMV phagemid containing the desired insert was excised from the lambda ZAP Express vector in the presence of ExAssist helper phage following the manufacturer's protocol. A phagemid containing an 8 kb insert (GVs-8D) was characterised by restriction mapping and sub-cloning. An open reading frame was identified at the 3' end of the insert and the antigen encoded by this open reading frame was named GV-33. Base sequence corresponding to GVs-8 was not found in the insert, and it was assumed that GV-33 was obtained as a non-specific product of the TMAC screening. By further sub-cloning and base sequencing, the 3' end of the gene was determined. The determined partial DNA sequence for GV-33 is provided in SEQ ID NO:74 with the corresponding predicted amino acid sequence being provided in SEQ ID NO:75. Sequence data from the 3' end of the clone showed homology to a previously identified 40.6 kDa outer membrane protein of M. tuberculosis. TKe " partial GV-33 gene was amplified from M. vaccae genomic DNA with primers based on the determined nucleotide sequence. This DNA fragment was cloned into EcoRv-digested pBluescript (Stratagene) with additional dTTP residues, and then transferred to pProEX HT expression vector (Gibco BRL) using EcoRl and Hindlll-subcloning. Recombinant protein was purified following the manufacturer's protocol. In subsequent studies, GV-33 was re-cloned into the alternative vector pET16 (Novagen). The ability of purified recombinant antigen to stimulate proliferation of T-cells and stimulation of interferon-γ production in human PBL from PPD-positive, healthy donors, was assayed as described previously in Example 2. The results are shown in Table 4, wherein (-) indicates a lack of activity. (+/-) indicates polypeptides having a result less than twice higher than background activity oϊ control media, (+) indicates polypeptides having activity two to four times above background, and (++) indicates polypeptides having activity greater than four times above background. TABLE 4 EXAMPLE 6 DETECTION OF NONSPECIFIC IMMUNE AMPLIFIER FROM WHOLE M. VACCAE AND THE CULTURE FILTRATE OF M. VACCAE This example illustrates the preparation of whole M. vaccae and M. vaccae culture filtrate and its non-specific immune amplifying or 'adjuvant' property. M. vaccae bacteria was cultured, pelleted and autoclaved as described in Example 1. Culture filtrates of live M. vaccae refer to the supernatant from 24 hour cultures of M. vaccae in 7H9 medium with glucose. A delipidated form of M. vaccae was prepared by sonicating autoclaved M. vaccae for four bursts of 30 seconds on ice using the Virsonic sonicator (Virtis, Disa, USA). The material was then centrifuged (9000 rpm, 20 minutes, JA10 rotor, brake = 5). The resulting pellet was suspended in 100 ml of chloro form/methanol (2:1), incubated at room temperature for 1 hour; recentrifuged, and the chloroform methanol extraction repeated. The pellet was obtained by centrifugation, dried in vacuo, weighed and resuspended in PBS at 50mg (dry weight) per ml as delipidated M. vaccae. Glycolipids were removed from the delipidated M. vaccae preparation by refluxing in 50% v/v ethanol for 2 hours. The insoluble material was collected by centrifugation (10,000 rpm, JA20 rotor, 15 mins, brake = 5). The extraction with 50% v/v ethanol ' under reflux was repeated twice more. The insoluble material was collected by centrifugation and washed in PBS. Proteins were extracted by resuspending the pellet in 2% SDS in PBS at 56 °C for 2 hours. The insoluble material was collected by centrifugation and the extraction with 2% SDS/PBS at 56 °C was repeated twice more. The pooled SDS extracts were cooled to 4 °C, and precipitated SDS was removed by centrifugation (10,000 rpm, JA20 rotor, 15 mins, brake = 5). Proteins were precipitated from the supernatant by adding an equal volume of acetone and incubating at -20 °C for 2 hours. The precipitated proteins were collected by centrifugation, washed in 50% v/v acetone, dried in vacuo, and redissolved in PBS. M. vaccae culture supernatant (S N), killed M. vaccae and delipidated M. vaccae were tested for adjuvant activity in the generation of cytotoxic T cell immune response to ovalbumin, a structurally unrelated protein, in the mouse. This anti- ovalbumin-specific cytotoxic response was detected as follows. C57BL/6 mice (2 per group) were immunized by the intraperitoneal injection of 100 μg of ovalbumin with the following test adjuvants: autoclaved M. vaccae; delipidated M. vaccae; delipidated M. vaccae with glycolipids also extracted and proteins extracted with SDS; the SDS protein extract treated with pronase (an enzyme which degrades protein); whole M. vaccae culture filtrate; and heat-killed M. tuberculosis or heat- killed M. bovis BCG, M. phlei or M. smegmatus or M. vaccae culture filtrate. After 10 days, spleen cells were stimulated in vitro for a further 6 days with E.G7 cells which are EL4 cells (a C57BL/6-derived T cell lymphoma) transfected with the ovalbumin gene and thus express ovalbumin. The spleen cells were then assayed for their ability to kill non-specifically EL4 target cells or to kill specifically the E.G7 ovalbumin expressing cells. Killing activity was detected by the release of 5 I Chromium with which the EL4 and E.G7 cells have been labelled (100 μCi per 2xl0 6 ), prior to the killing assay. Killing or cytolytic activity is expressed as % specific lysis using the formula: cpm in test cultures - cpm in control cultures xl00% _ . total cpm - cpm in control cultures It is generally known that ovalbumin-specific cytotoxic cells are generated only in mice immunized with ovalbumin with an adjuvant but not in mice immunized with ovalbumin alone. The diagrams that make up Fig. 4 show the effect of various M. vaccae derived adjuvant preparations on the generation of cytotoxic T cells to ovalbumin in C57BL/6 mice. As shown in Fig. 4A, cytotoxic cells were generated in mice immunized with (i) 10 μg, (ii) 100 μg or (iii) 1 mg of autoclaved M. vaccae or (iv) 75 μg of M. vaccae culture filtrate. Fig. 4B shows that cytotoxic cells were generated in mice immunized with (i) 1 mg whole autoclaved M. vaccae or (ii) 1 mg delipidated M. vaccae. As shown in Fig. 4C(i), cytotoxic cells were generated in mice immunized with 1 mg whole autoclaved M. vaccae; Fig. 4C(ii) shows the active material in 100 μg delipidated M. vaccae which then had glycolipids removed and the proteins extracted with SDS. Fig. 4C(iii) shows that active material in the adjuvant preparation of Fig. 4C(ii) was destroyed by treatment with the proteolytic enzyme pronase. By way of comparison, 100 μg of the SDS-extracted proteins had significantly stronger immune-enhancing ability (Fig. 4C(ii)) than did 1 mg whole autoclaved M. vaccae (Fig. 4C(i)). Mice immunized with 1 mg heat-killed M. vaccae (Fig. 4D(i)) generated cytotoxic cells to ovalbumin, but mice immunized separately with 1 mg heat-killed M. tuberculosis (Fig. 4D(ii)), 1 mg M. bovis BCG (Fig. 4D(iii)), 1 mg M. phlei (Fig. 4D(iv)), or 1 mg M smegmatis (Fig. 4D(v)) failed to generate cytotoxic cells. The SDS-extracted proteins derived from delipidated and deglycolipidated M. vaccae were analysed by polyacrylamide gel electrophoresis. As shown in Fig. 5, three major bands were observed after staining with silver. In subsequent studies, more of the SDS-extracted proteins described above were prepared by preparative SDS-PAGE on a BioRad Prep Cell (Hercules, CA). Fractions corresponding to molecular weight ranges were precipitated by trichloroacetic acid to remove SDS before assaying for adjuvant activity in the anti- ovalbumin^pecific cytotoxic response assay in C57BL/6 mice as described above. As seen in Fig. 6, the adjuvant activity was highest in the 60-70 kDa fraction. The most abundant protein in this size range was purified by SDS-PAGE blotted on to a polyvinylidene difluoride (PVDF) membrane and then sequenced. The sequence of the first ten amino acid residues is provided in SEQ ID NO:76. Comparison of this sequence with those in the gene bank as described above, revealed homology to the heat shock protein 65 (GroEL) gene from M. tuberculosis, indicating that this protein is an M. vaccae member of the GroEL family. An expression library of M. vaccae genomic DNA in BamHl -lambda ZAP Express (Stratagene) was screened using sera from cynomolgous monkeys immunised with M. vaccae secreted proteins prepared as described above. Positive plaques were identified using a colorimetric system. These plaques were re-screened until plaques were pure following standard procedures. pBK-CMV phagemid 2-1 containing an insert was excised from the lambda ZAP Express (Stratagene) vector in the presence of ExAssist helper phage following the manufacturer ' s protocol. The base sequence of the 5' end of the insert of this clone, hereinafter referred to as GV-27, was determined using Sanger sequencing with fluorescent primers on Perkin Elmer/Applied Biosystems Dvision automatic sequencer. The determined nucleotide sequence of the partial M. vaccae GroEL-homologue clone GV-27 is provided in SEQ ID NO:77 and the predicted amino acid sequence in SEQ ID NO:78. This clone was found to have homology to M. tuberculosis GroEL. A partial sequence of the 65 kDa heat shock protein of M. vaccae has been published by Kapur et al. (Arch. Pathol. Lab. Med. 7/9 :131-138, 1995). The nucleotide sequence of the Kapur et al. fragment is shown in SEQ ID NO:79 and the predicted amino acid sequence in SEQ ID NO:80. In subsequent studies, a full-length (except for the predicted 51 terminal nucleotides) DNA sequence for GV-27 was obtained (SEQ ID NO: 1 13). The corresponding predicted amino acid sequence is provided in SEQ ID NO: 1 14. GV- 27 was found to be 93.7% identical to the M. tuberculosis GroEL at the amino acid level. Two peptide fragments, comprising the N-terminal sequence (hereinafter referred to as GV-27A) and the carboxy terminal sequence of GV-27 (hereinafter referred tό~as GV-27B) were prepared using techniques well known in the art. The nucleotide sequences for GV-27A and GV-27B are provided in SEQ ID NO: 1 15 and 116, respectively, with the corresponding amino acid sequences being provided in SEQ ID NO: 1 17 and 1 18. The sequence of GV-27A is 95.8% identical to the M. tuberculosis GroEL sequence and contains the shorter M. vaccae sequence of Kapur et al. discussed above. The sequence for GV-27B shows about 92.2% identity to the corresponding region of M. tuberculosis HSP65. The M. vaccae culture filtrate described above was also fractionated by iso- electric focusing and the fractions assayed for adjuvant activity in the anti-ovalbumin- specific cytotoxic response assay in C57BL/6 mice as described above. As shown in Fig. 7, peak adjuvant activities were demonstrated in fractions corresponding to pi of 4.2-4.32 (fraction nos. 7-9), 4.49-4.57 (fraction nos. 13-17) and 4.81-5.98 (fraction nos. 23-27). EXAMPLE 7 AUTOCLAVED M. VACCAE GENERATES CYTOTOXIC CD8 T CELLS AGAINST M. TUBERCULOSIS INFECTED MACROPHAGES This example illustrates the ability of killed M. vaccae to stimulate cytotoxic CD8 T cells which preferentially kill macrophages that have been infected with M tuberculosis. Mice were immunized by the intraperitoneal injection of 500 μg of killed M. vaccae which was prepared as described in Example 1. Two weeks after immunization, the spleen cells of immunized mice were passed through a CD8 T cell enrichment column (R&D Systems, St. Paul, MN, USA). The spleen cells recovered from the column have been shown to be enriched up to 90% CD8 T cells. These T cells, as well as CD8 T cells from spleens of non-immunized mice, were tested for their ability to kill uninfected macrophages or macrophages which have been infected with M. tuberculosis. Macrophages were obtained from the peritoneal cavity of mice five days after they have~been given 1 ml of 3% thioglycolate intraperitoneally. The macrophages were infected overnight with M. tuberculosis at the ratio of 2 mycobacteria per macrophage. All macrophage preparations were labelled with 51 Chromium at 2 μci per 10 4 macrophages. The macrophages were then cultured with CD8 T cells overnight (16 hours) at killer to target ratios of 30:1. Specific killing was detected by the release of 51 Chromium and expressed as % specific lysis, calculated as in Example 5. The production of IFN-γ and its release into medium after 3 days of co-culture of CD8 T cells with macrophages was measured using an enzyme-linked immunosorbent assay (ELISA). ELISA plates were coated with a rat monoclonal antibody directed to mouse IFN-γ (Pharmigen, San Diego, CA, USA) in PBS for 4 hours at 4 °C. Wells were blocked with PBS containing 0.2% Tween 20 for 1 hour at room temperature. The plates were then washed four times in PBS containing 0.2% Tween 20, and samples diluted 1 :2 in culture medium in the ELISA plates were incubated overnight at room temperature. The plates were again washed, and a biotinylated monoclonal rat anti-mouse IFN-γ antibody (Pharmigen), diluted to 1 μg/ml in PBS, was added to each well. The plates were then incubated for 1 hour at room temperature, washed, and horseradish peroxidase-coupled avidin D (Sigma A- 3151) was added at a 1 :4,000 dilution in PBS. After a further 1 hour incubation at room temperature, the plates were washed and OPD substrate added. The reaction was stopped after 10 min with 10% (v/v) HCl. The optical density was determined at 490 nm. Fractions that resulted in both replicates giving an OD two-fold greater than the mean OD from cells cultured in medium alone were considered positive. As shown in Table 5, CD8 T cells from spleens of mice immunized with M. vaccae were cytotoxic for macrophages infected with M. tuberculosis and did not lyse uninfected macrophages. The CD8 T cells from non-immunized mice did not lyse macrophages. CD8 T cells from naive or non-immunized mice do produce IFN-γ when cocultured with infected macrophages. The amount of IFN-γ produced in coculture was greater with CD8 T cells derived from M. vaccae immunized mice. TABLE 5 EFFECT WITH M. TUBERCULOSIS INFECTED AND UNINFECTED MACROPHAGES % Specific Lysis IFN-γ (ng ml) of Macrophages CD8 T cells uninfected infected uninfected infected Control 0 0 0.7 24.6 M. vaccae Immunized 0 95 2.2 43.8 EXAMPLE 8 DNA CLONING STRATEGY FOR THE M. VACCAE ANTIGENS GV-23. GV-24. GV-25. GV-26. GV-38A AND GV-38B M. vaccae (ATCC Number 15483) was grown in sterile Medium 90 at 37 °C for 4 days and harvested by centrifugation. Cells were resuspended in 1 ml Trizol (Gibco BRL, Life Technologies, Gaithersburg, Maryland) and RNA extracted according to the standard manufacturer ' s protocol. M. tuberculosis strain H37Rv (ATCC Number 27294) was grown in sterile Middlebrooke 7H9 medium with Tween 80™ and oleic acid/ albumin dextrose/catalase additive (Difco Laboratories, Detroit, Michigan) at 37 °C and harvested under appropriate laboratory safety conditions. Cells were resuspended in 1 ml Trizol (Gibco BRL) and RNA extracted according to the manufacturer's standard protocol. Total M. tuberculosis and M. vaccae RNA was depleted of 16S and 23 S ribosomal RNA (rRNA) by hybridisation of the total RNA fraction to oligonucleotides AD 10 and ADH (SEQ ID NO: 81 and 82) complementary to M. tuberculosis rRNA. These oligonucleotides were designed from mycobacterial 16S rRNA sequences published by Bottger (FEMS Microbiol. Lett. 65: 171 - 176, 1989) and from sequences deposited in the databanks. Depletion was done by hybridisation of total RNA~fo oligonucleotides AD10 and ADH immobilised on nylon membranes (Hybond N, Amersham International, United Kingdom). Hybridisation was repeated until rRNA bands were not visible on ethidium bromide-stained agarose gels. An oligonucleotide, AD 12 (SEQ ID NO: 83), consisting of 20 dATP-residues, was ligated to the 3' ends of the enriched mRNA fraction using RNA ligase. First strand cDNA synthesis was performed following standard protocols, using oligonucleotide AD7 (SEQ ID NO:84) containing a poly(dT) sequence. The M. tuberculosis and M. vaccae cDNA was used as template for single- sided-specific PCR (3S-PCR). For this protocol, a degenerate oligonucleotide AD1 (SEQ ID NO:85) was designed based on conserved leader sequences and membrane protein sequences. After 30 cycles of amplification using primer AD 1 as 5'-primer and AD7 as 3'-primer, products were separated on a urea/polyacrylamide gel. DNA bands unique to M vaccae were excised and re-amplified using primers AD1 and AD7. After gel purification, bands were cloned into pGEM-T (Promega) and the base sequence determined. Searches with the determined nucleotide and predicted amino acid sequences of band 12B21 (SEQ ID NOS: 86 and 87, respectively) showed homology to the pota gene of E.coli encoding the ATP-binding protein of the spermidine/putrescine ABC transporter complex published by Furuchi et al. (Jnl Biol Chem. 266: 20928-20933, 1991 ). The spermidine/putrescine transporter complex of E.coli consists of four genes and is a member of the ABC transporter family. The ABC (ATP-binding Cassette) transporters typically consist of four genes: an ATP-binding gene, a periplasmic, or substrate binding, gene and two transmembrane genes. The transmembrane genes encode proteins each characteristically having six membrane- spanning regions. Homologues (by similarity) of this ABC transporter have been identified in the genomes of Haemophilus influenza (Fleischmann et al. Science 269 :496-512, 1995) and Mycoplasma genitalium (Fraser, et al. Science, 270:391-403, 1995). An M. vaccae genomic DNA library constructed in BamHl -digested lambda ZAP Express (Stratagene) was probed with the radiolabelled 238 bp band 12B21 following standard protocols. A plaque was purified to purity by repetitive screening and a phagemid containing a 4.5 kb insert was identified by Southern blotting and hybridisation. The nucleotide sequence of the full-length M. vaccae homologue of pota (ATP-binding protein) was identified by subcloning of the 4.5 kb fragment and base sequencing. The gene consisted of 1449 bp including an untranslated 