METHOD OF PROTECTING CROP PLANTS AGAINST INSECT PESTS

Abstract: The present invention provides a method of controlling Sesamia species in crop plants, but especially in maize and other cereal plants, including, but not limited to, Sesamia nonagrioides, S inferens, S calamistis, S cretica, etc. comprising applying a toxin protein of Bacillus thuringiensis to the crop plant to be protected. The toxin being preferably CryIA(b) a vegetative insecticidal protein (VIP), or a mixture thereof.

Description: METHOD OF PROTECTING CROP PUNTS AGAINST INSECT PESTS The present invention relates to a method of controlling Sesamia species in crop plants by use of toxin proteins obtainable from Bacillus thuringiensis and/or other Bacillus species. Bacillus thuringiensis belongs to the large group of gram-positive, aerobic, endospore-forming bacteria. Unlike other very closely related species of Bacillus such as B. cereus or B. anthracis, the majority of the hitherto known Bacillus thuringiensis species produce in the course of their sporulation a parasporal inclusion body which, due to its crystalline structure, is generally referred to also as a crystalline body. This crystalline body is composed of insecticidally active crystalline protoxin proteins, the so-called δ-endotoxins. These protein crystals are responsible for the toxicity to insects of Bacillus thuringiensis. Th e δ-endotoxin does not exhibit its insecticidal activity until after oral ingestion of the crystalline body, when the latter is dissolved in the intestinal juice of the target insects. In most cases the actual toxic component is released from the protoxin as a result of proteolytic cleavage caused by the action of proteases from the digestive tract of the insects. The δ-endotoxins of the various Bacillus thuringiensis strains are characterized by high specificity toward certain target insects, especially with respect to various Lepidoptera, Coleoptera and Diptera larvae, and by a high degree of activity against such succeptible larvae. A further advantage in using δ-endotoxins of Bacillus thuringiensis resides in the fact that the toxins are harmless to humans, other mammals, birds and fish. The various insecticidal crystal proteins from Bacillus thuringiensis have been classified based upon their spectrum of activity and sequence similarity. The classification put forth by Hόfte and Whiteley, Microbiol. Rev. 53: 242-255 (1989) placed the then known insecticidal crystal proteins into four major classes. Generally, the major classes are defined by their spectrum of activity, with the Cryl proteins active against Lepidoptera, Cryll proteins active against both Lepidoptera and Diptera, Crylll proteins beeing active against Coleoptera, and CrylV proteins against Diptera. Within each major class, the δ-endotoxins are grouped according to sequence similarity. The Cryl proteins are typically produced as 130-140 kDa protoxin proteins which are proteolytically cleaved to produce insecticidally active toxin proteins about 60-70 kDa in size. The active portion of the δ-endotoxin resides in the NH 2 -terminal portion of the full- length molecule. Hόfte and Whiteley, supra, classified the then known Cryl proteins into six groups, IA(a), IA(b), IA(c), IB, IC, and ID. Since then, proteins classified as CrylE, CrylF, CrylG, CrylH and CrylX have also been characterized. The spectrum of insecticidal activity of an individual δ-endotoxin from Bacillus thuringiensis tends to be quite narrow, with a given δ-endotoxin being active against only a few insects. Specificity is the result of the efficiency of the various steps involved in producing an active toxin protein and its subsequent ability to interact with the epithelial cells in the insect digestive tract. Up to now no such activity is reported for species of the lepidopteran genus Sesamia, which cause considerable damage in cereal crops, especially in the southern hemisphere including the mediterranean area. The yield losses caused by Sesamia species in maize are in a range of between 5% to 10%, but can reach up to 40% in severe cases. To the contrary, it was believed in the art that Bt toxins such as the Cryl-type toxins mentioned above are not active against Sesamia species and can not be suitably used for controlling Seamia pests in crop plants. It is therefore one of the objects of this invention to provide a method of controlling Sesamia species in crop plants, but preferably in maize and other cereal plants, including, but not limited to, Sesamia nonagrioides, S inferens, S calamistis, S cretica, etc. This object could surprisingly be achieved within the scope of the invention by applying a δ-endotoxin protein of Bacillus thuringiensis, but especially a Cryl-type toxin protein, to the crop plant to be protected. Another class of toxin proteins obtainable from vegetative cultures of Bacillus species, the so-called VIPs including VIP1 , VIP2 and VIP3 [EP-A 0 690 916; International Application no EP95/03826, the disclosure of which is incorporated herein by reference in its entirety], can also be used in a method according to the invention for controlling Sesamia