5' region of 320 bp containing putative -10 and -35 promoter elements. The nucleotide and predicted amino acid sequences of the M. vaccae pota homologue are provided in SEQ ID NOS:88 and 89, respectively. The nucleotide sequence of the M. vaccae pota gene was used to design primers EV24 and EV25 (SEQ ID NO: 90 and 91) for expression cloning. The amplified DNA fragment was cloned into pProEX HT prokaryotic expression system (Gibco BRL) and expression in an appropriate E.coli host was induced by addition of 0.6 mM isopropylthio-β-galactoside (IPTG). The recombinant protein was named GV-23 and purified from inclusion bodies according to the manufacturer ' s protocol. In subsequent studies, GV-23 (SEQ ID NO: 88) was re-cloned into the alternative vector pETl 6 (Novagen). A 322 bp Sall-BamHl subclone at the 3'-end of the 4.5 kb insert described above showed homology to the potd gene, (periplasmic protein), of the spermidine/putrescine ABC transporter complex of E. coll The nucleotide sequence of this subclone is shown in SEQ ID NO:92. To identify the gene, the radiolabelled insert of this subclone was used to probe an M. vaccae genomic DNA library constructed in the Sail -site of lambda Zap Express (Stratagene) following standard protocols. A clone was identified of which 1342 bp showed homology with the potd gene of E. coli. The potd homologue of M. vaccae was identified by sub-cloning and base sequencing. The determined nucleotide and predicted amino acid sequences are shown in SEQ ID NO: 93 and 94. For expression cloning, primers EV26 and EV27 (SEQ ID NOS.95-96) were designed from the determined M. vaccae potd homologue. The amplified fragment was cloned into pProEX HT Prokaryotic expression system (Gibco BRL). Expression in an appropriate E. coli host was induced by addition of 0.6 mM IPTG and the recombinant protein named GV24. The recombinant antigen was purified from inclusion bodies according to the protocol of the supplier. In subsequent studies, GV- 24 (SEQ ID ' NO: 93) was re-cloned into the alternative vector pET16 (Novagen). The ability of purified recombinant protein GV-23 and GV-24 to stimulate proliferation of T cells and interferon- production in human PBL was determined as described in Example 2. The results of these assays are provided in Table 6, wherein (-) indicates a lack of activity, (+/-) indicates polypeptides having a result less than twice higher than background activity of control media, (+) indicates polypeptides having activity two to four times above background, (++) indicates polypeptides having activity greater than four times above background, and (ND) indicates not determined. TABLE 6 Base sequence adjacent to the M vaccae potd gene-homologue was found to show homology to the potb gene of the spermidine/putrescine ABC transporter complex of E.coli, which is one of two transmembrane proteins in the ABC transporter complex. The M. vaccae potb homologue (referred to as GV-25) was identified through further subcloning and base sequencing. The determined nucleotide and predicted amino acid sequences for GV-25 are shown in SEQ ID NOS :97 and 98, respectively. Further subcloning and base sequence analysis of the adjacent 509 bp failed to reveal significant homology to PotC, the second transmembrane protein of E.coli, and suggests that a second transmembrane protein is absent in the M. vaccae homologue of the ABC transporter. An open reading frame with homology to M. tuberculosis acetyl-CoA acetyl transferase, however, was identified starting 530 bp downstream of the transmembrane protein and the translated protein was named GV-26. The determined partial nucleotide sequence and predicted amino acid sequence for GV-26 are shown SEQ ID NO:99 and 100. Using a protocol similar to that described above for the isolation of GV-23, the 3S-PCR band 12B28 (SEQ ID NO: 119) was used to screen the M. vaccae genomic library constructed in the BamHI-site of lambda ZAP Express (Stratagene). The clone isolated from the library contained a novel open reading frame and the antigen encoded by this gene was named GV-38A. The determined nucleotide sequence and predicted amino acid sequence of GV-38A are shown in SEQ ID NO: 120 and 121 , respectively. Comparison of these sequences with those in the gene bank, revealed some homology to an unknown M. tuberculosis protein previously identified in cosmid MTCY428.12. (SPTREMBL:P71915). Upstream of the GV-38A gene, a second novel open reading frame was identified and the antigen encoded by this gene was named GV-38B The determined 5' and 3' nucleotide sequences for GV-38B are provided in SEQ ID NO 122 and 123, respectively, with the corresponding predicted amino acid sequences being provided in SEQ ID NO: 124 and 125, respectively This protein was found to show homology to an unknown M tuberculosis protein identified in cosmid MTCY428 11 (SPTREMBL: P71914). Both the GV-38A and GV-38B antigens were amplified for expression cloning into pET16 (Novagen). GV-38A was amplified with primers KR1 1 and KR12 (SEQ ID NO 126 and 127) and GV-38B with primers KR13 and KR14 (SEQ ID NO- 128 and 129). Protein expression in the host cells BL21(DE3) was induced with 1 M IPTG. however no protein expression was obtained from these constructs Hydrophobic regions were identified in the N-termini of antigens GV-38A and GV- 38B which may inhibit expression of these constructs The hydrophobic region present in GV-38A was identified as a possible transmembrane motif with six membrane spanning regions. To express the antigens without the hydrophobic regions, primers KR20 for GV-38A, (SEQ ID NO: 130) and KR21 for GV-38B (SEQ ID NO. 131 ) were designed. The truncated GV-38A gene was amplified with primers KR20 and KR12, and the truncated GV-38B gene with KR21 and KR14 The determined nucleotide sequences of truncated GV38A and GV-38B are shown in SEQ ID NO. 132 and 133, respectively, with the corresponding predicted amino acid sequenceS"beιng shown in SEQ ID NO: 134 and 135, respectively. EXAMPLE 9 PURIFICATION AND CHARACTERISATION OF POLYPEPTIDES FROM M VACCAE CULTURE FILTRATE BY PREPARATIVE ISOELECTRIC FOCUSING AND PREPARATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS M. vaccae soluble proteins were isolated from culture filtrate using preparative isoelectric focusing and preparative polyacrylamide gel electrophoresis as described below. Unless otherwise noted, all percentages in the following example are weight per volume. M. vaccae (ATCC Number 15483) was cultured in 250 1 sterile Medium 90 which had been fractionated by ultrafiltration to remove all proteins of greater than 10 kDa molecular weight. The medium was centrifuged to remove the bacteria, and sterilised by filtration through a 0.45 m filter. The sterile filtrate was concentrated by ultrafiltration over a 10 kDa molecular weight cut-off membrane. Proteins were isolated from the concentrated culture filtrate by precipitation with 10% trichloroacetic acid. The precipitated proteins were re-dissolved in 100 mM Tris. HCl pH 8.0. and re-precipitated by the addition of an equal volume of acetone. The acetone precipitate was dissolved in water, and proteins were re-precipitated by the addition of an equal volume of chloroform:methanol 2: 1 (v/v). The chloroform:methanol precipitate was dissolved in water, and the solution was freeze - dried. The freeze-dried protein was dissolved in iso-electric focusing buffer, containing 8 M deionised urea, 2% Triton X-100, 10 mM dithiothreitol and 2% ampholytes (pH 2.5 - 5.0). The sample was fractionated by preparative iso-electric focusing on a horizontal bed of Ultrodex gel at 8 watts constant power for 16 hours. Proteins were eluted from the gel bed fractions with water and concentrated by precipitation with 10% trichloroacetic acid. Pools of fractions containing proteins of interest were identified by analytical polyacrylaTnide gel electrophoresis and fractionated by preparative polyacrylamide gel electrophoresis. Samples were fractionated on 12.5% SDS-PAGE gels, and electroblotted onto nitrocellulose membranes. Proteins were located on the membranes by staining with Ponceau Red, destained with water and eluted from the membranes with 40% acetonitrile/O.lM ammonium bicarbonate pH 8.9 and then concentrated by lyophilisation. Eluted proteins were assayed for their ability to induce proliferation and interferon-γ secretion from the peripheral blood lymphocytes of immune donors as detailed in Example 2. Proteins inducing a strong response in these assays were selected for further study. Selected proteins were further purified by reversed-phase chromatography on a Vydac Protein C4 column, using a trifluoroacetic acid-acetonitrile system. Purified proteins were prepared for protein sequence determination by SDS-polyacrylamide gel electrophoresis, and electroblotted onto PVDF membranes. Protein sequences were determined as in Example 3. The proteins were named GV-40, GV-41 , GV-42, GV-43 and GV-44. The determined N-terminal sequences for these polypeptides are shown in SEQ ID NOS: 101 -105. respectively. Subsequent studies led to the isolation of a 5', middle fragment and 3' DNA sequence for GV-42 (SEQ ID NO: 136, 137 and 138, respectively). The corresponding predicted amino acid sequences are provided in SEQ ID NO: 139, 140 and 141, respectively. All of these amino acid sequences were compared to known amino acid sequences in the EMBL data base using TFASTA. No significant homologies were obtained with GV-40, GV42 and GV-44. GV-41 had similarity to a putative ribosome recycling factor from M. tuberculosis, a protein responsible for the release of ribosomes from mRNA at the termination of protein biosynthesis. GV-43 showed homology (by similarity) to a previously identified unknown M. tuberculosis and M. leprae protein. EXAMPLE 10 IMMUNE MODULATING PROPERTIES OF DELIPIDATED AND DEGLYCOSYLATED M. VACCAE AND RECOMBINANT PROTEINS FROM M. VACCAE This example illustrates the processing of different constituents of M.vaccae and their immune modulating properties. Heat-killed M. vaccae and M. vaccae culture filtrate M. vaccae (ATCC Number 15483) was cultured in sterile Medium 90 (yeast extract, 2.5 g/1; tryptone, 5 g/1; glucose 1 g/1) at 37 °C. The cells were harvested by centrifugation, and transferred into sterile Middlebrook 7H9 medium (Difco Laboratories, Detroit, MI, USA) with glucose at 37 °C for one day. The medium was then centrifuged to pellet the bacteria, and the culture filtrate removed. The bacterial pellet was resuspended in phosphate buffered saline at a concentration of 10 mg/ml, equivalent to 10 10 M. vaccae organisms per ml. The cell suspension was then autoclaved for 15 min at 120 °C. The culture filtrate was passaged through a 0.45 μM filter into sterile bottles. Lyophilised, Delipidated and Deglycosylated M.vaccae To prepare delipidated M.vaccae, the autoclaved M. vaccae was pelleted by centrifugation, the pellet washed with water and collected again by centrifugation and then freeze-dried. An aliquot of this freeze-dried M. vaccae was set aside and referred to as lyophilised M.vaccae. When used in experiments it was resuspended in PBS to the desired concentration. Freeze-dried M vaccae was extracted with chloroform/methanol (2:1) for 60 mins at room temperature, and the extraction was repeated once. The residue from chloroform/methanol extraction was further extracted with 50% ethanol by refluxing for two hours. The 50% ethanol extraction was repeated two times. The pooled 50% ethanol extracts were used as a source of M.vaccae glycolipids (see below). The residue from the 50% ethanol extraction was freeze-dried and weighed. The amount of delipidated M.vaccae prepared was equivalent to 11.1% of the starting wet weight of M.vaccae used. For bioassay, the delipidated and deglycosylated M.vaccae DO-M. vaccae; referred to as delipidated M.vaccae~ Figures 8 and 9), was resuspended in phosphate-buffered saline by sonication, and sterilised by autoclaving. M.vaccae glycolipids The pooled 50% ethanol extracts described above were dried by rotary evaporation , redissolved in water, and freeze-dried. The amount of glycolipid recovered was 1.2% of the starting wet weight of M.vaccae used. For bioassay, the glycolipids were dissolved in phosphate-buffered saline. Production of Intcrleukin-12 from macrophages As detailed below, whole heat-killed M.vaccae and M. vaccae constituents were shown to stimulate the production of interleukin-12 (IL-12) from macrophages, an important component of the Thl response. A group of C57BL/6J mice were injected intraperitoneally with DIFCO thioglycolate and after three days, peritoneal macrophages were collected and placed in cell culture with interferon-gamma for three hours. The culture medium was replaced and various concentrations of whole heat-killed M. vaccae, lyophilized M. vaccae, DD- vaccae (referred to as delipidated M. vaccae in Figure 8) and M. vaccae glycolipids were added. After a further three days at 37 °C, the culture supematants were assayed for the presence of IL-12 produced by macrophages. As shown in Figure 8, the M. vaccae preparations stimulated the production of IL-12 from macrophages. Figures 9A, B, and C show data from separate experiments in which groups of C57BL/6 mice (Fig. 9A), BALB/C mice (Fig. 9B) or C3H/HeJ mice (Fig. 9C) were given DIFCO thioglycolate intraperitoneally and, after three days, peritoneal macrophages were collected and placed in culture with interferon-gamma for three hours. The culture medium was replaced and various concentrations of M.vaccae recombinant proteins GVc-3 (GV 3), GVc4P (GV 4P), GVc-7 (GV7), GV-23, GV 27, heat killed M.vaccae, OD-M.vaccae (referred to as delipidated M. vaccae in Figures 9A, B and C), M.vaccae glycolipids or lipopolysaccharide were added. After three days at 37°C, the culture supematants were assayed for the presence of IL-12 produced " By macrophages. As shown in Figures 9A, B and C, the recombinant proteins and M.vaccae preparations stimulated the production of IL-12 from macrophages. EXAMPLE 1 1 EFFECT OF INTRADERMAL ROUTE OF IMMUNISATION WITH M. VACCAE ON TUBERCULOSIS IN CYNOMOLGOUS MONKEYS This example illustrates the effect of immunisation with M.vaccae or M.vaccae culture filtrate intradermally in cynomolgous monkeys prior to challenge with live M. tuberculosis. M.vaccae (ATCC Number 15483) was cultured in sterile Medium 90 (yeast extract, 2.5g/l; tryptone, 5g/l; glucose, lg/I) at 37°C. The cells were harvested by centrifugation, and transferred into sterile Middlebrook 7H9 medium (Difco Laboratories, Detroit, MI, USA) with glucose at 37°C for one day. The medium was then centrifuged to pellet the bacteria, and the culture filtrate removed. The bacterial pellet was resuspended in phosphate buffered saline at a concentration of lOmg/ml, equivalent to 10'° M.vaccae organisms per ml. The cell suspension was then autoclaved for 15 min at 120°C. The culture filtrate was passaged through a 0.45 μM filter into sterile bottles. Three groups of cynomolgous monkeys were included in this study, with each group containing 2 monkeys. One group of monkeys were immunised with whole heat-killed M. vaccae; one group were immunised with M. vaccae culture filtrate and a control group received no immunisations. The composition employed for immunisation, amount of immunogen and route of administration for each group of monkeys are provided in Table 7. TABLE 7 COMPARISON OF INTRADERMAL ROUTE OF IMMUNISATION with culture filtrate) 38I5-B lOOμg intradermal Prior to immunisation, all monkeys were weighed (Wt kgs), body temperature measured (temp), and a blood sample taken for determination of erythrocyte sedimentation rate (ESR mm/hr) and lymphocyte proliferation (LPA) to an in vitro challenge with purified protein (PPD) prepared from Mycobacterium bovis. At day 33 post-immunisation these measurements were repeated. At day 34, all monkeys received a second immunisation using the same amount of M.vaccae. On day 62, body weight, temperature, ESR and LPA to PPD were measured, then all monkeys were infected with 10 3 colony forming units of the Erdman strain of M. tuberculosis. Twenty eight days following infection, body weight, temperature, ESR and LPA to PPD were measured in all monkeys, and the lungs were X-rayed to determine whether infection with live M. tuberculosis had resulted in the onset of pneumonia. As shown in Tables 8A, B and C, the monkeys in the control group showed radiologic evidence of pulmonary tuberculosis by 28 days after infection with M. tuberculosis. Clinical disease was not evident 84 days after infection in monkeys immunised intradermally with two doses of 500 μg of M. vaccae. The onset of clinical disease was delayed in both monkeys immunised intradermally with 100 μg of M vaccae culture filtrate. TABLE 8A CONTROL MONKEYS ND = Not Done TABLE 8B MONKEYS IMMUNISED WITH WHOLE HEAT- KILLED M. VACCAE (500 μg) INTRADERMALLY ND = Not Done TABLE 8C MONKEYS IMMUNISED WITH CULTURE FILTRATE (lOOμg) INTRADERMALLY ND Not Done Although the present invention has been described in some detail by way of illustration and example for purposes of clarity of understanding, changes and modifications can be carried out without departing from the scope of the invention which is intended to be limited only by the scope of the appended claims. SEQUENCE LISTING (1) GENERAL INFORMATION (i) APPLICANT (n) TITLE OF THE INVENTION COMPOUNDS AND METHODS FOR TREATMENT AND DIAGNOSIS OF MYCOBACTERIAL INFECTIONS ( ) NUMBER OF SEQUENCES. 141 (iv) CORRESPONDENCE ADDRESS (A) ADDRESSEE Russell McVeagh West-Walker (B) STREET The Todd Building, Cπr Brandon Street & Lambtoπ Quay (C) CITY Wellington (D) STATE (E) COUNTRY- New Zealand (F) ZIP (v) COMPUTER READABLE FORM (A) MEDIUM TYPE Diskette (B) COMPUTER. IBM Compatible (C) OPERATING SYSTEM: DOS (D) SOFTWARE WordPerfect 52 (vi) CURRENT APPLICATION DATA. (A) APPLICATION NUMBER (B) FILING DATE (C) CLASSIFICATION. (VII) PRIOR APPLICATION DATA (A) APPLICATION NUMBER. (B) FILING DATE. (vni) ATTORNEY/AGENT INFORMATION (A) NAME 1 Bennett, Michael Roy (B) REGISTRATION NUMBER- (C) REFERENCE/DOCKET NUMBER- 22238\MRB (ix) TELECOMMUNICATION INFORMATION. (A) TELEPHONE +64 4 499 9058 (BJ .TELEFAX: +64 4 499 9306 (C) TELEX. ( 2 ) INFORMATION FOR SEQ ID NO : l : ( i ) SEQUENCE CHARACTERISTICS : (A) LENGTH : 25 amino acids (B) TYPE : amino acid (C) STRANDEDNESS : single (D) TOPOLOGY : linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: Ala Pro Val Gly Pro Gly Xaa Ala Ala Tyr Val Gin Gin Val Pro Asp 1 5 ιo 15 Gly Pro Gly Ser Val Gin Gly Met Ala 20 25 (2) INFORMATION FOR SEQ ID NO .2 (l) SEQUENCE CHARACTERISTICS (A) LENGTH- 10 amino acids (B) TYPE, ammo acid (C) STRANDEDNESS single (D) TOPOLOGY linear (u) MOLECULE TYPE: protein (x ) SEQUENCE DESCRIPTION: SEQ ID NO 2 • Met Xaa Asp Gin Leu Lys Val Asn Asp Asp 1 5 10 (2) INFORMATION FOR SEQ ID NO .3 (l) SEQUENCE CHARACTERISTICS (A) LENGTH: 11 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (u) MOLECULE TYPE protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 3 : Met Xaa Pro Val Pro Val Ala Thr Ala Ala Tyr 1 5 10 (2) INFORMATION FOR SEQ ID NO : • (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (iii .MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 4 : Thr Pro Ala Pro Ala Pro Pro Pro Tyr Val Asp His Val Glu Gin Ala 1 5 10 15 Lys Phe Gly Asp Leu 20 (2) INFORMATION FOR SEQ ID NO : 5 - (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single <D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi ) SEQUENCE DESCRIPTION SEQ ID NO : 5 ■ Met Gin Ala Phe Asn Ala Asp Ala Tyr Ala Phe Ala Lys Arg Glu Lys 1 5 10 15 Val Ser Leu Ala Pro Gly Val Pro Xaa Val Phe Glu Thr 20 25 (2) INFORMATION FOR SEQ ID NO : 6 • (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 ammo acids (B) TYPE, amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (li) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 6 : Met Ala Asp Pro Asn Xaa Ala lie Leu Gin Val Ser Lys Thr Thr Arg 1 5 10 IS Gly Gly Gin Ala Ala 20 (2) INFORMATION FOR SEQ ID NO : 7 : (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 11 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( i i ) MOLECULE TYPE : protein (xi ) SEQUENCE DESCRIPTION : SEQ ID NO : 7 : Met Pro He Leu Gin Val Ser Gin Thr Gly Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO : 8 : (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 8 : Met Xaa Asp Pro He Xaa Leu Gin Leu Gin Val Ser Ser Thr 1 5 10 (2) INFORMATION FOR SEQ ID NO : 9 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH 16 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: Single (D) TOPOLOGY, linear (11) MOLECULE TYPE, protein (XI ) SEQUENCE DESCRIPTION SEQ ID NO .9 Lys Ala Thr Tyr Val Gin Gly Gly Leu Gly Arg He Glu Ala Arg Val 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 10. (l) SEQUENCE CHARACTERISTICS (A) LENGTH . 9 amino acids (B) TYPE, amino acid (C) STRANDEDNESS. single (D) TOPOLOGY- linear (n) MOLECULE TYPE, protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO.10 Lys Xaa Gly Leu Ala Asp Leu Ala Pro 1 5 (2) INFORMATION FOR SEQ ID NO: 11- (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (C) STRANDEDNESS: single (D) TOPOLOGY linear (ii) MOLECULE TYPE: protein (ix) FEATURE: JA) NAME/KEY: Other (B) LOCATION: 12...12 (D) OTHER INFORMATION: Residue can be either Glu or He (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 11: Lys Xaa Tyr Ala Leu Ala Leu Met Ser Ala Val Xaa Ala Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO: 12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein ( xi ) SEQUENCE DESCRIPTION - SEQ ID NO - 12 Lys Asn Pro Gin Val Ser Asp Glu Leu Xaa Thr 1 5 10 ( 2 ) INFORMATION FOR SEQ ID NO . 13 . ( l ) SEQUENCE CHARACTERISTICS (A) LENGTH . 21 amino acids (C) STRANDEDNESS. single (D) TOPOLOGY linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION SEQ ID NO: 13. Ala Pro Ala Pro Ala Ala Pro Ala Xaa Gly Asp Pro Ala Ala Val Val 1 5 10 15 Ala Ala Asn Ser Thr 20 (2) INFORMATION FOR SEQ ID NO: 14 (l) SEQUENCE CHARACTERISTICS (A) LENGTH: 15 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION. SEQ ID NO: 14: Glu Ala Glu Val Xaa Tyr Leu Gly Gin Pro Gly Glu Leu Val Asn 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 ammo acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 2...2 (D) OTHER INFORMATION: Residue can be either Gly or Ala (A) NAME/KEY: Other (B) LOCATION. 15...15 (D) OTHER INFORMATION: Residue can be either Pro or Ala (XI ) SEQUENCE DESCRIPTION: SEQ ID NO: 15: A la Xaa Val Val Pro Pro Xaa Gly Pro Pro Ala Pro Gly Ala Xaa 1 5 10 15 (2) INFORMATION FOR SEQ ID NO.16 (I) SEQUENCE CHARACTERISTICS (A) LENGTH 15 ammo acids (C) STRANDEDNESS. single (D) TOPOLOGY- linear (II) MOLECULE TYPE: protein (XI) SEQUENCE DESCRIPTION: SEQ ID NO: 16- Ala Pro Ala Pro Asp Leu Gin Gly Pro Leu Val Ser Thr Leu Ser 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 17 (l) SEQUENCE CHARACTERISTICS- (A) LENGTH: 25 amino acids (B) TYPE: am o ac d (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xl) SEQUENCE DESCRIPTION: SEQ ID NO.17: Ala Thr Pro Asp Trp Ser Gly Arg Tyr Thr Val Val Thr Phe Ala Ser 1 5 10 15 Asp Lys Leu Gly Thr Ser Val Ala Ala 20 25 (2) INFORMATION FOR SEQ ID NO: 18: <i)_S.EQUENCE CHARACTERISTICS. (A) LENGTH: 25 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (u) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 15...15 (D) OTHER INFORMATION: Residue can be either Ala or Arg (A) NAME/KEY: Other (B) LOCATION: 23...23 (D) OTHER INFORMATION: Residue can be either Val or Leu (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 18: Ala Pro Pro Tyr Asp Asp Arg Gly Tyr Val Asp Ser Thr Ala Xaa Xaa 1 5 10 15 Ala Ser Pro Pro Thr Leu Xaa Val Val 20 25 ( 2 ) INFORMATION FOR SEQ ID NO . 19 ( l ) SEQUENCE CHARACTERISTICS (A) LENGTH - 8 amino acids ( B ) TYPE , ammo acid (C) STRANDEDNESS: Single (D) TOPOLOGY linear (n) MOLECULE TYPE, protein (xi) SEQUENCE DESCRIPTION- SEQ ID NO 19 Glu Pro Glu Gly Val Ala Pro Pro 1 5 (2) INFORMATION FOR SEQ ID NO 20 (l) SEQUENCE CHARACTERISTICS (A) LENGTH. 25 am o acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein ( l ) SEQUENCE DESCRIPTION SEQ ID NO.20 Glu Pro Ala Gly He Pro Ala Gly Phe Pro Asp Val Ser Ala Tyr Ala 1 5 10 15 Ala Val Asp Pro Xaa Xaa Tyr Val Val 20 25 (2) INFORMATION FOR SEQ ID NO: 21: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 21. Ala Pro Val Gly Pro Gly Xaa Ala Ala Tyr Val Gin Gin Val Pro 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 22: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (C) STRANDEDNESS Single (D) TOPOLOGY linear (a) MOLECULE TYPE, protein (Xl) SEQUENCE DESCRIPTION SEQ ID NO.22- Phe Ser Arg Pro Gly Leu Pro Val Glu Tyr Leu Asp Val Phe Ser 1 5 10 15 (2) INFORMATION FOR SEQ ID NO 23 (l) SEQUENCE CHARACTERISTICS (A) LENGTH: 19 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE- protein (xi) SEQUENCE DESCRIPTION SEQ ID NO 23 Phe Ser Arg Pro Gly Leu Pro Val Glu Tyr Leu Met Val Pro Ser Pro 1 5 10 15 Ser Met Gly (2) INFORMATION FOR SEQ ID NO: 24- (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 ammo acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: protein (Xl) SEQUENCE DESCRIPTION: SEQ ID NO: 24 Phe Ser Arg Pro Gly Leu Pro Val Glu Tyr Leu Met Val Pro Ser 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 25: (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 14 amino acids (C) STRANDEDNESS: single (D) TOPOLOGY- linear ( i) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 25: Xaa Xaa Thr Gly Leu His Arg Leu Arg Met Met Val Pro Asn 1 5 10 ( 2 ) INFORMATION FOR SEQ ID NO : 26 : ( l ) SEQUENCE CHARACTERISTICS : (A) LENGTH : 20 amino acids ( B ) TYPE : ammo acid ( C ) STRANDEDNESS : singl e (D ) TOPOLOGY : l inear (ii) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 16...16 (D) OTHER INFORMATION: Residue can be either Ser or Val (A) NAME/KEY: Other (B) LOCATION: 17...17 (D) OTHER INFORMATION: Residue can be either Gin or Val (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26: Val Pro Ala Asp Pro Val Gly Ala Ala Ala Gin Ala Glu Pro Ala Xaa 1 5 10 15 Xaa Arg He Asp 20 (2) INFORMATION FOR SEQ ID NO: 27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other .IB) LOCATION: 4...4 (D) OTHER INFORMATION: Residue can be either Tyr or Pro (A) NAME/KEY: Other (B) LOCATION: 8...8 (D) OTHER INFORMATION: Residue can be either Val or Gly (A) NAME/KEY: Other (B) LOCATION: 9...9 (D) OTHER INFORMATION: Residue can be either He or Tyr (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 27: Asp Pro Xaa Xaa Asp He Glu Xaa Xaa Phe Ala Arg Gly Thr 1 5 10 (2) INFORMATION FOR SEQ ID NO: 28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS- single (D) TOPOLOGY, linear (11) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28 Ala Pro Ser Leu Ser Val Ser Asp Tyr Ala Arg Asp Ala Gly Phe 1 5 10 15 (2) INFORMATION FOR SEQ ID NO : 29 ■ (l) SEQUENCE CHARACTERISTICS. (A) LENGTH 16 amino acids (C) STRANDEDNESS: single (D) TOPOLOGY, linear (ii) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 2...2 (D) OTHER INFORMATION: Residue can be either Leu or Pro (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 29 Xaa Xaa Leu Ala Xaa Ala Xaa Leu Gly Xaa Thr Val Asp Ala Asp Gin 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 30: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH. 330 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single CDΛ TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 30: Met Lys Phe Val Asp Arg Phe Arg Gly Ala Val Ala Gly Met Leu Arg 1 5 10 15 Arg Leu Val Val Glu Ala Met Gly Val Ala Leu Leu Ser Ala Leu He 20 25 30 Gly Val Val Gly Ser Ala Pro Ala Glu Ala Phe Ser Arg Pro Gly Leu 35 40 45 Pro Val Glu Tyr Leu Gin Val Pro Ser Pro Ser Met Gly Arg Asp He 50 55 60 Lys Val Gin Phe Gin Asn Gly Gly Ala Asn Ser Pro Ala Leu Tyr Leu 65 70 75 80 Leu Asp Gly Leu Arg Ala Gin Asp Asp Phe Ser Gly Trp Asp He Asn 85 90 95 Thr Thr Ala Phe Glu Trp Tyr Tyr Gin Ser Gly He Ser Val Val Met 100 105 HO Pro Val Gly Gly Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Ser Pro Ala 115 120 125 Cys Gly Lys Ala Gly Cys Gin Thr Tyr Lys Trp Glu Thr Phe Leu Thr 130 135 140 Ser Glu Leu Pro Glu Tyr Leu Gin Ser Asn Lys Gin He Lys Pro Thr 145 150 155 160 Gly Ser Ala Ala Val Gly Leu Ser Met Ala Gly Leu Ser Ala Leu Thr 165 170 175 Leu Ala He Tyr His Pro Asp Gin Phe He Tyr Val Gly Ser Met Ser 180 185 190 Gly Leu Leu Asp Pro Ser Asn Ala Met Gly Pro Ser Leu He Gly Leu 195 200 205 Ala Met Gly Asp Ala Gly Gly Tyr Lys Ala Ala Asp Met Trp Gly Pro 210 215 220 Ser Thr Asp Pro Ala Trp Lys Arg Asn Asp Pro Thr Val Asn Val Gly 225 230 235 240 Thr Leu He Ala Asn Asn Thr Arg He Trp Met Tyr Cys Gly Asn Gly 245 250 255 Lys Pro Thr Glu Leu Gly Gly Asn Asn Leu Pro Ala Lys Leu Leu Glu 260 265 270 Gly Leu Val Arg Thr Ser Asn He Lys Phe Gin Asp Gly Tyr Asn Ala 275 280 285 Gly Gly Gly His Asn Ala Val Phe Asn Phe Pro Asp Ser Gly Thr His 290 295 300 Ser Trp Glu Tyr Trp Gly Glu Gin Leu Asn Asp Met Lys Pro Asp Leu 305 310 315 320 Gin Gin Tyr Leu Gly Ala Thr Pro Gly Ala 325 330 (2) INFORMATION FOR SEQ ID NO: 31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 327 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (iii .MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 31: Met He Asp Val Ser Gly Lys He Arg Ala Trp Gly Arg Trp Leu Leu 1 5 10 15 Val Gly Ala Ala Ala Thr Leu Pro Ser Leu He Ser Leu Ala Gly Gly 20 25 30 Ala Ala Thr Ala Ser Ala Phe Ser Arg Pro Gly Leu Pro Val Glu Tyr 35 40 45 Leu Gin Val Pro Ser Glu Ala Met Gly Arg Thr He Lys Val Gin Phe 50 55 60 Gin Asn Gly Gly Asn Gly Ser Pro Ala Val Tyr Leu Leu Asp Gly Leu 65 70 75 80 Arg Ala Gin Asp Asp Tyr Asn Gly Trp Asp He Asn Thr Ser Ala Phe 85 90 95 Glu Trp Tyr Tyr Gin Ser Gly Leu Ser Val Val Met Pro Val Gly Gly 100 105 110 Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Ser Pro Ala Cys Gly Lys Ala 115 120 125 Gly Cys Thr Thr Tyr Lys Trp Glu Thr Phe Leu Thr Ser Glu Leu Pro 130 135 140 Lys Trp Leu Ser Ala Asn Arg Ser Val Lys Ser Thr Gly Ser Ala Val 145 150 155 160 Val Gly Leu Ser Met Ala Gly Ser Ser Ala Leu He Leu Ala Ala Tyr 165 170 175 His Pro Asp Gin Phe He Tyr Ala Gly Ser Leu Ser Ala Leu Met Asp 180 185 190 Ser Ser Gin Gly He Glu Pro Gin Leu He Gly Leu Ala Met Gly Asp 195 200 205 Ala Gly Gly Tyr Lys Ala Ala Asp Met Trp Gly Pro Pro Asn Asp Pro 210 215 220 Ala Trp Gin Arg Asn Asp Pro He Leu Gin Ala Gly Lys Leu Val Ala 225 230 235 240 Asn Asn Thr His Leu Trp Val Tyr Cys Gly Asn Gly Thr Pro Ser Glu 245 250 255 Leu Gly Gly Thr Asn Val Pro Ala Glu Phe Leu Glu Asn Phe Val His 260 265 270 Gly Ser Asn Leu Lys Phe Gin Asp Ala Tyr Asn Gly Ala Gly Gly His 275 280 285 Asn Ala Val Phe Asn Leu Asn Ala Asp Gly Thr His Ser Trp Glu Tyr 290 295 300 Trp Gly Ala Gin Leu Asn Ala Met Lys Pro Asp Leu Gin Asn Thr Leu 305 310 315 320 Met Ala Val Pro Arg Ser Gly 325 (2) INFORMATION FOR SEQ ID NO: 32: (i) SEQUENCE CHARACTE ISTICS: (A) LENGTH: 338 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xU..SEQUENCE DESCRIPTION: SEQ ID NO: 32: Met Gin Leu Val Asp Arg Val Arg Gly Ala Val Thr Gly Met Ser Arg 1 5 10 15 Arg Leu Val Val Gly Ala Val Gly Ala Ala Leu Val Ser Gly Leu Val 20 25 30 Gly Ala Val Gly Gly Thr Ala Thr Ala Gly Ala Phe Ser Arg Pro Gly 35 40 45 Leu Pro Val Glu Tyr Leu Gin Val Pro Ser Pro Ser Met Gly Arg Asp 50 55 60 He Lys Val Gin Phe Gin Ser Gly Gly Ala Asn Ser Pro Ala Leu Tyr 65 70 75 80 Leu Leu Asp Gly Leu Arg Ala Gin Asp Asp Phe Ser Gly Trp Asp He 85 90 95 Asn Thr Pro Ala Phe Glu Trp Tyr Asp Gin Ser Gly Leu Ser Val Val 100 105 110 Met Pro Val Gly Gly Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Gin Pro 115 120 125 Ala Cys Gly Lys Ala Gly Cys Gin Thr Tyr Lys Trp Glu Thr Phe Leu 130 135 140 Thr Ser Glu Leu Pro Gly Trp Leu Gin Ala Asn Arg His Val Lys Pro 145 150 155 160 Thr Gly Ser Ala Val Val Gly Leu Ser Met Ala Ala Ser Ser Ala Leu 165 170 175 Thr Leu Ala He Tyr H s Pro Gin Gin Phe Val Tyr Ala Gly Ala Met 180 185 190 Ser Gly Leu Leu Asp Pro Ser Gin Ala Met Gly Pro Thr Leu He Gly 195 200 205 Leu Ala Met Gly Asp Ala Gly Gly Tyr Lys Ala Ser Asp Met Trp Gly 210 215 220 Pro Lys Glu Asp Pro Ala Trp Gin Arg Asn Asp Pro Leu Leu Asn Val 225 230 235 240 Gly Lys Leu He Ala Asn Asn Thr Arg Val Trp Val Tyr Cys Gly Asn 245 250 255 Gly Lys Pro Ser Asp Leu Gly Gly Asn Asn Leu Pro Ala Lys Phe Leu 260 265 270 Glu Gly Phe Val Arg Thr Ser Asn He Lys Phe Gin Asp Ala Tyr Asn 275 280 285 Ala Gly Gly Gly His Asn Gly Val Phe Asp Phe Pro Asp Ser Gly Thr 290 295 300 His Ser Trp Glu Tyr Trp Gly Ala Gin Leu Asn Ala Met Lys Pro Asp 305 310 315 320 Leu Gin Arg Ala Leu Gly Ala Thr Pro Asn Thr Gly Pro Ala Pro Gin 325 330 335 Gly Ala (2) INFORMATION FOR SEQ ID NO: 33: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 325 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: protein (xii.SEQUENCE DESCRIPTION: SEQ ID NO: 33: Met Thr Asp Val Ser Arg Lys He Arg Ala Trp Gly Arg Arg Leu Met 1 5 10 15 He Gly Thr Ala Ala Ala Val Val Leu Pro Gly Leu Val Gly Leu Ala 20 25 30 Gly Gly Ala Ala Thr Ala Gly Ala Phe Ser Arg Pro Gly Leu Pro Val 35 40 45 Glu Tyr Leu Gin Val Pro Ser Pro Ser Met Gly Arg Asp He Lys Val 50 55 60 Gin Phe Gin Ser Gly Gly Asn Asn Ser Pro Ala Val Tyr Leu Leu Asp 65 70 75 80 Gly Leu Arg Ala Gin Asp Asp Tyr Asn Gly Trp Asp He Asn Thr Pro 85 90 95 Ala Phe Glu Trp Tyr Tyr Gin Ser Gly Leu Ser He Val Met Pro Val 100 105 110 Gly Gly Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Ser Pro Ala Cys Gly 115 120 125 Lys Ala Gly Cys Gin Thr Tyr Lys Trp Glu Thr Phe Leu Thr Ser Glu 130 135 140 Leu Pro Gin Trp Leu Ser Ala Asn Arg Ala Val Lys Pro Thr Gly Ser 145 150 155 160 Ala Ala He Gly Leu Ser Met Ala Gly Ser Ser Ala Met He Leu Ala 165 170 175 Ala Tyr His Pro Gin Gin Phe He Tyr Ala Gly Ser Leu Ser Ala Leu 180 185 190 Leu Asp Pro Ser Gin Gly Met Gly Pro Ser Leu He Gly Leu Ala Met 195 200 205 Gly Asp Ala Gly Gly Tyr Lys Ala Ala Asp Met Trp Gly Pro Ser Ser 210 215 220 Asp Pro Ala Trp Glu Arg Asn Asp Pro Thr Gin Gin He Pro Lys Leu 225 230 235 240 Val Ala Asn Asn Thr Arg Leu Trp Val Tyr Cys Gly Asn Gly Thr Pro 245 250 255 Asn Glu Leu Gly Gly Ala Asn He Pro Ala Glu Phe Leu Glu Asn Phe 260 265 270 Val Arg Ser Ser Asn Leu Lys Phe Gin Asp Ala Tyr Asn Ala Ala Gly 275 280 285 Gly His Asn Ala Val Phe Asn Phe Pro Pro Asn Gly Thr His Ser Trp 290 295 300 Glu Tyr Trp Gly Ala Gin Leu Asn Ala Met Lys Gly Asp Leu Gin Ser 305 310 315 320 Ser Leu Gly Ala Gly 325 (2) INFORMATION FOR SEQ ID NO: 34. (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 338 amino acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 34: Met Gin Leu Val Asp Arg Val Arg Gly Ala Val Thr Gly Met Ser Arg 1 5 10 15 Arg Leu Val Val Gly Ala Val Gly Ala Ala Leu Val Ser Gly Leu Val 20 25 30 Gly Ala Val Gly Gly Thr Ala Thr Ala Gly Ala Phe Ser Arg Pro Gly 35 40 45 Leu Pro Val Glu Tyr Leu Gin Val Pro Ser Pro Ser Met Gly Arg Asp 50 55 60 He Lys Val Gin Phe Gin Ser Gly Gly Ala Asn Ser Pro Ala Leu Tyr 65 70 75 80 Leu Leu Asp Gly Leu Arg Ala Gin Asp Asp Phe Ser Gly Trp Asp He 85 90 95 Asn Thr Pro Ala Phe Glu Trp Tyr Asp Gin Ser Gly Leu Ser Val Val 100 105 110 Met Pro Val Gly Gly Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Gin Pro 115 120 125 Ala Cys Gly Lys Ala Gly Cys Gin Thr Tyr Lys Trp Glu Thr Phe Leu 130 135 140 Thr Ser Glu Leu Pro Gly Trp Leu Gin Ala Asn Arg His Val Lys Pro (2) INFORMATION FOR SEQ ID NO: 35: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 323 amino acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 35: Met Thr Asp Val Ser Arg Lys He Arg Ala Trp Gly Arg Arg Leu Met 1 5 10 15 He Gly Thr Ala Ala Ala Val Val Leu Pro Gly Leu Val Gly Leu Ala 20 25 30 Gly Gly Ala Ala Thr Ala Gly Ala Phe Ser Arg Pro Gly Leu Pro Val 35 40 45 Glu Tyr Leu Gin Val Pro Ser Pro Ser Met Gly Arg Asp He Lys Val 50 55 60 Gin Phe Gin Ser Gly Gly Asn Asn Ser Pro Ala Val Tyr Leu Leu Asp 65 70 75 80 Gly Leu Arg Ala Gin Asp Asp Tyr Asn Gly Trp Asp He Asn Thr Pro 85 90 95 Ala Phe Glu Trp Tyr Tyr Gin Ser Gly Leu Ser He Val Met Pro Val 100 105 no Gly Gly Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Ser Pro Ala Cys Gly 115 120 125 Lys Ala Gly Cys Gin Thr Tyr Lys Trp Glu Thr Leu Leu Thr Ser Glu 130 135 140 Leu Pro Gin Trp Leu Ser Ala Asn Arg Ala Val Lys Pro Thr Gly Ser 145 150 155 160 Ala Ala He Gly Leu Ser Met Ala Gly Ser Ser Ala Met He Leu Ala 165 170 175 Ala Tyr His Pro Gin Gin Phe He Tyr Ala Gly Ser Leu Ser Ala Leu 180 185 190 Leu Asp Pro Ser Gin Gly