pests. The present invention thus relates to a method for protecting plants against damage caused by Sesamia species comprising directly or indirectly administering to the plant or the plant seed or the growing area to be protected a toxin protein of Bacillus spp, preferably a Cryl-type and/or a VIP-type protein mentioned above, either purely or in form of an ento- mocidal composition comprising at least one of the said proteins or a microorganism, but especially a Bacillus thuringiensis and/or a Bacillus cereus strain, containing at least one toxin gene encoding the said toxin proteins. Said microorganisms used in a method according to the invention may either be naturally occurring strains or, in the alternative, a recombinant strain comprising the toxin encoding DNA in recombinant form. In a further embodiment, a transgenic plant according to the invention may be used in a method of protecting plants against damage caused by Sesamia species comprising transforming the said plant with a toxin gene encoding a toxin protein from a Bacillus species, but especially a Cryl-type toxin protein and/or a VIP-type protein, and expressing the said toxin protein in an amount sufficient to provide control against Sesamia species upon planting the so transformed plant within an area where the said insect pest may occur. CrylA type genes are known from various Bacillus thuringiensis species including, but not limited to, Bt kurstaki D [cry IA(a); Schnepf et a/ (1985) J Biol Chem 260, 6264-6272], Bt subsp berliner[cry IA(b); Wabiko et al (1986) DNA 5, 305-314; Hδfte et al (1986) Eur J Biochem 161 , 273-280], Bt subsp kurstaki HD-73 [cry IA(c); Adang et al (1985) Gene 36, 289-300], Bt D2 [cry IB; Brizzard et al (1988) Nucl Acids Res 16, 2723-2724], Bt subsp entomocidus [crylC; Honee et a/ (1988) Nucl Acids Res 16, 6240], Bt subsp aizawai [cry IC, crylD; crylF; crylX; Sanchis ef a/ (1988), EP-A O 295 156; Gawron-Burke et al (1991 ), WO 91/16434], Bt subsp darmstadiensis [cry IE; Hofte and Whiteley (1989), EP-A 0 358 557], and Bt subsp kenyae [crylE; Visser et al (1990) J Bacteriol 172, 6783-6788; Kramer et al (1995, WO 95/34656]. Further cryl-type genes are disclosed in European Application 0 367 474, 0401 979 and in PCT International Application WO 90/13651. Preferred for use within the scope of the present invention are the expression products of crylA-type genes, but especially of crylA(b) type genes such as those derived from Bacillus thuringiensis var kurstaki or of synthetic variants thereof. Especially preferred are the crylA(b) type genes shown in SEQ ID NOS: 53 to 55. The entomocidal compositions to be used in the method according to the invention for protecting crop plants against Sesamia pests preferably comprise as an active ingredient at least one toxin protein from Bacillus thuringiensis preferably one Cryl-type toxin protein of Bacillus thuringiensis or a microorganism containing at least one gene encoding the said toxin protein, but especially a Bacillus thuringiensis strain containing at least one gene encoding the said toxin protein, or a derivative or mutant thereof, together with an agricultural adjuvant such as a carrier, diluent, surfactant or application-promoting adjuvant. The active ingredient contained in the entomocidal composition may also be a VIP-type toxin protein as disclosed in the European Application EP-A 0 690 91 6 and the PCT International Application no EP95/03826 or a microorganism containing at least one gene encoding the said VIP-type toxin protein or a combination of Cryl-type and VIP-type proteins either in an essentially pure form or as part of a microorganism . Preferred within the scope of protection are VIP-type toxin proteins as shown in SEQ ID NOS: 1 , 2, 4-7, 17-24, 26-32, 35, 36, 39, 40, 42, 43, 45, 46, 49, 50, 51 or 52. The composition may also contain a further biologically active compound. The said compound can be both a fertilizer or micronutrient donor or other preparations that influence plant growth. It can also be a selective herbicide, insecticide, fungicide, bactericide, nematicide, molluscide or mixtures of several of these preparations, if desired, together with further agriculturally acceptable carriers, surfactants or application-promoting adjuvants customarily employed in the art of formulation. Suitable carriers and adjuvants can be solid or liquid and correspond to the substances ordinarily employed in formulation technology, e.g. natural or regenerated mineral substances, solvents, dispersants, wetting agents, tackifiers, binders or fertilizers The composition may comprise from 0.1 to 99% by weight of the active ingredient, from 1 to 99.9% by weight of a solid or liquid adjuvant, and from 0 to 25% by weight of a surfactant. The active ingredient or the composition containing the said active ingredient, may be administered to the plants or crops to be protected together with certain other insecticides or chemicals (1993 Crop Protection Chemicals Reference, Chemical and Pharmaceutical Press, Canada) without loss of potency. It is compatible with most other commonly used agricultural spray materials but should