Met Gly Leu He Gly Leu Ala Met Gly Asp 195 200 205 Ala Gly Gly Tyr Lys Ala Ala Asp Met Trp Gly Pro Ser Ser Asp Pro 210 215 220 Ala Trp Glu Arg Asn Asp Pro Thr Gin Gin He Pro Lys Leu Val Ala 225 230 235 240 Asn Asn Thr Arg Leu Trp Val Tyr Cys Gly Asn Gly Thr Pro Asn Glu 245 250 255 Leu Gly Gly Ala Asn He Pro Ala Glu Phe Leu Glu Asn Phe Val Arg 260 265 270 Ser Ser Asn Leu Lys Phe Gin Asp Ala Tyr Lys Pro Ala Gly Gly His 275 280 285 Asn Ala Val Phe Asn Phe Pro Pro Asn Gly Thr His Ser Trp Glu Tyr 290 295 300 Trp Gly Ala Gin Leu Asn Ala Met Lys Gly Asp Leu Gin Ser Ser Leu 305 310 315 320 Gly Ala Gly (2) INFORMATION FOR SEQ ID NO.36: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 333 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 36: Met Lys Phe Leu Gin Gin Met Arg Lys Leu Phe Gly Leu Ala Ala Lys 1 5 10 15 Phe Pro Ala Arg Leu Thr He Ala Val He Gly Thr Ala Leu Leu Ala 20 25 30 Gly Leu Val Gly Val Val Gly Asp Thr Ala He Ala Val Ala Phe Ser 35 40 45 Lys Pro Gly Leu Pro Val Glu Tyr Leu Gin Val Pro Ser Pro Ser Met 50 55 60 Gly His Asp He Lys He Gin Phe Gin Gly Gly Gly Gin His Ala Val 65 70 75 80 Tyr Leu Leu Asp Gly Leu Arg Ala Gin Glu Asp Tyr Asn Gly Trp Asp 85 90 95 He Asn Thr Pro Ala Phe Glu Glu Tyr Tyr His Ser Gly Leu Ser Val 100 105 110 He Met Pro Val Gly Gly Gin Ser Ser Phe Tyr Ser Asn Trp Tyr Gin 115 120 125 Pro Ser Gin Gly Asn Gly Gin His Tyr Thr Tyr Lys Trp Glu Thr Phe 130 135 140 Leu Thr Gin Glu Met Pro Ser Trp Leu Gin Ala Asn Lys Asn Val Leu 145 150 155 160 Pro Thr Gly Asn Ala Ala Val Gly Leu Ser Met Ser Gly Ser Ser Ala 165 170 175 Leu He Leu Ala Ser Tyr Tyr Pro Gin Gin Phe Pro Tyr Ala Ala Ser 180 185 190 Leu Ser Gly Phe Leu Asn Pro Ser Glu Gly Trp Trp Pro Thr Met He 195 200 205 Gly Leu Ala Met Asn Asp Ser Gly Gly Tyr Asn Ala Asn Ser Met Trp 210 215 220 Gly Pro Ser Thr Asp Pro Ala Trp Lys Arg Asn Asp Pro Met Val Gin 225 230 235 240 He Pro Arg Leu Val Ala Asn Asn Thr Arg He Trp Val Tyr Cys Gly 245 250 255 Asn Gly Ala Pro Asn Glu Leu Gly Gly Asp Asn He Pro Ala Lys Phe 260 265 270 Leu Glu Ser Leu Thr Leu Ser Thr Asn Glu He Phe Gin Asn Thr Tyr 275 280 285 Ala Ala Ser Gly Gly Arg Asn Gly Val Phe Asn Phe Pro Pro Asn Gly 290 295 300 Thr His Ser Trp Pro Tyr Trp Asn Gin Gin Leu Val Ala Met Lys Pro 305 310 315 320 Asp He Gin Gin He Leu Asn Gly Ser Asn Asn Asn Ala 325 330 (2) INFORMATION FOR SEQ ID NO: 37: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH. 340 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (i ) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION. SEQ ID NO : 37 : Met Thr Phe Phe Glu Gin Val Arg Arg Leu Arg Ser Ala Ala Thr Thr 1 5 10 15 Leu Pro Arg Arg Val Ala He Ala Ala Met Gly Ala Val Leu Val Tyr 20 25 30 Gly Leu Val Gly Thr Phe Gly Gly Pro Ala Thr Ala Gly Ala Phe Ser 35 40 45 Arg Pro Gly Leu Pro Val Glu Tyr Leu Gin Val Pro Ser Ala Ser Met 50 55 60 Gly Arg Asp He Lys Val Gin Phe Gin Gly Gly Gly Pro His Ala Val 65 70 75 80 Tyr Leu Leu Asp Gly Leu Arg Ala Gin Asp Asp Tyr Asn Gly Trp Asp 85 90 95 He Asn Thr Pro Ala Phe Glu Glu Tyr Tyr Gin Ser Gly Leu Ser Val 100 105 110 He Met Pro Val Gly Gly Gin Ser Ser Phe Tyr Thr Asp Trp Tyr Gin 115 120 125 Pro Ser Gin Ser Asn Gly Gin Asn Tyr Thr Tyr Lys Trp Glu Thr Phe 130 135 140 Leu Thr Arg Glu Met Pro Ala Trp Leu Gin Ala Asn Lys Gly Val Ser 145 150 155 160 Pro Thr Gly Asn Ala Ala Val Gly Leu Ser Met Ser Gly Gly Ser Ala 165 170 175 Leu He Leu Ala Ala Tyr Tyr Pro Gin Gin Phe Pro Tyr Ala Ala Ser 180 185 190 Leu Ser Gly Phe Leu Asn Pro Ser Glu Gly Trp Trp Pro Thr Leu He 195 200 205 Gly Leu Ala Met Asn Asp Ser Gly Gly Tyr Asn Ala Asn Ser Met Trp 210 215 220 Gly Pro Ser Ser Asp Pro Ala Trp Lys Arg Asn Asp Pro Met Val Gin 225 230 235 240 He Pro Arg Leu Val Ala Asn Asn Thr Arg He Trp Val Tyr Cys Gly 245 250 255 Asn Gly Thr Pro Ser Asp Leu Gly Gly Asp Asn He Pro Ala Lys Phe 260 265 270 Leu Glu Gly Leu Thr Leu Arg Thr Asn Gin Thr Phe Arg Asp Thr Tyr 275 280 285 Ala Ala Asp Gly Gly Arg Asn Gly Val Phe Asn Phe Pro Pro Asn Gly 290 295 300 Thr His Ser Trp Pro Tyr Trp Asn Glu Gin Leu Val Ala Met Lys Ala 305 310 315 320 Asp He Gin His Val Leu Asn Gly Ala Thr Pro Pro Ala Ala Pro Ala 325 330 335 Ala Pro Ala Ala 340 (2) INFORMATION FOR SEQ ID NO: 38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 38: AGCGGCTGGG ACATCAACAC 0 (2) INFORMATION FOR SEQ ID NO: 39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 39: CAGACGCGGG TGTTGTTGGC 20 (2) INFORMATION FOR SEQ ID NO: 40: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1211 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS- single (D) TOPOLOGY: linear (11) MOLECULE TYPE: Genomic DNA (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 40- GGTACCGGAA GCTGGAGGAT TGACGGTATG AGACTTCTTG ACAGGATTCG TGGGCCTTGG 60 GCACGCCGTT TCGGCGTCGT GGCTGTCGCG ACAGCGATGA TGCCTGCTTT GGTGGGCCTG 120 GCTGGAGGGT CGGCGACCGC CGGAGCATTC TCCCGGCCAG GTCTGCCGGT GGAGTACCTG 180 ATGGTGCCTT CGCCGTCGAT GGGGCGCGAC ATCAAGATCC AGTTCCAGAG CGGTGGCGAG 240 AACTCGCCGG CTCTCTACCT GCTCGACGGC CTGCGTGCGC AGGAGGACTT CAACGGCTGG 300 GACATCAACA CTCAGGCTTT CGAGTGGTTC CTCGACAGCG GCATCTCCGT GGTGATGCCG 360 GTCGGTGGCC AGTCCAGCTT CTACACCGAC TGGTACGCCC CCGCCCGTAA CAAGGGCCCG 420 ACCGTGACCT ACAAGTGGGA GACCTTCCTG ACCCAGGAGC TCCCGGGCTG GCTGCAGGCC 480 AACCGCGCGG TCAAGCCGAC CGGCAGCGGC CCTGTCGGTC TGTCGATGGC GGGTTCGGCC 540 GCGCTGAACC TGGCGACCTG GCACCCGGAG CAGTTCATCT ACGCGGGCTC GATGTCCGGC 600 TTCCTGAACC CCTCCGAGGG CTGGTGGCCG TTCCTGATCA ACATCTCGAT GGGTGACGCC 660 GGCGGCTTCA AGGCCGACGA CATGTGGGGC AAGACCGAGG GGATCCCAAC AGCGGTTGGA 720 CAGCGCAACG ATCCGATGCT GAACATCCCG ACCCTGGTCG CCAACAACAC CCGTATCTGG 780 GTCTACTGCG GTAACGGCCA GCCCACCGAG CTCGGCGGCG GCGACCTGCC CGCCACGTTC 840 CTCGAAGGTC TGACCATCCG CACCAACGAG ACCTTCCGCG ACAACTACAT CGCCGCGGGT 900 GGCCACAACG GTGTGTTCAA CTTCCCGGCC AACGGCACGC ACAACTGGGC GTACTGGGGT 960 —. CGCGAGCTGC AGGCGATGAA GCCTGACCTG CAGGCGCACC TTCTCTGACG GTTGCACGAA 1020 ACGAAGCCCC CGGCCGATTG CGGCCGAGGG TTTCGTCGTC CGGGGCTACT GTGGCCGACA 1080 TAACCGAAAT CAACGCGATG GTGGCTCATC AGGAACGCCG AGGGGGTCAT TGCGCTACGA 1140 CACGAGGTGG GCGAGCAATC CTTCCTGCCC GACGGAGAGG TCAACATCCA CGTCGAGTAC 1200 TCCAGCGTGA A 1211 (2) INFORMATION FOR SEQ ID NO: 41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 485 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 41. AGCGGCTGGG ACATCAACAC CGCCGCCTTC GAGTGGTACG TCGACTCGGG TCTCGCGGTG 60 ATCATGCCCG TCGGCGGGCA GTCCAGCTTC TACAGCGACT GGTACAGCCC GGCCTGCGGT 120 AAGGCCGGCT GCCAGACCTA CAAGTGGGAG ACGTTCCTGA CCCAGGAGCT GCCGGCCTAC 180 CTCGCCGCCA ACAAGGGGGT CGACCCGAAC CGCAACGCGG CCGTCGGTCT GTCCATGGCC 240 GGTTCGGCGG CGCTGACGCT GGCGATCTAC CACCCGCAGC AGTTCCAGTA CGCCGGGTCG 300 CTGTCGGGCT ACCTGAACCC GTCCGAGGGG TGGTGGCCGA TGCTGATCAA CATCTCGATG 360 GGTGACGCGG GCGGCTACAA GGCCAACGAC ATGTGGGGTC CACCGAAGGA CCCGAGCAGC 420 GCCTGGAAGC GCAACGACCC GATGGTCAAC ATCGGCAAGC TGGTGGCCAA CAACACCCCC 480 CTCTC 485 (2) INFORMATION FOR SEQ ID NO:42: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1052 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (i ) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: GTTGATGAGA AAGGTGGGTT GTTTGCCGTT ATGAAGTTCA CAGAGAAGTG GCGGGGCTCC 60 αCAAAGGCGC-CGATGCACCG GGTGGGCGTT GCCGATATGG CCGCCGTTGC GCTGCCCGGA 120 CTGATCGGCT TCGCCGGGGG TTCGGCAACG GCCGGGGCAT TCTCCCGGCC CGGTCTTCCT 180 GTCGAGTACC TCGACGTGTT CTCGCCGTCG ATGGGCCGCG ACATCCGGGT CCAGTTCCAG 240 GGTGGCGGTA CTCATGCGGT CTACCTGCTC GACGGTCTGC GTGCCCAGGA CGACTACAAC 300 GGCTGGGACA TCAACACCCC TGCGTTCGAG TGGTTCTACG AGTCCGGCTT GTCGACGATC 360 ATGCCGGTCG GCGGACAGTC CAGCTTCTAC AGCGACTGGT ACCAGCCGTC TCGGGGCAAC 420 GGGCAGAACT ACACCTACAA GTGGGAGACG TTCCTGACCC AGGAGCTGCC GACGTGGCTG 480 GAGGCCAACC GCGGAGTGTC GCGCACCGGC AACGCGTTCG TCGGCCTGTC GATGGCGGGC 540 AGCGCGGCGC TGACCTACGC GATCCATCAC CCGCAGCAGT TCATCTACGC CTCGTCGCTG 600 TCAGGCTTCC TGAACCCGTC CGAGGGCTGG TGGCCGATGC TGATCGGGCT GGCGATGAAC 660 GACGCAGGCG GCTTCAACGC CGAGAGCATG TGGGGCCCGT CCTCGGACCC GGCGTGGAAG 720 CGCAACGACC CGATGGTCAA CATCAACCAG CTGGTGGCCA ACAACACCCG GATCTGGATC 780 TACTGCGGCA CCGGCACCCC GTCGGAGCTG GACACCGGGA CCCCGGGCCA GAACCTGATG 840 GCCGCGCAGT TCCTCGAAGG ATTCACGTTG CGGACCAACA TCGCCTTCCG TGACAACTAC 900 ATCGCAGCCG GCGGCACCAA CGGTGTCTTC AACTTCCCGG CCTCGGGCAC CCACAGCTGG 960 GGGTACTGGG GGCAGCAGCT GCAGCAGATG AAGCCCGACA TCCAGCGGGT TCTGGGAGCT 1020 CAGGCCACCG CCTAGCCACC CACCCCACAC CC 1052 (2) INFORMATION FOR SEQ ID NO: 43: ( ) SEQUENCE CHARACTERISTICS: (A) LENGTH: 326 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43: Met Arg Leu Leu Asp Arg He Arg Gly Pro Trp Ala Arg Arg Phe Gly 1 5 10 15 Val Val Ala Val Ala Thr Ala Met Met Pro Ala Leu Val Gly Leu Ala 20 25 30 Gly Gly Ser Ala Thr Ala Gly Ala Phe Ser Arg Pro Gly Leu Pro Val 35 40 45 Glu Tyr Leu Met Val Pro Ser Pro Ser Met Gly Arg Asp He Lys He 50 55 60 Gin Phe Gin Ser Gly Gly Glu Asn Ser Pro Ala Leu Tyr Leu Leu Asp 65 70 75 80 Gly Leu Arg Ala Gin Glu Asp Phe Asn Gly Trp Asp He Asn Thr Gin 85 90 95 Ala Phe Glu Trp Phe Leu Asp Ser Gly He Ser Val Val Met Pro Val 100 105 110 Gly Gly Gin Ser Ser Phe Tyr Thr Asp Trp Tyr Ala Pro Ala Arg Asn 115 120 125 Lys Gly Pro Thr Val Thr Tyr Lys Trp Glu Thr Phe Leu Thr Gin Glu 130 135 140 Leu Pro Gly Trp Leu Gin Ala Asn Arg Ala Val Lys Pro Thr Gly Ser 145 150 155 160 Gly Pro Val Gly Leu Ser Met Ala Gly Ser Ala Ala Leu Asn Leu Ala 165 170 175 Thr Trp His Pro Glu Gin Phe He Tyr Ala Gly Ser Met Ser Gly Phe 180 185 190 Leu Asn Pro Ser Glu Gly Trp Trp Pro Phe Leu He Asn He Ser Met 195 200 205 Gly Asp Ala Gly Gly Phe Lys Ala Asp Asp Met Trp Gly Lys Thr Glu 210 215 220 Gly He Pro Thr Ala Val Gly Gin Arg Asn Asp Pro Met Leu Asn He 225 230 235 240 Pro Thr Leu Val Ala Asn Asn Thr Arg He Trp Val Tyr Cys Gly Asn 245 250 255 Gly Gin Pro Thr Glu Leu Gly Gly Gly Asp Leu Pro Ala Thr Phe Leu 260 265 270 Glu Gly Leu Thr He Arg Thr Asn Glu Thr Phe Arg Asp Asn Tyr He 275 280 285 Ala Ala Gly Gly His Asn Gly Val Phe Asn Phe Pro Ala Asn Gly Thr 290 295 300 His Asn Trp Ala Tyr Trp Gly Arg Glu Leu Gin Ala Met Lys Pro Asp 305 310 315 320 Leu Gin Ala His Leu Leu 325 (2) INFORMATION FOR SEQ ID NO: 44. (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 161 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION. SEQ ID NO:44: Ser Gly Trp Asp He Asn Thr Ala Ala Phe Glu Trp Tyr Val Asp Ser 1 5 10 15 Gly Leu Ala Val He Met Pro Val Gly Gly Gin Ser Ser Phe Tyr Ser 20 25 30 Asp Trp Tyr Ser Pro Ala Cys Gly Lys Ala Gly Cys Gin Thr Tyr Lys 35 40 45 Trp Glu Thr Phe Leu Thr Gin Glu Leu Pro Ala Tyr Leu Ala Ala Asn 50 55 60 Lys Gly Val Asp Pro Asn Arg Asn Ala Ala Val Gly Leu Ser Met Ala 65 70 75 80 Gly Ser Ala Ala Leu Thr Leu Ala He Tyr His Pro Gin Gin Phe Gin 85 90 95 Tyr Ala Gly Ser Leu Ser Gly Tyr Leu Asn Pro Ser Glu Gly Trp Trp 100 105 no Pro Met Leu He Asn He Ser Met Gly Asp Ala Gly Gly Tyr Lys Ala 115 120 125 Asn Asp Met Trp Gly Pro Pro Lys Asp Pro Ser Ser Ala Trp Lys Arg 130 135 140 Asn Asp Pro Met Val Asn He Gly Lys Leu Val Ala Asn Asn Thr Pro 145 150 155 160 Leu (2) INFORMATION FOR SEQ ID NO: 5: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 334 amino acids (B) TYPE : ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE- protein (xi ) SEQUENCE DESCRIPTION. SEQ ID NO 45 Met Lys Phe Thr Glu Lys Trp Arg Gly Ser Ala Lys Ala Ala Met His 1 5 10 15 Arg Val Gly Val Ala Asp Met Ala Ala Val Ala Leu Pro Gly Leu He 20 25 30 Gly Phe Ala Gly Gly Ser Ala Thr Ala Gly Ala Phe Ser Arg Pro Gly 35 40 45 Leu Pro Val Glu Tyr Leu Asp Val Phe Ser Pro Ser Met Gly Arg Asp 50 55 60 He Arg Val Gin Phe Gin Gly Gly Gly Thr His Ala Val Tyr Leu Leu 65 70 75 80 Asp Gly Leu Arg Ala Gin Asp Asp Tyr Asn Gly Trp Asp He Asn Thr 85 90 95 Pro Ala Phe Glu Trp Phe Tyr Glu Ser Gly Leu Ser Thr He Met Pro 100 105 110 Val Gly Gly Gin Ser Ser Phe Tyr Ser Asp Trp Tyr Gin Pro Ser Arg 115 120 125 Gly Asn Gly Gin Asn Tyr Thr Tyr Lys Trp Glu Thr Phe Leu Thr Gin 130 135 140 Glu Leu Pro Thr Trp Leu Glu Ala Asn Arg Gly Val Ser Arg Thr Gly 145 150 155 160 Asn Ala Phe Val Gly Leu Ser Met Ala Gly Ser Ala Ala Leu Thr Tyr 165 170 175 Ala He His His Pro Gin Gin Phe He Tyr Ala Ser Ser Leu Ser Gly 180 185 190 Phe Leu Asn Pro Ser Glu Gly Trp Trp Pro Met Leu He Gly Leu Ala 195 200 205 Met Asn Asp Ala Gly Gly Phe Asn Ala Glu Ser Met Trp Gly Pro Ser 210 215 220 Ser Asp Pro Ala Trp Lys Arg Asn Asp Pro Met Val Asn He Asn Gin 225 230 235 240 Leu Val Ala Asn Asn Thr Arg He Trp He Tyr Cys Gly Thr Gly Thr 245 250 255 Pro Ser Glu Leu Asp Thr Gly Thr Pro Gly Gin Asn Leu Met Ala Ala 260 265 270 Gin Phe Leu Glu Gly Phe Thr Leu Arg Thr Asn He Ala Phe Arg Asp 275 280 285 Asn Tyr He Ala Ala Gly Gly Thr Asn Gly Val Phe Asn Phe Pro Ala 290 295 300 Ser Gly Thr His Ser Trp Gly Tyr Trp Gly Gin Gin Leu Gin Gin Met 305 310 315 320 Lys Pro Asp He Gin Arg Val Leu Gly Ala Gin Ala Thr Ala 325 330 (2) INFORMATION FOR SEQ ID NO: 46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 795 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (li) MOLECULE TYPE: Genomic DNA ( i) SEQUENCE DESCRIPTION: SEQ ID NO: 6: CTGCCGCGGG TTTGCCATCT CTTGGGTCCT GGGTCGGGAG GCCATGTTCT GGGTAACGAT 60 CCGGTACCGT CCGGCGATGT GACCAACATG CGAACAGCGA CAACGAAGCT AGGAGCGGCG 120 CTCGGCGCAG CAGCATTGGT GGCCGCCACG GGGATGGTCA GCGCGGCGAC GGCGAACGCC 180 CAGGAAGGGC ACCAGGTCCG TTACACGCTC ACCTCGGCCG GCGCTTACGA GTTCGACCTG 240 TTCTATCTGA CGACGCAGCC GCCGAGCATG CAGGCGTTCA ACGCCGACGC GTATGCGTTC 300 GCCAAGCGGG AGAAGGTCAG CCTCGCCCCG GGTGTGCCGT GGGTCTTCGA AACCACGATG 360 GCCGACCCGA ACTGGGCGAT CCTTCAGGTC AGCAGCACCA CCCGCGGTGG GCAGGCCGCC 420 CCGAACGCGC ACTGCGACAT CGCCGTCGAT GGCCAGGAGG TGCTCAGCCA GCACGACGAC 480 CCCTACAACG TGCGGTGCCA GCTCGGTCAG TGGTGAGTCA CCTCGCCGAG AGTCCGGCCA 540 GCGCCGGCGG CAGCGGCTCG CGGTGCAGCA CCCCGAGGCG CTGGGTCGCG CGGGTCAGCG 600 CGACGTAAAG ATCGCTGGCC CCGCGCGGCC CCTCGGCGAG GATCTGCTCC GGGTAGACCA 660 CCAGCACGGC GTCTAACTCC AGACCCTTGG TCTGCGTGGG TGCCACCGCG CCCGGGACAC 720 CGGGCGGGCC GATCACCACG CTGGTGCCCT CCCGGTCCGC CTCCGCACGC ACGAAATCGT 780 CGATGGCACC GGCGA 795 (2) INFORMATION FOR SEQ ID NO: 47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 142 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single D)L TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 47: Met Arg Thr Ala Thr Thr Lys Leu Gly Ala Ala Leu Gly Ala Ala Ala 1 5 10 15 Leu Val Ala Ala Thr Gly Met Val Ser Ala Ala Thr Ala Asn Ala Gin 20 25 30 Glu Gly His Gin Val Arg Tyr Thr Leu Thr Ser Ala Gly Ala Tyr Glu 35 40 45 Phe Asp Leu Phe Tyr Leu Thr Thr Gin Pro Pro Ser Met Gin Ala Phe 50 55 60 Asn Ala Asp Ala Tyr Ala Phe Ala Lys Arg Glu Lys Val Ser Leu Ala 65 70 75 80 Pro Gly Val Pro Trp Val Phe Glu Thr Thr Met Ala Asp Pro Asn Trp 85 90 95 Ala He Leu Gin Val Ser Ser Thr Thr Arg Gly Gly Gin Ala Ala Pro 100 105 HO Asn Ala His Cys Asp He Ala Val Asp Gly Gin Glu Val Leu Ser Gin 115 120 125 His Asp Asp Pro Tyr Asn Val Arg Cys Gin Leu Gly Gin Trp 130 135 140 (2) INFORMATION FOR SEQ ID NO 48 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 300 base pairs (B) TYPE nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY linear (ii) MOLECULE TYPE. Genomic DNA (xi) SEQUENCE DESCRIPTION SEQ ID NO 48: GCCAGTGCGC CAACGGTTTT CATCGATGCC GCACACAACC CCGGTGGGCC CTGCGCTTGC 60 CGAAGGCTGC GCGACGAGTT CGACTTCCGG TATCTCGTCG GCGTCGTCTC GGTGATGGGG 120 GACAAGGACG TGGACGGGAT CCGCCAGGAC CCGGGCGTGC CGGACGGGCG CGGTCTCGCA 180 CTGTTCGTCT CGGGCGACAA CCTTCGAAAG GGTGCGGCGC TCAACACGAT CCAGATCGCC 240 GAGCTGCTGG CCGCCCAGTT GTAAGTGTTC CGCCGAAATT GCATTCCACG CCGATAATCG 300 (2) INFORMATION FOR SEQ ID NO -49. (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 563 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (II) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 49: GGATCCTCGG CCGGCTCAAG AGTCCGCGCC GAGGTGGATG TGACGCTGGA CGGCTACGAG 60 TTCAGTCGGG CCTGCGAGGC GCTGTACCAC TTCGCCTGGG ACGAGTTCTG CGACTGGTAT 120 GTCGAGCTTG CCAAAGTGCA ACTGGGTGAA GGTTTCTCGC ACACCACGGC CGTGTTGGCC 180 ACCGTGCTCG ATGTGCTGCT CAAGCTTCTG CACCCGGTCA TGCCGTTCGT CACCGAGGTG 240 CTGTGGAAGG CCCTGACCGG GCGGGCCGGC GCGAGCGAAC GTCTGGGAAA TGTGGAGTCA 300 CTGGTCGTCG CGGACTGGCC CACGCCCACC GGATACGCGC TGGATCAGGC TGCCGCACAA 360 CGGATCGCCG ACACCCAGAA GTTGATCACC GAGGTGCGCC GGTTCCGCAG CGATCAGGGT 420 CTGGCCGACC GCCAGCGGGT GCCTGCCCGG TTGTCCGGCA TCGACACCGC GGGTCTGGAC 480 GCCCATGTCC CGGCGGTGCG CGCGCTGGCC TGGCTTGACC GAGGGTGATG AGGGCTTCAC 540 CGCGTCCGAA TCGGTCGAGG TGC 563 (2) INFORMATION FOR SEQ ID NO: 50- (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 434 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( i) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 50: GGGCCGGGCC CGAGGATGAG CAAGTTCGAA GTCGTCACCG GGATGGCGTT CGCGGCTTTC 60 GCCGACGCGC CCATCGACGT CGCCGTCGTC GAGGTCGGGC TCGGTGGTCG CTGGGACGCG 120 ACGAACGTGG TGAACGCACC GGTCGCGGTC ATCACCCCGA TCGGGGTGGA CCACACCGAC 180 TACCTCGGTG ACACGATCGC CGAGATCGCC GGGGAGAAGG CCGGAAATCA TCACCCGCCA 240 GCCGACGACC TGGTGCCGAC CGACACCGTC GCCGTGCTGG CGCGGCAGGT TCCCGAGGCC 300 ATGGAGGTGC TGCTGGCCCA GGCGGTGCGC TCGGATGCGG CTGTAGCGCG CGAGGATTCG 360 GAGTGCGCGG TGCTGGGCCG TCAGGTCGCC ATCGGCGGCA GCTGCTCCGG TTGCAGGGGC 420 TCGGTOGCGT CTAC 434 (2) INFORMATION FOR SEQ ID NO: 51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 438 base pairs (JB). TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA ( i) SEQUENCE DESCRIPTION: SEQ ID NO: 51: GGATCCCACT CCCGCGCCGG CGGCGGCCAG CTGGTACGGC CATTCCAGCG TGCTGATCGA 60 GGTCGACGGC TACCGCGTGC TGGCCGACCC GGTGTGGAGC AACAGATGTT CGCCCTCACG 120 GGCGGTCGGA CCGCAGCGCA TGCACGACGT CCCGGTGCCG CTGGAGGCGC TTCCCGCCGT 180 GGACGCGGTG GTGATCGCCA ACGACCACTA CGACCACCTC GACATCGACA CCATCGTCGC 240 GTTGGCGCAC ACCCAGCGGG CCCCGTTCGT GGTGCCGTTG GGCATCGGCG CACACCTGCG 300 CA A GTGGGGC GTCCCCGAGG CGCGGATCGT CGAGTTGGAC TGGCACGAAG CCCACCGCAT 360 CGACGACCTG ACGCTGGTCT GCACCCCCGC CCGGCACTTC TCCGGCCGGT TGTTCTCCCG 420 CGACTCGACG CTGTGGGC 438 (2) INFORMATION FOR SEQ ID NO: 52 (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 87 amino acids (C) STRANDEDNESS: Single (D) TOPOLOGY, linear (n) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION SEQ ID NO: 52- Ala Ser Ala Pro Thr Val Phe He Asp Ala Ala His Asn Pro Gly Gly 1 5 10 15 Pro Cys Ala Cys Arg Arg Leu Arg Asp Glu Phe Asp Phe Arg Tyr Leu 20 25 30 Val Gly Val Val Ser Val Met Gly Asp Lys Asp Val Asp Gly He Arg 35 40 45 Gin Asp Pro Gly Val Pro Asp Gly Arg Gly Leu Ala Leu Phe Val Ser 50 55 60 Gly Asp Asn Leu Arg Lys Gly Ala Ala Leu Asn Thr He Gin He Ala 65 70 75 80 Glu Leu Leu Ala Ala Gin Leu 85 (2) INFORMATION FOR SEQ ID NO: 53: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 175 ammo acids (B) TYPE, ammo acid (C) STRANDEDNESS: single (β). TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 53: Gly Ser Ser Ala Gly Ser Arg Val Arg Ala Glu Val Asp Val Thr Leu 1 5 10 15 Asp Gly Tyr Glu Phe Ser Arg Ala Cys Glu Ala Leu Tyr His Phe Ala 20 25 30 Trp Asp Glu Phe Cys Asp Trp Tyr Val Glu Leu Ala Lys Val Gin Leu 35 40 45 Gly Glu Gly Phe Ser His Thr Thr Ala Val Leu Ala Thr Val Leu Asp 50 55 60 Val Leu Leu Lys Leu Leu His Pro Val Met Pro Phe Val Thr Glu Val 65 70 75 80 Leu Trp Lys Ala Leu Thr Gly Arg Ala Gly Ala Ser Glu Arg Leu Gly 85 90 95 Asn Val Glu Ser Leu Val Val Ala Asp Trp Pro Thr Pro Thr Gly Tyr 100 105 HO Ala Leu Asp Gin Ala Ala Ala Gin Arg He Ala Asp Thr Gin Lys Leu 115 120 125 He Thr Glu Val Arg Arg Phe Arg Ser Asp Gin Gly Leu Ala Asp Arg 130 135 140 Gin Arg Val Pro Ala Arg Leu Ser Gly He Asp Thr Ala Gly Leu Asp 145 150 155 160 Ala His Val Pro Ala Val Arg Ala Leu Ala Trp Leu Asp Arg Gly 165 170 175 (2) INFORMATION FOR SEQ ID NO : 54 (l) SEQUENCE CHARACTERISTICS- (A) LENGTH- 144 ammo acids (B) TYPE, ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY, linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION SEQ ID NO 54 Gly Pro Gly Pro Arg Asn Ser Lys Phe Glu Val Val Thr Gly Met Ala 1 5 10 15 Phe Ala Ala Phe Ala Asp Ala Pro He Asp Val Ala Val Val Glu Val 20 25 30 Gly Leu Gly Gly Arg Trp Asp Ala Thr Asn Val Val Asn Ala Pro Val 35 40 45 Ala Val He Thr Pro He Gly Val Asp His Thr Asp Tyr Leu Gly Asp 50 55 60 Thr He Ala Glu He Ala Gly Glu Lys Ala Gly Asn His His Pro Pro 65 70 75 80 Ala Asp Asp Leu Val Pro Thr Asp Thr Val Ala Val Leu Ala Arg Gin 85 90 95 Val Pro Glu Ala Asn Glu Val Leu Leu Ala Gin Ala Val Arg Ser Asp 100 105 110 Ala Ala Val Ala Arg Glu Asp Ser Glu Cys Ala Val Leu Gly Arg Gin 115 120 125 Val Ala Lie Gly Gly Ser Cys Ser Gly Cys Arg Gly Ser Val Ala Ser 130 135 140 (2) INFORMATION FOR SEQ ID NO .-55: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 145 ammo acids (B) TYPE: ammo acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:55. Asp Pro Thr Pro Ala Pro Ala Ala Ala Ser Trp Tyr Gly His Ser Ser 1 5 10 15 Val Leu He Glu Val Asp Gly Tyr Arg Val Leu Ala Asp Pro Val Trp 20 25 30 Ser A sn A rg Cys Ser Pro Ser Arg Ala Val Gly Pro Gin Arg Met His 35 40 45 Asp Val Pro Val Pro Leu Glu Ala Leu Pro Ala Val Asp Ala Val Val 50 55 60 He Ser Asn Asp His Tyr Asp His Leu Asp He Asp Thr He Val Ala 65 70 75 80 Leu Ala His Thr Gin Arg Ala Pro Phe Val Val Pro Leu Gly He Gly 85 90 95 Ala His Leu Arg Lys Trp Gly Val Pro Glu Ala Arg He Val Glu Leu 100 105 110 Asp Trp His Glu Ala His Arg He Asp Asp Leu Thr Leu Val Cys Thr 115 120 125 Pro Ala Arg His Phe Ser Gly Arg Leu Phe Ser Arg Asp Ser Thr Leu 130 135 140 Trp 145 (2) INFORMATION FOR SEQ ID NO: 56: (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 10 am o acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii ) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 1...1 (D) OTHER INFORMATION: Residue can be either Gly, He, Leu or Val (A) NAME/KEY: Other (B) LOCATION: 2...2 (D) OTHER INFORMATION: Residue can be either He, Leu, Gly or Ala (xi-V -SEQUENCE DESCRIPTION: SEQ ID NO: 56 Xaa Xaa Ala Pro Xaa Gly Asp Ala Xaa Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO: 57: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: ammo acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 7...7 (D) OTHER INFORMATION: Residue can be either He or Leu (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 57: Pro Glu Ala Glu Ala Asn Xaa Arg 1 5 (2) INFORMATION FOR SEQ ID NO: 58: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (ix) FEATURE: (A) NAME/KEY: Other (B) LOCATION: 4...4 (D) OTHER INFORMATION: Residue can be either Gin or Gly (A) NAME/KEY: Other (B) LOCATION: 5...5 (D) OTHER INFORMATION: Residue en be either Gly or Gin (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 58: Thr Ala Asn Xaa Xaa Glu Tyr Tyr Asp Asn Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO: 59: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ijj. -MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 59: Asn Ser Pro Arg Ala Glu Ala Glu Ala Asn Leu Arg Gly Tyr Phe Thr 1 5 10 15 Ala Asn Pro Ala Glu Tyr Tyr Asp Leu Arg Gly He Leu Ala Pro He 20 25 30 Gly Asp (2) INFORMATION FOR SEQ ID NO: 60: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other ( X i) SEQUENCE DESCRIPTION: SEQ ID NO: 60: CCGGTGGGCC CGGGCTGCGC 0 (2) INFORMATION FOR SEQ ID NO: 61: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other ( i) SEQUENCE DESCRIPTION: SEQ ID NO: 61: TGGCCGGCCA CCACGTGGTA 0 (2) INFORMATION FOR SEQ ID NO: 62: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 313 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 62: GCCGGTGGGC CCGGGCTGCG CGGAATACGC GGCAGCCAAT CCCACTGGGC CGGCCTCGGT 60 GCAGGGAATG TCGCAGGACC CGGTCGCGGT GGCGGCCTCG AACAATCCGG AGTTGACAAC 120 GCTGTACGGC -TGCACTGTCG GGCCAGCTCA ATCCGCAAGT AAACCTGGTG GACACCCTCA 180 ACAGCGGTCA GTACACGGTG TTCGCACCGA CCAACGCGGC ATTTAGCAAG CTGCCGGCAT 240 CCACGATCGA CGAGCTCAAG ACCAATTCGT CACTGCTGAC CAGCATCCTG ACCTACCACG 300 TGGTGGCCGG CCA 313 (2) INFORMATION FOR SEQ ID NO:63: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 63: Glu Pro Ala Gly Pro Leu Pro Xaa Tyr Asn Glu Arg Leu His Thr Leu 1 5 10 15 Xaa Gin (2) INFORMATION FOR SEQ ID NO: 64: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 64: Gly Leu Asp Asn Glu Leu Ser Leu Val Asp Gly Gin Gly Arg Thr Leu 1 5 10 15 Thr Val Gin Gin Xaa Asp Thr Phe Leu 20 25 (2) INFORMATION FOR SEQ ID NO: 65: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 65: Asp Pro Xaa Pro Asp He Glu Val Glu Phe Ala Arg Gly Thr Gly Ala 1 5 10 15 Glu Pro G-ϊy Leu Xaa Xaa Val Xaa Asp Ala 20 25 (2) INFORMATION FOR SEQ ID NO: 66: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 66: ACCGCCCTCG AGTTCTCCCG GCCAGGTCTG CC 32 (2) INFORMATION FOR SEQ ID NO: 67: ( l ) SEQUENCE CHARACTERISTICS : (A) LENGTH 32 base pairs (B) TYPE : nucleic acid ( C ) STRANDEDNESS . s ingle ( D ) TOPOLOGY , l inear (a) MOLECULE TYPE: Other ( i) SEQUENCE DESCRIPTION. SEQ ID NO:67 AAGCACGAGC TCAGTCTCTT CCACGCGGAC GT 2 (2) INFORMATION FOR SEQ ID NO -68. (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 30 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS- single (D) TOPOLOGY: linear (n) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION- SEQ ID NO:68: CATGGATCCA TTCTCCCGGC CCGGTCTTCC 0 (2) INFORMATION FOR SEQ ID NO: 69- (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 69: TTTGAATTCT AGGCGGTGGC CTGAGC 6 (2) INFORMATION FOR SEQ ID NO: 70: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 161 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 70: Ser Gly Trp Asp He Asn Thr Ala Ala Phe Glu Trp Tyr Val Asp Ser 1 5 10 15 Gly Leu Ala Val He Met Pro Val Gly Gly Gin Ser Ser Phe Tyr Ser 20 25 30 Asp Trp Tyr Ser Pro Ala Cys Gly Lys Ala Gly Cys Gin Thr Tyr Lys 35 40 45 Trp Glu Thr Phe Leu Thr Gin Glu Leu Pro Ala Tyr Leu Ala Ala Asn 50 55 60 Lys Gly Val Asp Pro Asn Arg Asn Ala Ala Val Gly Leu Ser Met Ala 65 70 75 80 Gly Ser Ala Ala Leu Thr Leu Ala He Tyr His Pro Gin Gin Phe Gin 85 90 95 Tyr Ala Gly Ser Leu Ser Gly Tyr Leu Asn Pro Ser Glu Gly Trp Trp 100 105 110 Pro Met Leu He Asn He Ser Met Gly Asp Ala Gly Gly Tyr Lys Ala 115 120 125 Asn Asp Met Trp Gly Arg Thr Glu Asp Pro Ser Ser Ala Trp Lys Arg 130 135 140 Asn Asp Pro Met Val Asn He Gly Lys Leu Val Ala Asn Asn Thr Pro 145 150 155 160 Leu (2) INFORMATION FOR SEQ ID NO.71: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (a) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 71: GAGAGACTCG AGAACGCCCA GGAAGGGCAC CAG 3 ) INFORMATION FOR SEQ ID NO: 72: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 72: GAGAGACTCG AGTGACTCAC CACTGACCGA GC 32 (2) INFORMATION FOR SEQ ID NO: 73: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS. single (D) TOPOLOGY, linear (n) MOLECULE TYPE- Other (xi ) SEQUENCE DESCRIPTION- SEQ ID NO: 73. GGNGCNGCNC ARGCNGARCC 0 (2) INFORMATION FOR SEQ ID NO.74 (l) SEQUENCE CHARACTERISTICS: (A) LENGTH 825 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS. single (D) TOPOLOGY linear (a) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION. SEQ ID NO: 74 TTGGATCCCA CTCCCGCGCC GGCGGCGGCC AGCTGGTACG GCCATTCCAG CGTGCTGATC 60 GAGGTCGACG GCTACCGCGT GCTGGCCGAC CCGGTGTGGA GCAACAGATG TTCGCCCTCA 120 CGGGCGGTCG GACCGCAGCG CATGCACGAC GTCCCGGTGC CGCTGGAGGC GCTTCCCGCC 180 GTGGACGCGG TGGTGATCAG CCACGACCAC TACGACCACC TCGACATCGA CACCATCGTC 240 GCGTTGGCGC ACACCCAGCG GGCCCCGTTC GTGGTGCCGT TGGGCATCGG CGCACACCTG 300 CGCAAGTGGG GCGTCCCCGA GGCGCGGATC GTCGAGTTGG ACTGGCACGA AGCCCACCGC 360 ATAGACGACC TGACGCTGGT CTGCACCCCC GCCCGGCACT TCTCCGGACG GTTGTTCTCC 420 CGCGACTCGA CGCTGTGGGC GTCGTGGGTG GTCACCGGCT CGTCGCACAA GGCGTTCTTC 480 GGTGGCGAGA-CCGGATACAC GAAGAGCTTC GCCGAGATCG GCGACGAGTA CGGTCCGTTC 540 GATCTGACCC TGCTGCCGAT CGGGGCCTAC CATCCCGCGT TCGCCGACAT CCACATGAAC 600 CCCGAGGAGG CGGTGCGCGC CCATCTGGAC CTGACCGAGG TGGACAACAG CCTGATGGTG 660 CCCATCCACT GGGCGACATT CCGCCTCGCC CCGCATCCGT GGTCCGAGCC CGCCGAACGC 720 CTGCTGACCG CTGCCGACGC CGAGCGGGTA CGCCTGACCG TGCCGATTCC CGGTCAGCGG 780 GTGGACCCGG AGTCGACGTT CGACCCGTGG TGGCGGTTCT GAACC 825 (2) INFORMATION FOR SEQ ID NO: 75: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 273 ammo acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE: protein (Xl ) SEQUENCE DESCRIPTION: SEQ ID NO: 75: Leu Asp Pro Thr Pro Ala Pro Ala Ala Ala Ser Trp Tyr Gly His Ser 1 5 10 15 Ser Val Leu He Glu Val Asp Gly Tyr Arg Val Leu Ala Asp Pro Val 20 25 30 Trp Ser Asn Arg Cys Ser Pro Ser Arg Ala Val Gly Pro Gin Arg Met 35 40 45 His Asp Val Pro Val Pro Leu Glu Ala Leu Pro Ala Val Asp Ala Val 50 55 60 Val He Ser His Asp His Tyr Asp His Leu Asp He Asp Thr He Val 65 70 75 80 Ala Leu Ala His Thr Gin Arg Ala Pro Phe Val Val Pro Leu Gly He 85 90 95 Gly Ala His Leu Arg Lys Trp Gly Val Pro Glu Ala Arg He Val Glu 100 105 110 Leu Asp Trp His Glu Ala His Arg He Asp Asp Leu Thr Leu Val Cys 115 120 125 Thr Pro Ala Arg His Phe Ser Gly Arg Leu Phe Ser Arg Asp Ser Thr 130 135 140 Leu Trp Ala Ser Trp Val Val Thr Gly Ser Ser His Lys Ala Phe Phe 145 150 155 160 Gly Gly Asp Thr Gly Tyr Thr Lys Ser Phe Ala Glu He Gly Asp Glu 165 170 175 Tyr Gly Pro Phe Asp Leu Thr Leu Leu Pro He Gly Ala Tyr His Pro 180 185 190 Ala Phe Ala Asp He His Met Asn Pro Glu Glu Ala Val Arg Ala His 195 200 205 Leu Asp Leu Thr Glu Val Asp Asn Ser Leu Met Val Pro He His Trp 210 215 220 Ala Thr Phe Arg Leu Ala Pro His Pro Trp Ser Glu Pro Ala Glu Arg 225 230 235 240 Leu Leu Thr Ala Ala Asp Ala Glu Arg Val Arg Leu Thr Val Pro He 245 250 255 Pro Gly Gin Arg Val Asp Pro Glu Ser Thr Phe Asp Pro Trp Trp Arg 260 265 270 Phe (2) INFORMATION FOR SEQ ID NO: 76: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 76: Ala Lys Thr He Ala Tyr Asp Glu Glu Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO: 77: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 337 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (a) MOLECULE TYPE: Genomic DNA (Xl) SEQUENCE DESCRIPTION: SEQ ID NO: 77: GATCCCTACA TCCTGCTGGT CAGCTCCAAG GTGTCGACCG TCAAGGATCT GCTCCCGCTG 60 CTGGAGAAGG TCATCCAGGC CGGCAAGCCG CTGCTGATCA TCGCCGAGGA CGTCGAGGGC 120 GAGGCCCTGT CCACGCTGGT GGTCAACAAG ATCCGCGGCA CCTTCAAGTC CGTCGCCGTC 180 AAGGCTCCGG GCTTCGGTGA CCGCCGCAAG GCGATGCTGC AGGACATGGC CATCCTCACC 240 GGTGGTCAGG TCGTCAGCGA AAGAGTCGGG CTGTCCCTGG AGACCGCCGA CGTCTCGCTG 300 CTGGGCCAGG CCCGCAAGGT CGTCGTCACC AAGGACA 337 (2) INFORMATION FOR SEQ ID NO: 78: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 112 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:78: Asp Pro T-ys He Leu Leu Val Ser Ser Lys Val Ser Thr Val Lys Asp 1 5 10 15 Leu Leu Pro Leu Leu Glu Lys Val He Gin Ala Gly Lys Pro Leu Leu 20 25 30 He He Ala Glu Asp Val Glu Gly Glu Ala Leu Ser Thr Leu Val Val 35 40 45 Asn Lys He Arg Gly Thr Phe Lys Ser Val Ala Val Lys Ala Pro Gly 50 55 60 Phe Gly Asp Arg Arg Lys Ala Met Leu Gin Asp Met Ala He Leu Thr 65 70 75 80 Gly Gly Gin Val Val Ser Glu Arg Val Gly Leu Ser Leu Glu Thr Ala 85 90 95 Asp Val Ser Leu Leu Gly Gin Ala Arg Lys Val Val Val Thr Lys Asp 100 105 110 (2) INFORMATION FOR SEQ ID NO: 79: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 360 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (a) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 79: CCGTACGAGA AGATCGGCGC TGAGCTGGTC AAAGAGGTCG CCAAGAAGAC CGACGACGTC 60 GCGGGCGACG GCACCACCAC CGCCACCGTG CTCGCTCAGG CTCTGGTTCG CGAAGGCCTG 120 CGCAACGTCG CAGCCGGCGC CAACCCGCTC GGCCTCAAGC GTGGCATCGA GAAGGCTGTC 180 GAGGCTGTCA CCCAGTCGCT GCTGAAGTCG GCCAAGGAGG TCGAGACCAA GGAGCAGATT 240 TCTGCCACCG CGGCGATCTC CGCCGGCGAC ACCCAGATCG GCGAGCTCAT CGCCGAGGCC 300 ATGGACAAGG TCGGCAACGA GGGTGTCATC ACCGTCGAGG AGTCGAACAC CTTCGGCCTG 360 (2) INFORMATION FOR SEQ ID NO: 80: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 120 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 80: Pro Tyr Glu Lys He Gly Ala Glu Leu Val Lys Glu Val Ala Lys Lys 1 5 10 15 Thr Asp Asp Val Ala Gly Asp Gly Thr Thr Thr Ala Thr Val Leu Ala 20 25 30 Gin Ala Leu Val Arg Glu Gly Leu Arg Asn Val Ala Ala Gly Ala Asn 3-5" 40 45 Pro Leu Gly Leu Lys Arg Gly He Glu Lys Ala Val Glu Ala Val Thr 50 55 60 Gin Ser Leu Leu Lys Ser Ala Lys Glu Val Glu Thr Lys Glu Gin He 65 70 75 80 Ser Ala Thr Ala Ala He Ser Ala Gly Asp Thr Gin He Gly Glu Leu 85 90 95 He Ala Glu Ala Met Asp Lys Val Gly Asn Glu Gly Val He Thr Val 100 105 110 Glu Glu Ser Asn Thr Phe Gly Leu 115 120 (2) INFORMATION FOR SEQ ID NO: 81: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 43 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE: Other (xi ) SEQUENCE DESCRIPTION- SEQ ID NO: 81: ACTGACGCTG AGGAGCGAAA GCGTGGGGAG CGAACAGGAT TAG 3 (2) INFORMATION FOR SEQ ID NO: 82: (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 43 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other ( i) SEQUENCE DESCRIPTION: SEQ ID NO: 82: CGACAAGGAA CTTCGCTACC TTAGGACCGT CATAGTTACG GGC 3 (2) INFORMATION FOR SEQ ID NO: 83: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO.-83: AAAAAAAAAA AAAAAAAAAA 0 __2) INFORMATION FOR SEQ ID NO: 84: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 84: GGAAGGAAGC GGCCGCTTTT TTTTTTTTTT T 1 (2) INFORMATION FOR SEQ ID NO: 85: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS. single (D) TOPOLOGY: linear (a) MOLECULE TYPE. Other (xi) SEQUENCE DESCRIPTION. SEQ ID NO 85 GAGAGAGAGC CCGGGCATGC TSCTSCTSCT S 1 (2) INFORMATION FOR SEQ ID NO -86 (l) SEQUENCE CHARACTERISTICS (A) LENGTH- 238 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear In) MOLECULE TYPE. Genomic DNA (Xl ) SEQUENCE DESCRIPTION: SEQ ID NO -86 CTCGATGAAC CGCTCGGAGC GCTCGACCTG AAGCTGCGCC ACGTCATGCA GTTCGAGCTC 60 AAGCGCATCC AGCGGGAGGT CGGGATCACG TTCATCTACG TGACCCACGA CCAGGAAGAG 120 GCGCTCACGA TGAGTGACCG CATCGCGGTG ATGAACGCCG GCAACGTCGA ACAGATCGGC 180 AGCCCGACCG AGATCTACGA CCGTCCCGCG ACGGTGTTCG TCGCCAGCTT CATCGAAT 238 (2) INFORMATION FOR SEQ ID NO: 87. (l) SEQUENCE CHARACTERISTICS (A) LENGTH: 79 ammo acids (C) STRANDEDNESS: single ( ■ © TOPOLOGY: linear (a) MOLECULE TYPE: protein (Xl) SEQUENCE DESCRIPTION: SEQ ID NO: 87: Leu Asp Glu Pro Leu Gly Ala Leu Asp Leu Lys Leu Arg His Val Met 1 5 10 15 Gin Phe Glu Leu Lys Arg He Gin Arg Glu Val Gly He Thr Phe He 20 25 30 Tyr Val Thr His Asp Gin Glu Glu Ala Leu Thr Met Ser Asp Arg He 35 40 45 Ala Val Met Asn Ala Gly Asn Val Glu Gin He Gly Ser Pro Thr Glu 50 55 60 He Tyr Asp Arg Pro Ala Thr Val Phe Val Ala Ser Phe He Glu 65 70 75 (2) INFORMATION FOR SEQ ID NO: 88: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1518 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA ( i) SEQUENCE DESCRIPTION: SEQ ID NO: 88: CACTCGCCAT GGGTGTTACA ATACCCCACC AGTTCCTCGA AGTAAACGAA CAGAACCGTG 60 ACATCCAGCT GAGAAAATAT TCACAGCGAC GAAGCCCGGC CGATGCCTGA TGGGGTCCGG 120 CATCAGTACA GCGCGCTTTC CTGCGCGGAT TCTATTGTCG AGTCCGGGGT GTGACGAAGG 180 AATCCATTGT CGAAATGTAA ATTCGTTGCG GAATCACTTG CATAGGTCCG TCAGATCCGC 240 GAAGGTTTAC CCCACAGCCA CGACGGCTGT CCCCGAGGAG GACCTGCCCT GACCGGCACA 300 CACATCACCG CTGCAGAACC TGCAGAACAG ACGGCGGATT CCGCGGCACC GCCCAAGGGC 360 GCGCCGGTGA TCGAGATCGA CCATGTCACG AAGCGCTTCG GCGACTACCT GGCCGTCGCG 420 GACGCAGACT TCTCCATCGC GCCCGGGGAG TTCTTCTCCA TGCTCGGCCC GTCCGGGTGT 480 GGGAAGACGA CCACGTTGCG CATGATCGCG GGATTCGAGA CCCCGACTGA AGGGGCGATC 540 CGCCTCGAAG GCGCCGACGT GTCGAGGACC CCACCCAACA AGCGCAACGT CAACACGGTG 600 TTCCAGCACT ACGCGCTGTT CCCGCACATG ACGGTCTGGG ACAACGTCGC GTACGGCCCG 660 CGCAGCAAGA AACTCGGCAA AGGCGAGGTC CGCAAGCGCG TCGACGAGCT GCTGGAGATC 720 GTCCGGCTGA CCGAATTTGC CGAGCGCAGG CCCGCCCAGC TGTCCGGCGG GCAGCAGCAG 780 CGGGTGGCGT TGGCCCGGGC ACTGGTGAAC TACCCCAGCG CGCTGCTGCT CGATGAACCG 840 CTCGGAGCG€ -TCGACCTGAA GCTGCGCCAC GTCATGCAGT TCGAGCTCAA GCGCATCCAG 900 CGGGAGGTCG GGATCACGTT CATCTACGTG ACCCACGACC AGGAAGAGGC GCTCACGATG 960 AGTGACCGCA TCGCGGTGAT GAACGCCGGC AACGTCGAAC AGATCGGCAG CCCGACCGAG 1020 ATCTACGACC GTCCCGCGAC GGTGTTCGTC GCCAGCTTCA TCGGACAGGC CAACCTCTGG 1080 GCGGGCCGGT GCACCGGCCG CTCCAACCGC GATTACGTCG AGATCGACGT TCTCGGCTCG 1140 ACGCTGAAGG CACGCCCGGG CGAGACCACG ATCGAGCCCG GCGGGCACGC CACCCTGATG 1200 GTGCGTCCGG AACGCATCCG GGTCACCCCG GGCTCCCAGG ACGCGCCGAC CGGTGACGTC 1260 GCCTGCGTGC GTGCCACCGT CACCGACCTG ACCTTCCAAG GTCCGGTGGT GCGGCTCTCG 1320 CTGGCCGCTC CGGACGACTC GACCGTGATC GCCCACGTCG GCCCCGAGCA GGATCTGCCG 1380 CTGCTGCGCC CCGGCGACGA CGTGTACGTC AGCTGGGCAC CGGAAGCCTC CCTGGTGCTT 1440 CCCGGCGACG ACATCCCCAC CACCGAGGAC CTCGAAGAGA TGCTCGACGA CTCCTGAGTC 1500 ACGCTTCCCG ATTGCCGA 1518 (2) INFORMATION FOR SEQ ID NO: 89. (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 376 ammo acids (B) TYPE: ammo acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (a) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 89: Val He Glu He Asp His Val Thr Lys Arg Phe Gly Asp Tyr Leu Ala 1 5 10 15 Val Ala Asp Ala Asp Phe Ser He Ala Pro Gly Glu Phe Phe Ser Met 20 25 30 Leu Gly Pro Ser Gly Cys Gly Lys Thr Thr Thr Leu Arg Met He Ala 35 40 45 Gly Phe Glu Thr Pro Thr Glu Gly Ala He Arg Leu Glu Gly Ala Asp 50 55 60 Val Ser Arg Thr Pro Pro Asn Lys Arg Asn Val Asn Thr Val Phe Gin 65 70 75 80 His Tyr Ala Leu Phe Pro His Met Thr Val Trp Asp Asn Val Ala Tyr 85 90 95 Gly Pro Arg Ser Lys Lys Leu Gly Lys Gly Glu Val Arg Lys Arg Val 100 105 110 Asp Glu Leu Leu Glu He Val Arg Leu Thr Glu Phe Ala Glu Arg Arg 115 120 125 Pro Ala Gin Leu Ser Gly Gly Gin Gin Gin Arg Val Ala Leu Ala Arg 130 135 140 Ala Leu Val Asn Tyr Pro Ser Ala Leu Leu Leu Asp Glu Pro Leu Gly 145 150 155 160 Ala Leu Asp Leu Lys Leu Arg His Val Met Gin Phe Glu Leu Lys Arg 165 170 175 He Gin Arg Glu Val Gly He Thr Phe He Tyr Val Thr His Asp Gin 180 185 190 Glu Glu Ala Leu Thr Met Ser Asp Arg He Ala Val Met Asn Ala Gly 195 200 205 Asn Val Glu Gin He Gly Ser Pro Thr Glu He Tyr Asp Arg Pro Ala 210 215 220 Thr Val Phe Val Ala Ser Phe He Gly Gin Ala Asn Leu Trp Ala Gly 225 230 235 240 Arg Cys Thr Gly Arg Ser Asn Arg Asp Tyr Val Glu He Asp Val Leu 245 250 255 Gly Ser Thr Leu Lys Ala Arg Pro Gly Glu Thr Thr He Glu Pro Gly 260 265 270 Gly His Ala Thr Leu Met Val Arg Pro Glu Arg He Arg Val Thr Pro 275 280 285 Gly Ser Gin Asp Ala Pro Thr Gly Asp Val Ala Cys Val Arg Ala Thr 290 295 300 Val Thr Asp Leu Thr Phe Gin Gly Pro Val Val Arg Leu Ser Leu Ala 30 5 310 315 320 Ala Pro Asp Asp Ser Thr Val He Ala His Val Gly Pro Glu Gin Asp 325 330 335 Leu Pro Leu Leu Arg Pro Gly Asp Asp Val Tyr Val Ser Trp Ala Pro 340 345 350 Glu Ala Ser Leu Val Leu Pro Gly Asp Asp He Pro Thr Thr Glu Asp 355 360 365 Leu Glu Glu Met Leu Asp Asp Ser 370 375 (2) INFORMATION FOR SEQ ID NO: 90: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 90: GAGAGACTCG AGGTGATCGA GATCGACCAT GTC 3 (2) INFORMATION FOR SEQ ID NO: 91: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 91: AGAGACTCGA -GCAATCGGGA AGCGTGACTC A 31 (2) INFORMATION FOR SEQ ID NO: 92: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 323 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (Xi) SEQUENCE DESCRIPTION: SEQ ID NO : 92 : GTCGACTACA AAGAAGACTT CAACGACAAC GAGCAGTGGT TCGCCAAGGT CAAGGAGCCG 60 TTGTCGCGCA AGCAGGACAT AGGCGCCGAC CTGGTGATCC CCACCGAGTT CATGGCCGCG 120 CGCGTCAAGG GCCTGGGATG GCTCAATGAG ATCAGCGAAG CCGGCGTGCC CAATCGCAAG 180 AATCTGCGTC AGGACCTGTT GGACTCGAGC ATCGACGAGG GCCGCAAGTT CACCGCGCCG 240 TACATGACCG GCATGGTCGG TCTCGCCTAC AACAAGGCAG CCACCGGACG CGATATCCGC 300 ACCATCGACG ACCTCTGGGA TCC 323 (2) INFORMATION FOR SEQ ID NO -93: (l) SEQUENCE CHARACTERISTICS. (A) LENGTH: 1341 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 3 CCCCACCCCC TTCCCTGGAG CCGACGAAAG GCACCCGCAC ATGTCCCGTG ACATCGATCC 60 CCACCTGCTG GCCCGAATGA CCGCACGCCG CACCTTGCGT CGCCGCTTCA TCGGCGGTGG 120 CGCCGCGGCC GCCGCGGGCC TGACCCTCGG TTCGTCGTTC CTGGCGGCGT GCGGGTCCGA 180 CAGTGGGACC TCGAGCACCA CGTCACAGGA CAGCGGCCCC GCCAGCGGCG CCCTGCGCGT 240 CTCCAACTGG CCGCTCTATA TGGCCGACGG TTTCATCGCA GCGTTCCAGA CCGCCTCGGG 300 CATCACGGTC GACTACAAAG AAGACTTCAA CGACAACGAG CAGTGGTTCG CCAAGGTCAA 360 GGAGCCGTTG TCGCGCAAGC AGGACATAGG CGCCGACCTG GTGATCCCCA CCGAGTTCAT 420 GGCCGCGCGC GTCAAGGGCC TGGGATGGCT CAATGAGATC AGCGAAGCCG GCGTGCCCAA 480 TCGCAAGAAT CTGCGTCAGG ACCTGTTGGA CTCGAGCATC GACGAGGGCC GCAAGTTCAC 540 CGCGCCGTAC ATGACCGGCA TGGTCGGTCT CGCCTACAAC AAGGCAGCCA CCGGACGCGA 600 TATCCGCACC ATCGACGACC TCTGGGATCC CGCGTTCAAG GGCCGCGTCA GTCTGTTCTC 660 CGACGTCCAG GACGGCCTCG GCATGATCAT GCTCTCGCAG GGCAACTCGC CGGAGAATCC 720 GACCACCGAG TCCATTCAGC AGGCGGTCGA TCTGGTCCGC GAACAGAACG ACAGGGGGTC 780 AGATCCGTCG CTTCACCGGC AACGACTACG CCGACGACCT GGCCGCAGAA ACATCGCCAT 840 CGCGCAGGCG TACTCCGGTG ACGTCGTGCA GCTGCAGGCG GACAACCCCG ATCTGCAGTT 900 CATCGTTCCC GAATCCGGCG GCGACTGGTT CGTCGACACG ATGGTGATCC CGTACACCAC 960 GCAGAACCAG AAGGCCGCCG AGGCGTGGAT CGACTACATC TACGACCGAG CCAACTACGC 1020 CAAGCTGGTC GCGTTCACCC AGTTCGTGCC CGCACTCTCG GACATGACCG ACGAACTCGC 1080 CAAGGTCGAT CCTGCATCGG CGGAGAACCC GCTGATCAAC CCGTCGGCCG AGGTGCAGGC 1140 GAACCTGAAG TCGTGGGCGG CACTGACCGA CGAGCAGACG CAGGAGTTCA ACACTGCGTA 1200 CGCCGCCGTC ACCGGCGGCT GACGCGGTGG TAGTGCCGAT GCGAGGGGCA TAAATGGCCC 1260 TGCGGACGCG AGGAGCATAA ATGGCCGGTG TCGCCACCAG CAGCCGTCAG CGGACAAGGT 1320 CGCTCCGTAT CTGATGGTCC T 1341 (2) INFORMATION FOR SEQ ID NO: 94: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 393 amino acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 94: Met Ser Arg Asp He Asp Pro His Leu Leu Ala Arg Met Thr Ala Arg 1 5 10 15 Arg Thr Leu Arg Arg Arg Phe He Gly Gly Gly Ala Ala Ala Ala Ala 20 25 30 Gly Leu Thr Leu Gly Ser Ser Phe Leu Ala Ala Cys Gly Ser Asp Ser 35 40 45 Gly Thr Ser Ser Thr Thr Ser Gin Asp Ser Gly Pro Ala Ser Gly Ala 50 55 60 Leu Arg Val Ser Asn Trp Pro Leu Tyr Met Ala Asp Gly Phe He Ala 65 70 75 80 Ala Phe Gin Thr Ala Ser Gly He Thr Val Asp Tyr Lys Glu Asp Phe 85 90 95 Asn Asp Asn Glu Gin Trp Phe Ala Lys Val Lys Glu Pro Leu Ser Arg 100 105 110 Lys Gin Asp He Gly Ala Asp Leu Val He Pro Thr Glu Phe Met Ala U5 120 125 Ala Arg Val Lys Gly Leu Gly Trp Leu Asn Glu He Ser Glu Ala Gly 130 135 140 Val Pro Asn Arg Lys Asn Leu Arg Gin Asp Leu Leu Asp Ser Ser He 145 ISO 155 160 Asp Glu Gly Arg Lys Phe Thr Ala Pro Tyr Met Thr Gly Met Val Gly 165 170 175 Leu Ala Tyr Asn Lys Ala Ala Thr Gly Arg Asp He Arg Thr He Asp 180 185 190 Asp Leu Trp Asp Pro Ala Phe Lys Gly Arg Val Ser Leu Phe Ser Asp 195 200 205 Val Gin Asp Gly Leu Gly Met He Met Leu Ser Gin Gly Asn Ser Pro 210 215 220 Glu Asn Pro Thr Thr Glu Ser He Gin Gin Ala Val Asp Leu Val Arg 225 230 235 240 Glu Gin Asn Asp Arg Gly Ser Asp Pro Ser Leu His Arg Gin Arg Leu 245 250 255 Arg Arg Arg Pro Gly Arg Arg Asn He Ala He Ala Gin Ala Tyr Ser 260 265 270 Gly Asp Val Val Gin Leu Gin Ala Asp Asn Pro Asp Leu Gin Phe He 275 280 285 Val Pro Glu Ser Gly Gly Asp Trp Phe Val Asp Thr Met Val He Pro 290 295 300 Tyr Thr Thr Gin Asn Gin Lys Ala Ala Glu Ala Trp He Asp Tyr He 305 310 315 320 Tyr Asp Arg Ala Asn Tyr Ala Lys Leu Val Ala Phe Thr Gin Phe Val 325 330 335 Pro Ala Leu Ser Asp Met Thr Asp Glu Leu Ala Lys Val Asp Pro Ala 340 345 350 Ser Ala Glu Asn Pro Leu He Asn Pro Ser Ala Glu Val Gin Ala Asn 355 360 365 Leu Lys Ser Trp Ala Ala Leu Thr Asp Glu Gin Thr Gin Glu Phe Asn 370 375 380 Thr Ala Tyr Ala Ala Val Thr Gly Gly 385 390 (2) INFORMATION FOR SEQ ID NO 95 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 22 base pairs (B) TYPE, nucleic acid (C) STRANDEDNESS single (D) TOPOLOGY linear (u) MOLECULE TYPE Other (xi ) SEQUENCE DESCRIPTION SEQ ID NO: 95 ATGTCCCGTG ACATCGATCC CC 2 (2) INFORMATION FOR SEQ ID NO 96 (l) SEQUENCE CHARACTERISTICS (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single CD). TOPOLOGY, linear (n) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 96: ATCGGCACTA CCACCGCGTC A 21 (2) INFORMATION FOR SEQ ID NO : 97 (l) SEQUENCE CHARACTERISTICS: (A) LENGTH- 861 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS- single (D) TOPOLOGY linear (a) MOLECULE TYPE. Genomic DNA (xi) SEQUENCE DESCRIPTION SEQ ID NO 97 GCCGGCGCTC GCATATCTCG CGATCTTCTT CCGTGGTGCC GTTCTTCTCG CTGGCACGCA 60 CCTCGTTGTC GGAGACCGGC GGCTCGGTGT TCATGCCGAC GCTGACGTTC GCCTGGGACT 120 TCGGCAACTA CGTCGACGCG TTCACGATGT ACCACGAGCA GATCTTCCGC TCGTTCGGCT 180 ACGCGTTCGT CGCCACGGTG CTGTGCCTGT TGCTGGCGTT CCCGCTGGCC TACGTCATCG 240 CGTTCAAGGC CGGCCGGTTC AAGAACCTGA TCCTGGGGCT GGTGATCCTG CCGTTCTTCG 300 TCACGTTCCT GATCCGCACC ATTGCGTGGA AGACGATCCT GGCCGACGAA GGCTGGGTGG 360 TCACCGCGCT GGGCGCCATC GGGCTGCTGC CTGACGAGGG CCGGCTGCTG TCCACCAGCT 420 GGGCGGTCAT CGGCGGTCTG ACCTACAACT GGATCATCTT CATGATCCTG CCGCTGTACG 480 TCAGCCTGGA GAAGATCGAC CCGCGTCTGC TGGAGGCCTC CCAGGACCTC TACTCGTCGG 540 CGCCGCGCAG CTTCGGCAAG GTGATCCTGC CGATGGCGAT GCCCGGGGTG CTGGCCGGGA 600 GCATGCTGGT GTTCATCCCG GCCGTCGGCG ACTTCATCAA CGCCGACTAT CTCGGCAGTA 660 CCCAGACCAC CATGATCGGC AACGTGATCC AGAAGCAGTT CCTGGTCGTC AAGGACTATC 720 CGGCGGCGGC CGCGCTGAGT CTGGGGCTGA TGTTGCTGAT CCTGATCGGC GTGCTCCTCT 780 ACACACGGGC GCTGGGTTCG GAGGATCTGG TATGACCACC CAGGCAGGCG CCGCACTGGC 840 CACCGCCGCC CAGCAGGATC C 861 (2) INFORMATION FOR SEQ ID NO.98 (l) SEQUENCE CHARACTERISTICS. (A) LENGTH. 259 ammo acids (B) TYPE: amino acid Sr STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xl) SEQUENCE DESCRIPTION: SEQ ID NO: 98 Val Val Pro Phe Phe Ser Leu Ala Arg Thr Ser Leu Ser Glu Thr Gly 1 5 ιo 15 Gly Ser Val Phe Met Pro Thr Leu Thr Phe Ala Trp Asp Phe Gly Asn 20 25 30 Tyr Val Asp Ala Phe Thr Met Tyr His Glu Gin He Phe Arg Ser Phe 35 40 45 Gly Tyr Ala Phe Val Ala Thr Val Leu Cys Leu Leu Leu Ala Phe Pro 50 55 60 Leu Ala Tyr Val He Ala Phe Lys Ala Gly Arg Phe Lys Asn Leu He 65 70 75 80 Leu Gly Leu Val He Leu Pro Phe Phe Val Thr Phe Leu He Arg Thr 85 90 95 He Ala Trp Thr He Leu Ala Asp Glu Gly Trp Val Val Thr Ala Leu 100 105 ° Gly Ala He Gly Leu Leu Pro Asp Glu Gly Arg Leu Leu Ser Thr Ser 115 120 125 Trp Ala Val He Gly Gly Leu Thr Tyr Asn Trp He He Phe Met He 130 135 140 Leu Pro Leu Tyr Val Ser Leu Glu Lys He Asp Pro Arg Leu Leu Glu 145 150 155 160 Ala Ser Gin Asp Leu Tyr Ser Ser Ala Pro Arg Ser Phe Gly Lys Val 165 170 175 He Leu Pro Met Ala Met Pro Gly Val Leu Ala Gly Ser Met Leu Val 180 185 190 Phe He Pro Ala Val Gly Asp Phe He Asn Ala Asp Tyr Leu Gly Ser 195 200 205 Thr Gin Thr Thr Met He Gly Asn Val He Gin Lys Gin Phe Leu Val 210 215 220 Val Lys Asp Tyr Pro Ala Ala Ala Ala Leu Ser Leu Gly Leu Met Leu 225 230 235 240 Leu He Leu He Gly Val Leu Leu Tyr Thr Arg Ala Leu Gly Ser Glu 245 250 255 Asp Leu Val (2) INFORMATION FOR SEQ ID NO: 99: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 277 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 99: GTAATCTTTG CTGGAGCCCG TACGCCGGTA GGCAAACTCA TGGGTTCGCT CAAGGACTTC 60 AAGGGCAGCG ATCTCGGTGC CGTGGCGATC AAGGGCGCCC TGGAGAAAGC CTTCCCCGGC 120 GTCGACGACC CTGCTCGTCT CGTCGAGTAC GTGATCATGG GCCAAGTGCT CTCCGCCGGC 180 GCCGGCCAGA TGCCCGCCCG CCAGGCCGCC GTCGCCGCCG GCATCCCGTG GGACGTCGCC 240 TCGCTGACGA TCAACAAGAT GTGCCTGTCG GGCATCG 277 (2) INFORMATION FOR SEQ ID NO: 100: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 92 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 100: Val He Phe Ala Gly Ala Arg Thr Pro Val Gly Lys Leu Met Gly Ser 1 5 10 15 Leu Lys Asp Phe Lys Gly Ser Asp Leu Gly Ala Val Ala He Lys Gly 20 25 30 Ala Leu Glu Lys Ala Phe Pro Gly Val Asp Asp Pro Ala Arg Leu Val 35 40 45 Glu Tyr Val He Met Gly Gin Val Leu Ser Ala Gly Ala Gly Gin Met 50 55 60 Pro Ala Arg Gin Ala Ala Val Ala Ala Gly He Pro Trp Asp Val Ala 65 70 75 80 Ser Leu Thr He Asn Lys Met Cys Leu Ser Gly He 85 90 (2) INFORMATION FOR SEQ ID NO.101 (l) SEQUENCE CHARACTERISTICS (A) LENGTH: 12 ammo acids (B) TYPE amino acid (C) STRANDEDNESS- single (D) TOPOLOGY linear In) MOLECULE TYPE: protein (ix) FEATURE. (A) NAME/KEY- Other (B) LOCATION: 1...1 (D) OTHER INFORMATION: Residue can be either Glu or Pro (A) NAME/KEY. Other (B) LOCATION: 2...2 (D) OTHER INFORMATION: Residue can be either Pro or Glu (xi) SEQUENCE DESCRIPTION. SEQ ID NO.101: Xaa Xaa Ala Asp Arg Gly Xaa Ser Lys Tyr Arg Xaa 1 5 10 <2) INFORMATION FOR SEQ ID NO: 102: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acids (B) TYPE: am o acid (C) STRANDEDNESS- single (D) TOPOLOGY: linear (a) MOLECULE TYPE: protein (Xl) SEQUENCE DESCRIPTION: SEQ ID NO:102. Xaa He Asp Glu Ser Leu Phe Asp Ala Glu Glu Lys Met Glu Lys Ala 1 5 10 15 Val Ser Val Ala Arg Asp Ser Ala 20 ( 2 ) INFORMATION FOR SEQ ID NO . 103 . (I) SEQUENCE CHARACTERISTICS (A) LENGTH 23 ammo acids (B) TYPE amino ac d (C) STRANDEDNESS single (D) TOPOLOGY linear (II) MOLECULE TYPE protein (Xl ) SEQUENCE DESCRIPTION SEQ ID NO 103 Xaa Xaa He Ala Pro Ala Thr Ser Gly Thr Leu Ser Glu Phe Xaa Ala 1 5 10 15 Xaa Lys Gly Val Thr Met Glu 20 (2) INFORMATION FOR SEQ ID NO 104 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 15 ammo acids (B) TYPE amino acid (C) STRANDEDNESS single (D) TOPOLOGY linear (ii) MOLECULE TYPE protein ( i) SEQUENCE DESCRIPTION SEQ ID NO 104 Pro Asn Val Pro Asp Ala Phe Ala Val Leu Ala Asp Arg Val Gly 1 5 10 15 (2) INFORMATION FOR SEQ ID NO 105 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 9 ammo acids (B) TYPE amino acid (C) STRANDEDNESS single (D) TOPOLOGY linear (ιι+ -MOLECULE TYPE protein (XI ) SEQUENCE DESCRIPTION SEQ ID NO 105 Xaa He Arg Val Gly Val Asn Gly Phe 1 5 (2) INFORMATION FOR SEQ ID NO: 106 (i) SEQUENCE CHARACTERISTICS (A) LENGTH 485 base pairs (B) TYPE nucleic acid (C) STRANDEDNESS single (D) TOPOLOGY linear (ll) MOLECULE TYPE cDNA (xi) SEQUENCE DESCRIPTION SEQ ID NO 106 10 AGCGGCTGGG ACATCAACAC CGCCGCCTTC GAGTGGTACG TCGACTCGGG TCTCGCGGTG 60 ATCATGCCCG TCGGCGGGCA GTCCAGCTTC TACAGCGACT GGTACAGCCC GGCCTGCGGT 120 AAGGCCGGCT GCCAGACCTA CAAGTGGGAG ACGTTCCTGA CCCAGGAGCT GCCGGCCTAC 180 CTCGCCGCCA ACAAGGGGGT CGACCCGAAC CGCAACGCGG CCGTCGGTCT GTCCATGGCC 240 GGTTCGGCGG CGCTGACGCT GGCGATCTAC CACCCGCAGC AGTTCCAGTA CGCCGGGTCG 300 CTGTCGGGCT ACCTGAACCC GTCCGAGGGG TGGTGGCCGA TGCTGATCAA CATCTCGATG 360 GGTGACGCGG GCGGCTACAA GGCCAACGAC ATGTGGGGTC GCACCGAGGA CCCGAGCAGC 420 GCCTGGAAGC GCAACGACCC GATGGTCAAC ATCGGCAAGC TGGTCGCCAA CAACACCCCC 480 CTCTC 485 (2) INFORMATION FOR SEQ ID NO: 107: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 501 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 107: ATGCCGGTGC GACGTGCGCG CAGTGCGCTT GCGTCCGTGA CCTTCGTCGC GGCCGCGTGC 60 GTGGGCGCTG AGGGCACCGC ACTGGCGGCG ACGCCGGACT GGAGCGGGCG CTACACGGTG 120 GTGACGTTCG CCTCCGACAA ACTCGGCACG AGTGTGGCCG CCCGCCAGCC AGAACCCGAC 180 TTCAGCGGTC AGTACACCTT CAGCACGTCC TGTGTGGGCA CCTGCGTGGC CACCGCGTCC 240 GACGGCCCGG CGCCGTCGAA CCCGACGATT CCGCAGCCCG CGCGCTACAC CTGGGACGGC 300 AGGCAGTGGT; " TGTTCAACTA CAACTGGCAG TGGGAGTGCT TCCGCGGCGC CGACGTCCCG 360 CGCGAGTACG CCGCCGCGCG TTCGCTGGTG TTCTACGCCC CGACCGCCGA CGGGTCGATG 420 TTCGGCACCT GGCGCACCGA NATCCTGGAN GGCCTCTGCA AGGGCACCGT GATCATGCCG 480 GTCGCGGCCT ATCCGGCGTA G 501 (2) INFORMATION FOR SEQ ID NO: 108: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 180 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 108: 11 ATGAACCAGC CGCGGCCCGA GGCCGAGGCG AACCTGCGGG GCTACTTCAC CGCCAACCCG 60 GCGGAGTACT ACGACCTGCG GGGCATCCTC GCCCCGATCG GTGACGCGCA GCGCAACTGC 120 AACATCACCG TGCTGCCGGT AGAGCTGCAG ACGGCCTACG ACACGTTCAT GGCCGGCTGA 180 (2) INFORMATION FOR SEQ ID NO: 109: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 166 ammo acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 109: Met Pro Val Arg Arg Ala Arg Ser Ala Leu Ala Ser Val Thr Phe Val 1 5 10 15 Ala Ala Ala Cys Val Gly Ala Glu Gly Thr Ala Leu Ala Ala Thr Pro 20 25 30 Asp Trp Ser Gly Arg Tyr Thr Val Val Thr Phe Ala Ser Asp Lys Leu 35 40 45 Gly Thr Ser Val Ala Ala Arg Gin Pro Glu Pro Asp Phe Ser Gly Gin 50 55 60 Tyr Thr Phe Ser Thr Ser Cys Val Gly Thr Cys Val Ala Thr Ala Ser 65 70 75 80 Asp Gly Pro Ala Pro Ser Asn Pro Thr He Pro Gin Pro Ala Arg Tyr 85 90 95 Thr Trp Asp Gly Arg Gin Trp Val Phe Asn Tyr Asn Trp Gin Trp Glu 100 105 110 Cys Phe Arg Gly Ala Asp Val Pro Arg Glu Tyr Ala Ala Ala Arg Ser 115 120 125 Leu Val Phe Tyr Ala Pro Thr Ala Asp Gly Ser Met Phe Gly Thr Trp 130 135 140 Arg Thr Xaa He Leu Xaa Gly Leu Cys Lys Gly Thr Val He Met Pro 145 150 155 160 Val Ala Ala Tyr Pro Ala 165 (2) INFORMATION FOR SEQ ID NO:110: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 74 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 110: Pro Arg Asp Thr His Pro Gly Ala Asn Gin Ala Val Thr Ala Ala Met 1 5 10 15 Asn Gin Pro Arg Pro Glu Ala Glu Ala Asn Leu Arg Gly Tyr Phe Thr 20 25 30 Ala Asn Pro Ala Glu Tyr Tyr Asp Leu Arg Gly He Leu Ala Pro He 35 40 45 Gly Asp Ala Gin Arg Asn Cys Asn He Thr Val Leu Pro Val Glu Leu 50 55 60 Gin Thr Ala Tyr Asp Thr Phe Met Ala Gly 65 70 (2) INFORMATION FOR SEQ ID NO : 111 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 503 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID MO : 111 : ATGCAGGTGC GGCGTGTTCT GGGCAGTGTC GGTGCAGCAG TCGCGGTTTC GGCCGCGTTA 60 TGGCAGACGG GGGTTTCGAT ACCGACCGCC TCAGCGGATC CGTGTCCGGA CATCGAGGTG 120 ATCTTCGCGC GCGGGACCGG TGCGGAACCC GGCCTCGGGT GGGTCGGTGA TGCGTTCGTC 180 AACGCGCTGC GGCCCAAGGT CGGTGAGCAG TCGGTGGGCA CCTACGCGGT GAACTACCCG 240 GCAGGATTCG GACTTCGACA AATCGGCGCC CATGGGCGCG GCCGACGCAT CGGGGCGGGT 300 GCAGTGGATG GCCGACAACT GCCCGGACAC CAAGCTTGTC CTGGGCGGCA TGTCGCANGG 360 CGCCGGCGTC ATCGACCTGA TCACCGTCGA TCCGCGACCG CTGGGCCGGT TCACCCCCAC 420 CCCGATGCCG CCCCGCGTCG CCGACCACGT GGCCGCCGTT GTGGTCTTCG GAAATCCGTT 480 GCGCGACATC CGTGGTGGCG GTC 503 (2) INFORMATION FOR SEQ ID NO: 112: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 167 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 112: Met Gin V.al Arg Arg Val Leu Gly Ser Val Gly Ala Ala Val Ala Val 1 5 10 15 Ser Ala Ala Leu Trp Gin Thr Gly Val Ser He Pro Thr Ala Ser Ala 20 25 30 Asp Pro Cys Pro Asp He Glu Val He Phe Ala Arg Gly Thr Gly Ala 35 40 45 Glu Pro Gly Leu Gly Trp Val Gly Asp Ala Phe Val Asn Ala Leu Arg 50 55 60 Pro Lys Val Gly Glu Gin Ser Val Gly Thr Tyr Ala Val Asn Tyr Pro 65 70 75 80 Ala Gly Phe Asp Phe Asp Lys Ser Ala Pro Met Gly Ala Ala Asp Ala 85 90 95 Ser Gly Arg Val Gin Trp Met Ala Asp Asn Cys Pro Asp Thr Lys Leu 100 105 110 Val Leu Gly Gly Met Ser Xaa Gly Ala Gly Val He Asp Leu He Thr 115 120 125 Val Asp Pro Arg Pro Leu Gly Arg Phe Thr Pro Thr Pro Met Pro Pro 130 135 140 Arg Val Ala Asp His Val Ala Ala Val Val Val Phe Gly Asn Pro Leu 145 150 155 160 Arg Asp He Arg Gly Gly Gly 165 ( 2 ) I N FORMAT ION FOR SEQ I D NO : 113 : ( l ) S EQUENCE CHARACTERI ST ICS : ( A ) LENGTH : 1569 base pai rs ( B ) TYPE : nucle i c acid ( C ) STRANDEDNESS : s ingl e ( D ) TOPOLOGY : l inear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 113: ATGGCCAAGA CAATTGCGTA TGACGAAGAG GCCCGCCGTG GCCTCGAGCG GGGCCTCAAC 60 GCCCTCGCAG ACGCCGTAAA GGTGACGTTG GGCCCGAAGG GTCGCAACGT CGTGCTGGAG 120 AAGAAGTGGG GCGCCCCCAC GATCACCAAC GATGGTGTGT CCATCGCCAA GGAGATCGAG 180 CTGGAGGACC CGTACGAGAA GATCGGCGCT GAGCTGGTCA AAGAGGTCGC CAAGAAGACC 240 GACGACGTCG CGGGCGACGG CACCACCACC GCCACCGTGC TCGCTCAGGC TCTGGTTCGC 300 GAAGGCCTGC GCAACGTCGC AGCCGGCGCC AACCCGCTCG GCCTCAAGCG TGGCATCGAG 360 AAGGCTGTCG AGGCTGTCAC CCAGTCGCTG CTGAAGTCGG CCAAGGAGGT CGAGACCAAG 420 GAGCAGATTT CTGCCACCGC GGCGATTTCC GCCGGCGACA CCCAGATCGG CGAGCTCATC 480 GCCGAGGCCA TGGACAAGGT CGGCAACGAG GGTGTCATCA CCGTCGAGGA GTCGAACACC 540 TTCGGCCTGC AGCTCGAGCT CACCGAGGGT ATGCGCTTCG ACAAGGGCTA CATCTCGGGT 600 TACTTCGTGA CCGACGCCGA GCGCCAGGAA GCCGTCCTGG AGGATCCCTA CATCCTGCTG 660 GTCAGCTCCA AGGTGTCGAC CGTCAAGGAT CTGCTCCCGC TGCTGGAGAA GGTCATCCAG 720 GCCGGCAAGC CGCTGCTGAT CATCGCCGAG GACGTCGAGG GCGAGGCCCT GTCCACGCTG 780 GTGGTCAACA AGATCCGCGG CACCTTCAAG TCCGTCGCCG TCAAGGCTCC GGGCTTCGGT 840 GACCGCCGCA AGGCGATGCT GCAGGACATG GCCATCCTCA CCGGTGGTCA GGTCGTCAGC 900 GAAAGAGTCG GGCTGTCCCT GGAGACCGCC GACGTCTCGC TGCTGGGCCA GGCCCGCAAG 960 " ~ " GTCGTCGTCA CCAAGGACGA GACCACCATC GTCGAGGGCT CGGGCGATTC CGATGCCATC 1020 GCCGGCCGGG TGGCTCAGAT CCGCGCCGAG ATCGAGAACA GCGACTCCGA CTACGACCGC 1080 GAGAAGCTGC AGGAGCGCCT GGCCAAGCTG GCCGGCGGTG TTGCGGTGAT CAAGGCCGGA 1140 GCTGCCACCG AGGTGGAGCT CAAGGAGCGC AAGCACCGCA TCGAGGACGC CGTCCGCAAC 1200 GCGAAGGCTG CCGTCGAAGA GGGCATCGTC GCCGGTGGCG GCGTGGCTCT GCTGCAGTCG 1260 GCTCCTGCGC TGGACGACCT CGGCCTGACG GGCGACGAGG CCACCGGTGC CAACATCGTC 1320 CGCGTGGCGC TGTCGGCTCC GCTCAAGCAG ATCGCCTTCA ACGGCGGCCT GGAGCCCGGC 1380 GTCGTTGCCG AGAAGGTGTC CAACCTGCCC GCGGGTCACG GCCTCAACGC CGCGACCGGT 1440 GAGTACGAGG ACCTGCTCAA GGCCGGCGTC GCCGACCCGG TGAAGGTCAC CCGCTCGGCG 1500 CTGCAGAACG CGGCGTCCAT CGCGGCTCTG TTCCTCACCA CCGAGGCCGT CGTCGCCGAC 1560 AAGCCGGAG 1569 (2; INFORMATION FOR SEQ ID NO: 114: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 523 amino acids (B) TYPE: am o acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 114 : Met Ala Lys Thr He Ala Tyr Asp Glu Glu Ala Arg Arg Gly Leu Glu 1 5 10 15 Arg Gly Leu Asn Ala Leu Ala Asp Ala Val Lys Val Thr Leu Gly Pro 20 25 30 Lvs Gly Arg Asn Val Val Leu Glu Lys Lys Trp Gly Ala Pro Thr He 35 40 45 Thr Asn Asp Gly Val Ser He Ala Lys Glu He Glu Leu Glu Asp Pro 50 55 60 Tyr Glu Lys He Gly Ala Glu Leu Val Lys Glu Val Ala Lys Lys Thr 65 70 75 * 80 Asp Asp Val Ala Gly Asp Gly Thr Thr Thr Ala Thr Val Leu Ala Gin 85 90 95 Ala Leu Val Arg Glu Gly Leu Arg Asn Val Ala Ala Gly Ala Asn Pro 100 105 110 Leu Gly Leu Lys Arg Gly He Glu Lys Ala Val Glu Ala Val Thr Gin 115 120 125 Ser Leu Leu Lys Ser Ala Lys Glu Val Glu Thr Lys Glu Gin He Ser 130 135 140 Ala Thr Ala Ala He Ser Ala Gly Asp Thr Gin He Gly Glu Leu He 145 150 155 160 Ala Glu Ala Met Asp Lys Val Gly Asn Glu Gly Val He Thr Val Glu 165 170 175 Glu Ser Asn Thr Phe Gly Leu Gin Leu Glu Leu Thr Glu Gly Met Arg 180 185 190 Phe Asp Lys Gly Tyr He Ser Gly Tyr Phe Val Thr Asp Ala Glu Arg 195 200 205 Gin Glu Ala Val Leu Glu Asp Pro Tyr He Leu Leu Val Ser Ser Lys 210 215 220 Val Ser liar Val Lys Asp Leu Leu Pro Leu Leu Glu Lys Val He Gin 225 230 235 240 Ala Gly Lys Pro Leu Leu He He Ala Glu Asp Val Glu Gly Glu Ala 245 250 255 Leu Ser Thr Leu Val Val Asn Lys He Arg Gly Thr Phe Lys Ser Val 260 265 270 Ala Val Lys Ala Pro Gly Phe Gly Asp Arg Arg Lys Ala Met Leu Gin 275 280 285 Asp Met Ala He Leu Thr Gly Gly Gin Val Val Ser Glu Arg Val Gly 290 295 300 Leu Ser Leu Glu Thr Ala Asp Val Ser Leu Leu Gly Gin Ala Arg Lys 305 310 315 320 Val Val Val Thr Lys Asp Glu Thr Thr He Val Glu Gly Ser Gly Asp 325 330 335 Ser Asp Ala He Ala Gly Arg Val Ala Gin He Arg Ala Glu He Glu 340 345 350 Asn Ser Asp Ser Asp Tyr Asp Arg Glu Lys Leu Gin Glu Arg Leu Ala 355 360 365 Lys Leu Ala Gly Gly Val Ala Val He Lys Ala Gly Ala Ala Thr Glu 370 375 380 Val Glu Leu Lys Glu Arg Lys His Arg He Glu Asp Ala Val Arg Asn 385 390 395 400 Ala Lys Ala Ala Val Glu Glu Gly He Val Ala Gly Gly Gly Val Ala 405 410 415 Leu Leu Gin Ser Ala Pro Ala Leu Asp Asp Leu Gly Leu Thr Gly Asp 420 425 430 Glu Ala Thr Gly Ala Asn He Val Arg Val Ala Leu Ser Ala Pro Leu 435 440 445 Lys Gin He Ala Phe Asn Gly Gly Leu Glu Pro Gly Val Val Ala G1J 450 455 460 Lys Val Ser Asn Leu Pro Ala Gly His Gly Leu Asn Ala Ala Thr Gly 465 470 475 480 Glu Tyr Glu Asp Leu Leu Lys Ala Gly Val Ala ^sp Pro Val Lys Val 485 490 495 Thr Arg Ser Ala Leu Gin Asn Ala Ala Ser lie Ala Ala Leu Phe Leu 500 505 510 Thr Thr Glu Ala Val Val Ala Asp Lys Pro Glu 515 520 (2) INFORMATION FOR SEQ ID NO: 115: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 647 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (a) MOLECULE TYPE: Genomic RNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 115: ATGGCCAAGA CAATTGCGTA TGACGAAGAG GCCCGCCGTG GCCTCGAGCG GGGCCTCAAC 60 GCCCTCGCAG ACGCCGTAAA GGTGACGTTG GGCCCGAAGG GTCGCAACGT CGTGCTGGAG 120 AAGAAGTGGG GCGCCCCCAC GATCACCAAC GATGGTGTGT CCATCGCCAA GGAGATCGAG 180 CTGGAGGACC CGTACGAGAA GATCGGCGCT GAGCTGGTCA AAGAGGTCGC CAAGAAGACC 240 GACGACGTCG CGGGCGACGG CACCACCACC GCCACCGTGC TCGCTCAGGC TCTGGTTCGC 300 GAAGGCCTGC GCAACGTCGC AGCCGGCGCC AACCCGCTCG GCCTCAAGCG TGGCATCGAG 360 AAGGCTGTCG AGGCTGTCAC CCAGTCGCTG CTGAAGTCGG CCAAGGAGGT CGAGACCAAG 420 GAGCAGATXI .CTGCCACCGC GGCGATTTCC GCCGGCGACA CCCAGATCGG CGAGCTCATC 480 GCCGAGGCCA TGGACAAGGT CGGCAACGAG GGTGTCATCA CCGTCGAGGA GTCGAACACC 540 TTCGGCCTGC AGCTCGAGCT CACCGAGGGT ATGCGCTTCG ACAAGGGCTA CATCTCGGGT 600 TACTTCGTGA CCGACGCCGA GCGCCAGGAA GCCGTCCTGG AGGATCC 647 (2) INFORMATION FOR SEQ ID NO : 116 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 927 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 116: GATCCCTACA TCCTGCTGGT CAGCTCCAAG GTGTCGACCG TCAAGGATCT GCTCCCGCTG 60 CTGGAGAAGG TCATCCAGGC CGGCAAGCCG CTGCTGATCA TCGCCGAGGA CGTCGAGGGC 120 GAGGCCCTGT CCACGCTGGT GGTCAACAAG ATCCGCGGCA CCTTCAAGTC CGTCGCCGTC 180 AAGGCTCCGG GCTTCGGTGA CCGCCGCAAG GCGATGCTGC AGGACATGGC CATCCTCACC 240 GGTGGTCAGG TCGTCAGCGA AAGAGTCGGG CTGTCCCTGG AGACCGCCGA CGTCTCGCTG 300 CTGGGCCAGG CCCGCAAGGT CGTCGTCACC AAGGACGAGA CCACCATCGT CGAGGGCTCG 360 GGCGATTCCG ATGCCATCGC CGGCCGGGTG GCTCAGATCC GCGCCGAGAT CGAGAACAGC 420 GACTCCGACT ACGACCGCGA GAAGCTGCAG GAGCGCCTGG CCAAGCTGGC CGGCGGTGTT 480 GCGGTGATCA AGGCCGGAGC TGCCACCGAG GTGGAGCTCA AGGAGCGCAA GCACCGCATC 540 GAGGACGCCG TCCGCAACGC GAAGGCTGCC GTCGAAGAGG GCATCGTCGC CGGTGGCGGC 600 GTGGCTCTGC TGCAGTCGGC TCCTGCGCTG GACGACCTCG GCCTGACGGG CGACGAGGCC 660 ACCGGTGCCA ACATCGTCCG CGTGGCGCTG TCGGCTCCGC TCAAGCAGAT CGCCTTCAAC 720 GGCGGCCTGG AGCCCGGCGT CGTTGCCGAG AAGGTGTCCA ACCTGCCCGC GGGTCACGGC 780 CTCAACGCCG CGACCGGTGA GTACGAGGAC CTGCTCAAGG CCGGCGTCGC CGACCCGGTG 840 AAGGTCACCC GCTCGGCGCT GCAGAACGCG GCGTCCATCG CGGCTCTGTT CCTCACCACC 900 GAGGCCGTCG TCGCCGACAA GCCGGAG 927 (2) INFORMATION FOR SEQ ID NO: 117: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 215 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein ( -SEQUENCE DESCRIPTION: SEQ ID NO: 117: Met Ala Lys Thr He Ala Tyr Asp Glu Glu Ala Arg Arg Gly Leu Glu 1 5 10 15 Arg Gly Leu Asn Ala Leu Ala Asp Ala Val Lys Val Thr Leu Gly Pro 20 25 30 Lys Gly Arg Asn Val Val Leu Glu Lys Lys Trp Gly Ala Pro Thr He 35 40 45 Thr Asn Asp Gly Val Ser He Ala Lys Glu He Glu Leu Glu Asp Pro 50 55 60 Tyr Glu Lys He Gly Ala Glu Leu Val Lys Glu Val Ala Lys Lys Thr 65 70 75 80 Asp Asp Val Ala Gly Asp Gly Thr Thr Thr Ala Thr Val Leu Ala Gin 85 90 95 Ala Leu Val Arg Glu Gly Leu Arg Asn Val Ala Ala Gly Ala Asn Pro 100 105 110 Leu Gly Leu Lys Arg Gly He Glu Lys Ala Val Glu Ala Val Thr Gin 115 120 125 Ser Leu Leu Lys Ser Ala Lys Glu Val Glu Thr Lys Glu Gin He Ser 130 135 140 Ala Thr Ala Ala He Ser Ala Gly Asp Thr Gin He Gly Glu Leu He 145 150 155 160 17 Ala Glu Ala Me:: ASP Lys Val Gly Asn Glu Gly Val Ho Thr Val Glu 165 170 175 Glu Ser Asn Thr Phe Gly Leu Gin Leu Glu Leu Thr Glu Gly Mer Arg 180 185 190 Phe Asp Lvs Gly Tyr He Ser Gly Tyr Phe Val Thr Asp Ala Glu Arg 195 200 205 Gin Glu Ala Val Leu Glu Asp 210 215 (2) INFORMATION FOR SEQ ID NO : 11 : (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 309 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 118: Asp Pro Tyr He Leu Leu Val Ser Ser Lys Val Ser Thr Val Lys Asp 1 5 10 15 Leu Leu Pro Leu Leu Glu Lys Val He Gin Ala Gly Lys Pro Leu Leu 20 25 30 He He Ala Glu Asp Val Glu Gly Glu Ala Leu Ser Thr Leu Val Val 35 40 45 Asn Lys He Arg Gly Thr Phe Lys Ser Val Ala Val Lys Ala Pro Gly 50 55 60 Phe Gly Asp Arg Arg Lys Ala Met Leu Gin Asp Met Ala He Leu Thr 65 70 75 80 Gly Gly Gin Val Val Ser Glu Arg Val Gly Leu Ser Leu Glu Thr Ala 85 90 95 Asp Val Ser Leu Leu Gly Gin Ala Arg Lys Val Val Val Thr Lys Asp 100 105 110 Glu Thr Thr He Val Glu Gly Ser Gly Asp Ser Asp Ala He Ala Gly 115 120 125 Arg Val Ala Gin He Arg Ala Glu He Glu Asn Ser Asp Ser Asp Tyr 130 135 140 Asp Arg Glu Lys Leu Gin Glu Arg Leu Ala Lys Leu Ala Gly Gly Val 145 150 155 160 Ala Val He Lys Ala Gly Ala Ala Thr Glu Val Glu Leu Lys Glu Arg 165 170 175 Lys His Arg He Glu Asp Ala Val Arg Asn Ala Lys Ala Ala Val Glu 180 185 190 Glu Gly He Val Ala Gly Gly Gly Val Ala Leu Leu Gin Ser Ala Pro 195 200 205 Ala Leu Asp Asp Leu Gly Leu Thr Gly Asp Glu Ala Thr Gly Ala Asn 210 215 220 He Val Arg Val Ala Leu Ser Ala Pro Leu Lys Gin He Ala Pne Asn 225 230 235 240 Gly Gly Leu Glu Pro Gly Val Val Ala Glu Lys Val Ser Asn Leu Pro 245 250 255 Ala Gly His Gly Leu Asn Ala Ala Thr Gly Glu Tyr Glu Asp Leu Leu 260 265 270 Lys Ala Gly Val Ala Asp Pro Val Lys Val Thr Arg Ser Ala Leu Gin 275 280 285 Asn Ala Ala Ser He Ala Ala Leu Phe Leu Thr Thr Glu Ala Val Val 290 295 300 Ala Asp Lys Pro Glu 305 (2) INFORMATION FOR SEQ ID NO : 119 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 162 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 119: CTCGTACAGG CGACGGAGAT CTCCGACGAC GCCACGTCGG TACGGTTGGT CGCCACCCTG 60 TTCGGCGTCG TGTTGTTGAC GTTGGTGCTG TCCGGGCTCA ACGCCACCCT CATCCAGGGC 120 GCACCAGAAG ACAGCTGGCG CAGGCGGATT CCGTCGATCT TC 162 (2) INFORMATION FOR SEQ ID NO: 120: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1366 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 120: GATGAGCAGC GTGCTGAACT CGACCTGGTT GGCCTGGGCC GTCGCGGTCG CGGTCGGGTT 60 CCCGGTGCTG CTGGTCGTGC TGACCGAGGT GCACAACGCG TTGCGTCGGC GCGGCAGCGC 120 GCTGGCCCGC CCGGTGCAAC TCCTGCGTAC CTACATCCTG CCGCTGGGCG CGTTGCTGCT 130 CCTGCTGGTA CAGGCGATGG AGATCTCCGA CGACGCCACG TCGGTACGGT TGGTCGCCAC 240 CCTGTTCGGC GTCGTGTTGT TGACGTTGGT GCTGTCCGGG CTCAACGCCA CCCTCATCCA 300 GGGCGCACCA GAAGACAGCT GGCGCAGGCG GATTCCGTCG ATCTTCCTCG ACGTCGCGCG 360 CTTCGCGCTG ATCGCGGTCG GTATCACCGT GATCATGGCC TATGTCTGGG GCGCGAACGT 420 GGGGGGCCTG TTCACCGCAC TGGGCGTCAC TTCCATCGTT CTTGGCCTGG CTCTGCAGAA 480 _. TTCGGTCGGT CAGATCATCT CGGGTCTGCT GCTGCTGTTC GAGCAACCGT TCCGGCTCGG 540 CGACTGGATC ACCGTCCCCA CCGCGGCGGG CCGGCCGTCC GCCCACGGCC GCGTGGTGGA 600 AGTCAACTGG CGTGCAACAC ATATCGACAC CGGCGGCAAC CTGCTGGTAA TGCCCAACGC 660 CGAACTCGCC GGCGCGTCGT TCACCAATTA CAGCCGGCCC GTGGGAGAGC ACCGGCTGAC 720 CGTCGTCACC ACCTTCAACG CCGCGGACAC CCCCGATGAT GTCTGCGAGA TGCTGTCGTC 780 GGTCGCGGCG TCGCTGCCCG AACTGCGCAC CGACGGACAG ATCGCCACGC TCTATCTCGG 840 TGCGGCCGAA TACGAGAAGT CGATCCCGTT GCACACACCC GCGGTGGACG ACTCGGTCAG 900 GAGCACGTAC CTGCGATGGG TCTGGTACGC CGCGCGCCGG CAGGAACTTC GCCTNAACGG 960 CGTCGCCGAC GANTTCGACA CGCCGGAACG GATCGCCTCG GCCATGCGGG CTGTGGCGTC 1020 CACACTGCGC TTGGCAGACG ACGAACAGCA GGAGATCGCC GACGTGGTGC GTCTGGTCCG 1080 TTACGGCAAC GGGGAACGCC TCCAGCAGCC GGGTCAGGTA CCGACCGGGA TGAGGTTCAT 1140 CGTAGACGGC AGGGTGAGTC TGTCCGTGAT CGATCAGGAC GGCGACGTGA TCCCGGCGCG 1200 GGTGCTCGAG CGTGGCGACT TCCTGGGGCA GACCACGCTG ACGCGGGAAC CGGTACTGGC 1260 GACCGCGCAC GCGCTGGAGG AAGTCACCGT GCTGGAGATG GCCCGTGACG AGATCGAGCG 1320 CCTGGTGCAC CGAAAGCCGA TCCTGCTGCA CGTGATCGGG GCCGTG 1366 (2) INFORMATION FOR SEQ ID NO: 121: ( ) SEQUENCE CHARACTERISTICS : (A) LENGTH: 455 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 121: Met Ser Ser Val Leu Asn Ser Thr Trp Leu Ala Trp Ala Val Ala Val 1 5 10 15 Ala Val Gly Phe Pro Val Leu Leu Val Val Leu Thr Glu Val His Asn 20 25 30 Ala Leu Arg Arg Arg Gly Ser Ala Leu Ala Arg Pro Val Gin Leu Leu 35 40 45 Arg Thr Tyr He Leu Pro Leu Gly Ala Leu Leu Leu Leu Leu Val Gin 50 55 60 Ala Met Glu He Ser Asp Asp Ala Thr Ser Val Arg Leu Val Ala Thr 65 70 75 80 Leu Phe Gly Val Val Leu Leu Thr Leu Val Leu Ser Gly Leu Asn Ala 85 90 95 Thr Leu He Gin Gly Ala Pro Glu Asp Ser Trp Arg Arg Arg He Pro 100 105 110 Ser He Phe Leu Asp Val Ala Arg Phe Ala Leu He Ala Val Gly He 115 120 125 Thr Val He Met Ala Tyr Val Trp Gly Ala Asn Val Gly Gly Leu Phe 130 135 140 Thr Ala Leu Gly Val Thr Ser He Val Leu Gly Leu Ala Leu Gin Asn 145 150 155 160 Ser Val GJy Gin He He Ser Gly Leu Leu Leu Leu Phe Glu Gin Pro 165 170 175 Phe Arg Leu Gly Asp Trp He Thr Val Pro Thr Ala Ala Gly Arg Pro 180 185 190 Ser Ala His Gly Arg Val Val Glu Val Asn Trp Arg Ala Thr His He 195 200 205 Asp Thr Gly Gly Asn Leu Leu Val Met Pro Asn Ala Glu Leu Ala Gly 210 215 220 Ala Ser Phe Thr Asn Tyr Ser Arg Pro Val Gly Glu His Arg Leu Thr 225 230 235 240 Val Val Thr Thr Phe Asn Ala Ala Asp Thr Pro Asp Asp Val Cys Glu 245 250 255 Met Leu Ser Ser Val Ala Ala Ser Leu Pro Glu Leu Arg Thr Asp Gly 260 265 270 Gin He Ala Thr Leu Tyr Leu Gly Ala Ala Glu Tyr Glu Lys Ser He 275 280 285 Pro Leu His Thr Pro Ala Val Asp Asp Ser Val Arg Ser Thr Tyr Leu 290 295 300 Arg Trp Val Trp Tyr Ala Ala Arg Arg Gin Glu Leu Arg Xaa Asn Gly 305 ' 310 315 320 Val Ala Asp Xaa Phe Asp Thr Pro Glu Arg He Ala Ser Ala Met Arg 325 330 335 Ala Val Ala Ser Thr Leu Arg Leu Ala Asp Asp Glu Gin Gin Glu lie 340 345 50 Ala Asp Val Val Arg Leu Val Arg Tyr Gly Asn Gly Glu Arg LeL. Gm 355 360 365 Gin Pro Gly GIr. Val Pro Thr Gly Mer Arg Phe He Val Asp Gly Arg 370 375 380 Val Ser Leu Ser Val He Asp Gin Asp Gly Asp Val He Pro Ala Arg 385 390 395 400 Val Leu Glu Arg Gly Asp Phe Leu Gly Gin Thr Thr Leu Thr Arg Glu 405 410 415 Pro Val Lea Ala Thr Ala His Ala Leu Glu Glu Val Thr Va Leu Glu 420 425 430 Met Ala Arg Asp Glu lie Glu Arg Leu Val his Arg Lys Pro lie Leu 435 440 445 (2) INFORMATION FOR SEQ ID NO: 122: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 898 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( i) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 122: ATGACAATTC TGCCCTGGAA TGCGCGAACG TCTGAACACC CGACGCGAAA AAGACGCGGG 60 CGCTACCACC TCCTGTCGCG GATGAGCATC CAGTCCAAGT TGCTGCTGAT GCTGCTTCTG 120 ACCAGCATTC TCTCGGCTGC GGTGGTCGGT TTCATCGGCT ATCAGTCCGG ACGGTCCTCG 180 CTGCGCGCAT CGGTGTTCGA CCGCCTCACC GACATCCGCG AGTCGCAGTC GCGCGGGTTG 240 GAGAATCAGT TCGCGGACCT GAAGAACTCG ATGGTGATTT ACTCGCGCGG CAGCACTGCC 300 ACGGAGGCGA TCGGCGCGTT CAGCGACGGT TTCCGTCAGC TCGGCGATGC GACGATCAAT 360 ACCGGGCAGG CGGCGTCATT GCGCCGTTAC TACGACCGGA CGTTCGCCAA CACCACCCTC 420 GACGACAGCC.GAAACCGCGT CGACGTCCGC GCGCTCATCC CGAAATCCAA CCCCCAGCGC 480 TATCTGCAGG CGCTCTATAC CCCGCCGTTT CAGAACTGGG AGAAGGCGAT CGCGTTCGAC 540 GACGCGCGCG ACGGCAGCGC CTGGTCGGCC GCCAATGCCA GATTCAACGA GTTCTTCCGC 600 GAGATCGTGC ACCGCTTCAA CTTCGAGGAT CTGATGCTGC TCGACCTCGA GGGCAACGTG 660 GTGTACTCCG CCTACAAGGG GCCGGATCTC GGGACAAACA TCGTCAACGG CCCCTATCGC 720 AACCGGGAAC TGTCGGAAGC CTACGAGAAG GCGGTCGCGT CGAACTCGAT CGACTATGTC 780 GGTGTCACCG ACTTCGGGTG GTACCTGCCT GCCGAGGAAC CGACCGCCTG GTTCCTGTCC 840 CCGGTCGGGT TGAAGGACCG AGTCGACGGT GTGATGGCGG TCCAGTTCCC CGGAATTC 898 (2) INFORMATION FOR SEQ ID NO: 123: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1259 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ 13 NO.1/3 CGCAATTGAT GACGGCGCGG GGACAGTGGC GTGACACCGC CATGGGAGAC ACCGGTGAGA 60 CCATCCTGGT CGGACCGGAC AATCTGATGC GCTCGGACT^ CCGGCTGTTC CGCGAGAACC 120 GGC-AGAAGTT CCTGGCCGAC GTCGTCGAGG GGGGAACCCC CCGGAGGTC GCCGACGAAT 180 CGGTTGACCG CCGCGGCACC ACGCTGGTGC AGCCGGTGAC CACCCGCTCC GTCGAGGAGG 240 CCCAACGCGG CAACACCGGG ACGACGATCG AGGACGACTA TCTCGGCCAC GAGGCGTTAC 300 AGGCGTACTC ACCGGTGGAC CTGCCGGGAC TGCACTGGGT GATCGTGGCC AAGATCGACA 360 CCGACGAGGC GTTCGCCCCG GTGGCGCAGT TCACCAGGAC CCTGGTGCTG TCGACGGTGA 420 TCATCATCTT CGGCGTGTCG CTGGCGGCCA TGCTGCTGGC GCGGTTGTTC GTCCGTCCGA 480 TCCGGCGGTT GCAGGCCGGC GCCCAGCAGA TCAGCGGCGG TGACT^CCGC CTCGCTCTGC 540 CGGTGTTGTC TCGTGACGAA TTCGGCGATC TGACAACAGC TTTCAACGAC ATG^GTCGCA 600 ATCTGTCGAT CAAGGACGAG CTGCTCGGCG AGGAGCGCGC CGAGAACCAA CGGCTGATGC 660 TGTCCCTGAT GCCCGAACCG GTGATGCAGC GCTACCTCGA CGGGGAGGAG ACGATCGCCC 720 AGGACCACAA GAACGTCACG GTGATCTTCG CCGACATGAT GGGCCTCGAC GAGTTGTCGC 780 GCATGTTGAC CTCCGAGGAA CTGATGGTGG TGGTCAACGA CCTGACCCGC CAGTTCGACG 840 CCGCCGCCGA GAGTCTCGGG GTCGACCACG TGCGGACGCT GCACGACGGG TACCTGGCCA 900 GCTGCGGGTT AGGCGTGCCG CGGCTGGACA ACGTCCGGCG CACGGTCAAT TTCGCGATCG 960 AAATGGACCG CATCATCGAC CGGCACGCCG CCGAGTCCGG GCACGACCTG CGGCTCCGCG 1020 CGGGCATCGA CACCGGGTCG GCGGCCAGCG GGCTGGTGGG GCGGTCCACG TTGGCGTACG 1080 ACATGTGGGC -TTCGGCGGTC GATGTCGCCT ACCAGGTGCA GCGCGGCTCC CCCCAGCCCG 1140 GCATCTACGT CACCTCGCGG GTGCACGAGG TCATGCAGGA AACTCTCGAC TTCGTCGCCG 1200 CCGGGGAGGT CGTCGGCGAG CGCGGCGTCG AGACGGTCTG GCGGTTGCAG GGCCACCCG 1259 (2) INFORMATION FOR SEQ ID NO: 124: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 299 ammo acids (C) STRANDEDNESS: single (D) TOPOLOGY: linear (a) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 124: Met Thr He Leu Pro Trp Asn Ala Arg Thr Ser Glu His Pro Thr Arg 1 5 10 15 Lys Arg Arg Gly Arg Tyr His Leu Leu Ser Arg Met Ser He Gin Ser 20 25 30 Lys Leu Leu Leu Met Leu Leu Leu Thr Ser He Leu Ser A^a Ala Val 35 40 45 Val Gly Phe He Gly Tyr Gin Ser Gly Arg Ser Ser Leu Arg Ala Ser 50 55 60 Val Phe Asp Arg Leu Thr Asp He Arg Glu Ser Gin Ser Arg Gly Leu 65 70 /5 80 Glu Asn Gin Phe Ala Asp Leu Lys Asn Ser Met Val He Tyr Ser Arg 85 90 95 Gly Ser Thr Ala Thr Glu Ala He Gly Ala Phe Ser Asp Gly Phe Arg 100 105 110 Gin Leu Gly Asp Ala Thr He Asn Thr Gly Gin Ala Ala Ser Leu Arg 115 120 125 Arg Tyr Tyr Asp Arg Thr Phe Ala Asn Thr Thr Leu Asp Asp Ser Gly 13C 135 140 Asn Arg Val Asp Val Arg Ala Leu He Pro Lys Ser Asn Pro Gin Arg 145 150 155 160 Tyr Leu Gin Ala Leu Tyr Thr Pro Pro Phe Gin Asn Trp Glu Lys Ala 165 170 175 He Ala Phe Asp Asp Ala Arg Asp Gly Ser Ala Trp Ser Ala Ala Asn 180 185 190 Ala Arg Phe Asn Glu Phe Phe Arg Glu He Val His Arg Phe Asn Phe 195 200 205 Glu Asp Leu Met Leu Leu Asp Leu Glu Gly Asn Val Val Tyr Ser Ala 210 215 220 Tyr Lys Gly Pro Asp Leu Gly Thr Asn He Val Asn Gly Pro Tyr Arg 225 230 235 240 Asn Arg Glu Leu Ser Glu Ala Tyr Glu Lys Ala Val Ala Ser Asn Ser 245 250 255 He Asp Tyr Val Gly Val Thr Asp Phe Gly Trp Tyr Leu Pro Ala Glu 260 265 270 Glu Pro Thr Ala Trp Phe Leu Ser Pro Val Gly Leu Lys Asp Arg Val 275 280 285 Asp Gly Val Met Ala Val Gin Phe Pro Gly He 290 295 (2) INFORMATION FOR SEQ ID NO: 125: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 419 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 125: Gin Leu Met Thr Ala Arg Gly Gin Trp Arg Asp Thr Gly Met Gly Asp 1 5 10 15 Thr Gly Glu Thr He Leu Val Gly Pro Asp Asn Leu Met Arg Ser Asp 20 25 30 Ser Arg Leu Phe Arg Glu Asn Arg Glu Lys Phe Leu Ala Asp Val Val 35 40 45 Glu Gly Gly Thr Pro Pro Glu Val Ala Asp Glu Ser Val Asp Arg Arg 50 55 60 Gly Thr Thr Leu Val Gin Pro Val Thr Thr Arg Ser Val Glu Glu Ala 65 70 75 80 Gin Arg Gly Asn Thr Gly Thr Thr He Glu Asp Asp Tyr Leu Gly His 85 90 95 Glu Ala Leu Gin Ala Tyr Ser Pro Val Asp Leu Pro Gly Leu His Trp 100 105 110 Val He Val Ala Lys He Asp Thr Asp Glu Ala Phe Ala Pro Val Ala 115 120 125 Gin Pne Thr Arg Thr Leu Val Leu Ser Thr Val He He He Phe Gly Gly His Pro (2) INFORMATION FOR SEQ ID NO: 126: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid {£ 1 STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: Other ( i) SEQUENCE DESCRIPTION: SEQ ID NO: 126: CCGGATCCGA TGAGCAGCGT GCTGAAC 27 (2) INFORMATION FOR SEQ ID NO: 127: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 127: GCGGATCCCA CGGCCCCGAT CACGTG 6 (2) INFORMATION FOR SEQ ID NO: 128- (l) SEQUENCE CHARACTERISTICS: (A) LENGTH. 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION SEQ ID NO: 128: CCGGATCCAA TGACATTTCT GCCCTGGAAT GCG 3 (2) INFORMATION FOR SEQ ID NO: 129: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (n) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 129: CCGGA1CCAT TCGGTGGCCC TGCAACCGCC AG 2 (2) INFORMATION FOR SEQ ID NO: 130: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (a) MOLECULE TYPE: Other (x ..SEQUENCE DESCRIPTION: SEQ ID NO: 130: CCGGATCCGG AGCAACCGTT CCGGCTC 7 (2) INFORMATION FOR SEQ ID NO: 131: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Other (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 131: CCGGATCCCG GCTATCAGTC CGGACGG 7 (2) INFORMATION FOR SEQ ID NO: 132: (1) SEQUENCE CHARACTERISTICS: (A) LENGTH: 844 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ 10 NO: 132: GAGCAACCGT TCCGGCTCGG CGACTGGATC ACCGTCCCCA CCGCGGCGGG CCGGCCGTCC 60 GCCCACGGCC GCGTGGTGGA AGTCAACTGG CGTGCΛACAC ATATCGACAC CGGCGGCAAC 120 CTGCTGGTAA TGCCCAACGC CGAACTCGCC GGCGCGTCGT TCACCAATTA CAGCCGGCCC 180 GTGGGAGAGC ACCGGCTGAC CGTCGTCACC ACCTTCAACG CCGCGGACAC CCCCGATGAT 240 GTCTGCGAGA TGCTGTCGTC GGTCGCGGCG TCGCTGCCCG AACTGCGCAC CGACGGACAG 300 ATCGCCACGC TCTATCTCGG TGCGGCCGAA TACGAGAAGT CGATCCCGTT GCACACACCC 360 GCGGTGGACG ACTCGGTCAG GAGCACGTAC CTGCGATGGG TCTGGTACGC CGCGCGCCGG 420 CAGGAACTTC GCCTAACGGC GTCGCCGACG ATTCGACACG CCGGAACGGA TCGCCTCGGC 480 CATGCGGGCT GTGGCGTCCA CACTGCGCTT GGCAGACGAC GAACAGCAGG AGATCGCCGA 540 CGTGGTGCGT CTGGTCCGTT ACGGCAACGG GGAACGCCTC CAGCAGCCGG GTCAGGTACC 600 GACCGGGATG AGGTTCATCG TAGACGGCAG GGTGAGTCTG TCCGTGATCG ATCAGGACGG 660 CGACGTGATC CCGGCGCGGG TGCTCGAGCG TGGCGACTTC CTGGGGCAGA CCACGCTGAC 720 GCGGGAACCG GTACTGGCGA CCGCGCACGC GCTGGAGGAA GTCACCGTGC TGGAGATGGC 780 CCGTGACGAG ATCGAGCGCC TGGTGCACCG AAAGCCGATC CTGCTGCACG TGATCGGGGC 840 CGTG 844 (2) INFORMATION FOR SEQ ID NO: 133: (i)...SEQUENCE CHARACTERISTICS: (A) LENGTH: 742 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 133: GGCTATCAGT CCGGACGGTC CTCGCTGCGC GCATCGGTGT TCGACCGCCT CACCGACATC 60 CGCGAGTCGC AGTCGCGCGG GTTGGAGAAT CAGTTCGCGG ACCTGAAGAA CTCGATGGTG 120 ATTTACTCGC GCGGCAGCAC TGCCACGGAG GCGATCGGCG CGTTCAGCGA CGGTTTCCGT 180 CAGCTCGGCG ATGCGACGAT CAATACCGGG CAGGCGGCGT CATTGCGCCG TTACTACGAC 240 CGGACGTTCG CCAACACCAC CCTCGACGAC AGCGGAAACC GCGTCGACGT CCGCGCGCTC 300 ATCCCGAAAT CCAACCCCCA GCGCTATCTG CAGGCGCTCT ATACCCCGCC GTTTCAGAAC 360 TGGGAGAAGG CGATCGCGTT CGACGACGCG CGCGACGGCA GCGCCTGGTC GGCCGCCAAT 420 GCCAGATTCA ACGAGTTCTT CCGCGAGATC GTGCACCGCT TCAACTTCGA GGATCTGATG 480 CTGCTCGACC TCGAGGGCAA CGTGGTGTAC TCCGCCTACA AGGGGCCGGA TCTCGGGACA 540 AACATCGTCA ACGGCCCCTΛ TCGCAACCGG GAACTGTCGG AAGCCTACGA GAAGGCGGTC 600 GCGTCGAACT CGATCGACTA TGTCGGTGTC ACCGACTTCG CGTGGTACCT GCCTGCCGAG 660 GAACCGACCG CCTGGTTCCT GTCCCCGGTC GGGTTGAAGG ΛCCGAGTCGA CGGTGTGATG 720 GCGGTCCAGT TCCCCGGAAT TC 742 (2) INFORMATION FOR SEQ ID NO: 134: (1) SEQUENCE CHARACTERISTICS: (A) LENGTH: 282 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 134: Glu Gin Pro Phe Arg Leu Gly Asp Trp He Thr Val Pro Thr Ala Ala 1 5 10 15 Gly Arg Pro Ser Ala His Gly Arg Val Val Glu Val Asn Trp Arg Ala 20 25 30 Thr His He Asp Thr Gly Gly Asn Leu Leu Val Met Pro Asn Ala Glu 35 40 45 Leu Ala Gly Ala Ser Phe Thr Asn Tyr Ser Arg Pro Val Gly Glu His 50 55 60 Arg Leu Thr Val Val Thr Thr Phe Asn Ala Ala Asp Thr Pro Asp Asp 65 70 75 80 Val Cys Glu Met Leu Ser Ser Val Ala Ala Ser Leu Pro Glu Leu Arg 85 90 95 Thr Asp Gly Gin He Ala Thr Leu Tyr Leu Gly Ala Ala Glu Tyr Glu 100 105 110 Lys Ser He Pro Leu His Thr Pro Ala Val Asp Asp Ser Val Arg Ser 115 120 125 Thr Tyr Leu Arg Trp Val Trp Tyr Ala Ala Arg Arg Gin Glu Leu Arg 130 135 140 Xaa Asn Gly Val Ala Asp Xaa Phe Asp Thr Pro Glu Arg He Ala Ser 145 150 155 160 Ala Met Arg Ala Val Ala Ser Thr Leu Arg Leu Ala Asp Asp Glu Gin 165 170 175 Gin Glu He Ala Asp Val Val Arg Leu Val Arg Tyr Gly Asn Gly Glu 180 185 190 Arg Leu Gin Gin Pro Gly Gin Val Pro Thr Gly Met Arg Phe He Val 195 200 205 Asp Gly Arg Val Ser Leu Ser Val He Asp Gin Asp Gly Asp Val He 210 215 220 Pro Ala Arg Val Leu Glu Arg Gly Asp Phe Leu Gly Gin Thr Thr Leu 225 230 235 240 Thr Arg Glu Pro Val Leu Ala Thr Ala His Ala Leu Glu Glu Val Thr 245 250 255 Val Leu Glu Met Ala Arg Asp Glu He Glu Arg Leu Val His Arg Lys 260 265 270 Pro He Leu Leu His Val He Gly Ala Val 275 280 (2) INFORMATION FOR SEQ ID NO: 135: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 247 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 135: Gly Tyr Gin Ser Gly Arg Ser Ser Leu Arg Ala Ser Val Phe Asp Arg 1 5 10 15 Leu Thr Asp He Arg Glu Ser Gin Ser Arg Gly Leu Glu Asn Gin Phe 20 25 30 Ala Asp Leu Lys Asn Ser Met Val He Tyr Ser Arg Gly Ser Thr Ala 35 40 45 Tnr Glu Ala He Gly Ala Phe Ser Asp Gly Phe Arg Gin Leu Gly Asp 50 55 60 Ala Thr He Asn Thr Gly Gin Ala Ala Ser Leu Arg Arg Tyr Tyr Asp 65 70 75 80 Arg Thr Phe Ala Asn Thr Thr Leu Asp Asp Ser Gly Asn Arg Val Asp 85 90 95 Val Arg Ala Leu He Pro Lys Ser Asn Pro Gin Arg Tyr Leu Gin Ala 100 105 110 Leu Tyr Thr Pro Pro Phe Gin Asn Trp Glu Lys Ala He Ala Phe Asp 115 120 125 Asp Ala Arg Asp Gly Ser Ala Trp Ser Ala Ala Asn Ala Arg Phe Asn 130 135 140 Glu Phe Phe Arg Glu He Val His Arg Phe Asn Phe Glu Asp Leu Met 145 150 155 160 Leu Leu Asp Leu Glu Gly Asn Val Val Tyr Ser Ala Tyr Lys Gly Pro 165 170 175 Asp Leu Gly Thr Asn He Val Asn Gly Pro Tyr Arg Asn Arg Glu Leu 180 185 190 Ser Glu Ala Tyr Glu Lys Ala Val Ala Ser Asn Ser He Asp Tyr Val 195 200 205 Gly Val Thr Asp Phe Gly Trp Tyr Leu Pro Ala Glu Glu Pro Thr Ala 210 215 220 Trp Phe Leu Ser Pro Val Gly Leu Lys Asp Arg Val Asp Gly Val Met 225 230 235 240 Ala Val Gin Phe Pro Gly He 245 (2) INFORMATION FOR SEQ ID NO: 136: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 45 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 136: ATGAGCGAAA TCGCCCGNCC CTGGCGGGTT CTGGCATGTG GCATC 45 (2) INFORMATION FOR SEQ ID NO: 137: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 340 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (i ) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 137: GCCACCGGCG GCGCCGCCGC GGTGCCCGCC GGGGTGAGCG CCCCGGCGGT CGCGCCGGCC 60 CCCGCGATGC CCGCCCGCCC GGTGTCCACG ATCGCGCCGG CGACCTCGGG CACGCTCAGC 120 GAGTTTTTCG CCGCCAAGGG CGTCACGATG GAGCCGCAGT CCAGCCGCGA CTTCCGCGCC 180 CTCAACATCG TGCTGCCGAA GCCGCGGGGC TGGGAGCACA TCCCGGACCC GAACGTGCCG 240 GACGCGTTCG CGGTGCTGGC CGACCGGGTC AGNGGTAAAG GTCAGNAGTC GACAAACGCC 300 CACGTGGTGG TCGACAAACA CGTAGGCGAG TTCGACGGCA 340 (2) INFORMATION FOR SEQ ID NO: 138: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 235 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: Genomic DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 138: GGTGACCACC AGCGTNGAAC AGGTCGTTGC CGAAGCCGCG GAGGCCACCG ACGCGATTGT 60 CAACGGCTTC AAGGTCAGCG TTCCGGGTCC GGGTCCGGCC GCACCGCCAC CTGCACCCGG 120 TGCCCCCGGT GTCCCGCCCG CCCCCGGCGC CCCGGCGCTG CCGCTGGCCG TCGCACCACC 180 CCCGGCTCCC GCTGTTCCCG CCGTGGCGCC CGCGCCACAG CTGCTGGGAC TGCAG 235 (2) INFORMATION FOR SEQ ID NO: 139: (i) SEQUENCE CHARACTERISTICS: (A). LENGTH: 15 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 139: Met Ser Glu He Ala Arg Pro Trp Arg Val Leu Ala Cys Gly He 1 5 10 15 (2) INFORMATION FOR SEQ ID NO: 140: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 113 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 140 : Ala Thr Glv Glv Ala Ala Ala Val Pro Ala Gly Val Ser Ala Pro Ala 1 5 10 15 Val Ala Pro Ala Pro Ala Met Pro Ala Arq Pro Val Ser Thr He Ala 20 25 30 Pro Ala Thr Ser Gly Thr Leu Ser Glu Phe Phe Ala Ala Lys Gly Val 35 40 45 Thr Met Glu Pro Gin Ser Ser Arg Asp Phe Arg Ala Leu Asn He Val 50 55 60 Leu Pro Lys Pro Arg Gly Trp Glu His He Pro Asp Pro Asn Val Pro 65 70 75 80 Asp Ala Phe Ala Val Leu Ala Asp Arg Val Gly Gly Lys Gly Gin Xaa 85 90 95 Ser Thr Asn Ala His Val Val Val Asp Lys His Val Gly Glu Phe Asp 100 105 110 Gly (2) INFORMATION FOR SEQ ID NO : 1 1 : (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: am o acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 141: Val Thr Thr Ser Val Glu Gin Val Val Ala Ala Ala Asp Ala Thr Glu 1 5 10 15 Ala He Val Asn Gly Phe Lys Val Ser Val Pro Gly Pro Gly Pro Ala 20 25 30 Ala Pro Pro Pro Ala Pro Gly Ala Pro Gly Val Pro Pro Ala Pro Gly 35 40 45 Ala Pro Ala Leu Pro Leu Ala Val Ala Pro Pro Pro Ala Pro Ala Val 50 55 60 Pro Ala Val Ala Pro Ala Pro Gin Leu 65 70

Claims: Claims 1. A poiypeptide comprising an immunogenic portion of a soluble M. vaccae antigen, or a variant thereof, wherein the antigen induces an immune response in patients previously exposed to a mycobacterium. 2. A poiypeptide comprising an immunogenic portion of an M. vaccae antigen, wherein the antigen includes a sequence selected from the group consisting of: (a) sequences recited in SEQ ID NOS: 1-4, 9-16, 18-21, 23, 25, 26, 28, 29. 44, 45, 47, 52-55, 63, 64, 70, 75, 89, 94, 98, 100-105, 109, 1 10. 1 12, 121 , 124, 125, 134, 135, 140 and 141 ; and (b) sequences having at least about a 99% probability of being the same as a sequence recited in SEQ ID NOS: 1 -4, 9-16, 18-21 , 23, 25. 26, 28, 29, 44, 45, 47, 52-55, 63, 64, 70, 75, 89, 94, 98, 100-105, 109, 1 10, 1 12, 121 , 124, 125, 134, 135, 140 and 141 as measured by computer algorithm BLASTP. 3. A poiypeptide comprising an immunogenic portion of an M. vaccae antigen, wherein the antigen comprises an amino acid sequence encoded by a DNA molecule selected from the group consisting of: (a) -sequences recited in SEQ ID NOS: 40-42, 46, 48-51 , 74, 88, 93, 97, 99, 106-108, 1 1 1, 120, 122, 123, 132, 133 and 136-138; (b) complements of the sequences recited in SEQ ID NOS:40-42, 46, 48- 51 , 74, 88, 93, 97, 99, 106-108, 1 1 1 , 120, 122, 123, 132, 133 and 136- 138; and (c) sequences having at least about a 99% probability of being the same as a sequence of (a) or (b) as measured by computer algorithm FASTA. 4. A DNA molecule comprising a nucleotide sequence encoding a poiypeptide according to any one of claims 1-3. 5. An expression vector comprising a DNA molecule according to claim 4. 6. A host cell transformed with an expression vector according to claim 5. 7. The host cell of claim 6, wherein the host cell is selected from the group consisting of E. coli, mycobacteria, insect, yeast and mammalian cells. 8. A fusion protein comprising two or more polypeptides according to any one of claims 1-3. 9. A pharmaceutical composition comprising one or more polypeptides according to any one of claims 1-3, and a physiologically acceptable carrier. 10. A pharmaceutical composition comprising a DNA molecule according to claim 4 and a physiologically acceptable carrier. 1 1. A pharmaceutical composition comprising one or more components secreted by M. vaccae cells in culture and a physiological acceptable carrier. 12. A pharmaceutical composition comprising a fusion protein according to claim 8 a»d-a physiologically acceptable carrier. 13. A vaccine comprising one or more polypeptides according to any one of claims 1-3, and a non-specific immune response amplifier. 14. A vaccine comprising a DNA molecule according to claim 4 and a non-specific immune response amplifier. 15. A vaccine comprising one or more components secreted by M. vaccae cells in culture and a non-specific immune response amplifier. 16. A vaccine comprising a fusion protein according to claim 8 and a non ¬ specific immune response amplifier. 17. A vaccine according to any one of claims 13-16 wherein the nonspecific immune response amplifier is an adjuvant. 18. A vaccine according to any one of claims 13-16 wherein the nonspecific immune response amplifier comprises delipidated M. vaccae cells. 19. A vaccine according to any one of claims 13-16 wherein the nonspecific immune response amplifier comprises culture filtrate from M. vaccae. 20. A method for inducing protective immunity in a patient, comprising administering to a patient a pharmaceutical composition according to any one of claims 9-12. 21. A method for inducing protective immunity in a patient, comprising administering to a patient a vaccine according to any one of claims 13-19. 22. A method for detecting mycobacterial infection in a patient, comprising: (a) — -contacting dermal cells of a patient with one or more polypeptides according to any one of claims 1 -3; and (b) detecting an immune response on the patient's skin. 23. The method of claim 22 wherein the immune response is induration. 24. A diagnostic kit comprising: (a) a poiypeptide according to any one of claims 1-3; and (b) apparatus sufficient to contact the poiypeptide with the dermal cells of a patient. 25. A method for detecting mycobacterial infection in a biological sample, comprising: (a) contacting the biological sample with one or more polypeptides according to any one of claims 1 -3; and (b) detecting in the sample the presence of antibodies that bind to at least one of the polypeptides. 26. The method of claim 25 wherein step (a) additionally comprises contacting the biological sample with a 38 kD M tuberculosis antigen and step (b) additionally comprises detecting in the sample the presence of antibodies that bind to the 38 kD M. tuberculosis antigen. 27. The method of claim 25 wherein the polypeptide(s) are bound to a solid support. 28. The method of claim 25 wherein the biological sample is selected from the group consisting of whole blood, serum, plasma, saliva, cerebrospinal fluid and urine. 29. A method for detecting mycobacterial infection in a biological sample, comprising: (a) contacting the biological sample with a binding agent which is capable of binding to a poiypeptide according to any one of claims 1 -3 ; and (b) detecting in the sample a protein or poiypeptide that binds to the binding agent. 30. The method of claim 29 wherein the binding agent is a monoclonal antibody. 31. The method of claim 29 wherein the binding agent is a polyclonal antibody. 32. A diagnostic kit comprising: (a) at least one poiypeptide according to any one of claims 1 -3; and (b) a detection reagent. 33. The kit of claim 32 wherein the poiypeptide is immobilized on a solid support. 34. The kit of claim 32 wherein the detection reagent comprises a reporter group conjugated to a binding agent. 35. The kit of claim 34 wherein the binding agent is selected from the group consisting of anti-immunoglobulins, Protein G, Protein A and lectins. 36. The kit of claim 34 wherein the reporter group is selected from the group consisting of radioisotopes, fluorescent groups, luminescent groups, enzymes, biotin and dye particles. 37. A monoclonal antibody that binds to a poiypeptide according to any one of claims 1-3. 38. A polyclonal antibody that binds to a poiypeptide according to any one of claims 1-3-, 39. A method for enhancing a non-specific immune response to an antigen comprising administering a component selected from the group consisting of: (a) delipidated M. vaccae cells; (b) deglycosylated M. vaccae cells; and (c) delipidated and deglycosylated M. vaccae cells 40. A method for enhancing a non-specific immune response to an antigen comprising administering culture filtrate from M. vaccae cells. 41. A composition comprising a component selected from the group consisting of: (a) delipidated M. vaccae cells; (b) deglycosylated M. vaccae cells; and (c) delipidated and deglycosylated M. vaccae cells. 42. A method for inducing protective immunity in a patient comprising administering a composition according to claim 41. 43. A vaccine comprising a non-specific immune response amplifier and a component selected from the group consisting of: (a) delipidated M. vaccae cells; (b) deglycosylated M. vaccae cells; and (c) delipidated and deglycosylated M. vaccae cells. 44. A method for inducing protective immunity in a patient, comprising administering to a patient a vaccine according to claim 43. 45. A method for enhancing a non-specific immune response to an antigen comprising administering a poiypeptide, the poiypeptide comprising an immunogenic portion of an antigen, wherein the antigen includes a sequence selected from the group consisting of: (a) sequences recited in SEQ ID NO: 1 14, 1 17 and 1 18; and (b) sequences having at least about 97% identity to a sequence recited in SEQ ID NO: 1 14, 1 17 and 118. 46. A vaccine comprising a poiypeptide, the poiypeptide comprising an immunogenic portion of an antigen, wherein the antigen includes a sequence selected from the group consisting of: (a) sequences recited in SEQ ID NOS: 1 14, 1 17 and 1 18; and (b) sequences having at least about 97% identity to a sequence of SEQ ID NOS: 1 14, 117 and 1 18. 47. An immunologically reactive fragment of an M. vaccae antigen consisting essentially of an amino acid sequence selected from the group consisting of: (a) sequences recited in SEQ ID NOS: 1 14 and 1 18; and (b) sequences having at least about 97% identity to a sequence recited in SEQ ID NOS: 1 14 and 1 18. 48. A method for enhancing protective immunity against a mycobacterial infection comprising administering a poiypeptide, the poiypeptide comprising an immunogenic portion of an antigen, wherein the antigen includes a sequence selected from the group consisting of: (a) sequences recited in SEQ ID NO: 1 14, 1 17 and 1 18; and (b) sequences having at least about 97% identity to a sequence recited in SEQ ID NO: 1 14, 1 17 and 1 18. 49. A poiypeptide comprising an immunogenic portion of an M. vaccae antigen, wherein the antigen includes a sequence selected from the group consisting of: (a) sequences recited in SEQ ID NO: 1 14, 1 17 and 1 18; and (b) sequences having at least about 97% identity to a sequence recited in SEQ ID NO: 1 14, 1 17 and 1 18.

Inventors: HIYAMA JUN, PRESTIDGE ROSS L, SCOTT LINDA M, SKINNER MARGOT A, TAN PAUL, VISSER ELIZABETH S, HIYAMA, JUN, PRESTIDGE, ROSS, L., SCOTT, LINDA, M., SKINNER, MARGOT, A., TAN, PAUL, VISSER, ELIZABETH, S.
Applicants: GENESIS RES & DEV CORP LTD, GENESIS RESEARCH & DEVELOPMENT CORPORATION LIMITED
Application year: 1997
Main classification: A61K39
IPC codes: A61K31, A61K35, A61K38, A61K39, A61K48, A61P31, C07K14, C07K16, C12N1, C12N5, C12N15, C12P21, C12Q1, G01N33