not be used in extremely alkaline spray solutions if a Cryl-type toxin is involved. It may be administered as a dust, a suspension, a wettable powder or in any other material form suitable for agricultural application. The active ingredient, that is preferably a Cryl-type toxin protein of Bacillus thuringiensis and or one of the VIP-type proteins mentioned previously, or the composition comprising the said active ingredient may be applied to (a) an environment in which the insect pest may occur, (b) a plant or plant part in order to protect said plant or plant part from damage caused by an insect pest, or (c) seed in order to protect a plant which develops from said seed from damage caused by an insect pest. A preferred method of application in the area of plant protection is application to the foliage of the plants (foliar application), with the number of applications and the rate of application depending on the plant to be protected and the risk of infestation by the pest in question. However, the active ingredient may also penetrate the plants through the roots (systemic action) if the locus of the plants is impregnated with a liquid formulation or if the active ingredient is incorporated in solid form into the locus of the plants, for example into the soil, e.g. in granular form (soil application). In paddy rice crops, such granules may be applied in metered amounts to the flooded rice field. The compositions to be used in a method according to the invention are also suitable for protecting plant propagating material, e.g. seed, such as fruit, tubers or grains, or plant cuttings, from insect pests. The propagation material can be treated with the formulation before planting: seed, for example, can be dressed before being sown. The active ingredient of the invention can also be applied to grains (coating), either by impregnating the grains with a liquid formulation or by coating them with a solid formulation. The formulation can also be applied to the planting site when the propagating material is being planted, for example to the seed furrow during sowing. The invention relates also to those methods of treating plant propagation material and to the plant propagation material thus treated. Within the scope of the invention the compositions may be applied in any method known for treatment of seed or soil with bacterial strains. For example, see US Patent No.4,863,866. The strains are effective for biocontrol even if the microorganism is not living. Preferred is, however, the application of the living microorganism. Target crops to be protected within the scope of the present invention are those that are host plants for Sesamia species including, but not limited to, the following species of plants: maize, wheat, barley, rye, oats, rice, sorghum, millet and related crops, forage grasses (orchardgrass, fescue, and the like), and sugar cane. The active ingredient according to the invention may be used in unmodified form or together with any suitable agriculturally acceptable carrier. Such carriers are adjuvants conventionally employed in the art of agricultural formulation, and are therefore formulated in known manner to emulsifiable concentrates, coatable pastes, directly sprayable or dilutable solutions, dilute emulsions, wettable powders, soluble powders, dusts, granulates, and also encapsulations, for example, in polymer substances. Like the nature of the compositions, the methods of application, such as spraying, atomizing, dusting, scattering or pouring, are chosen in accordance with the intended objective and the prevailing circumstances. Advantageous rates of application are normally from about 50 g to about 5 kg of active ingredient (a.i.) per hectare ("ha", approximately 2.471 acres), preferably from about 100 g to about 2kg a.iJha. Important rates of application are about 200 g to about 1kg a.i./ha and 200g to 500g a.i./ha. For seed dressing advantageous application rates are 0.5 g to 1000 g a.i.per 100 kg seed, preferably 3 g to 100 g a.i. per 100 kg seed or 10 g to 50 g a.i.per 100 kg seed. Suitable carriers and adjuvants can be solid or liquid and correspond to the substances ordinarily employed in formulation technology, e.g. natural or regenerated mineral substances, solvents, dispersants, wetting agents, tackifiers, binders or fertilizers. The formulations, i.e. the entomocidal compositions, preparations or mixtures thereof with other active ingredients, and, where appropriate, a solid or liquid adjuvant, are prepared in known manner, e.g., by homogeneously mixing and/or grinding the active ingredients with extenders, e.g., solvents, solid carriers, and in some cases surface-active compounds (surfactants). Suitable solvents are: aromatic hydrocarbons, preferably the fractions containing 8 to 12 carbon atoms, e.g. xylene mixtures or substituted naphthalenes, phthalates such as dibutyl phthalate or dioctyl phthalate, aliphatic hydrocarbons such as cyclohexane or paraffins, alcohols and glycols and their ethers and esters, such as ethanol, ethylene glycol monomethyl or monoethyl ether, ketones such as cyclohexanone, strongly polar solvents such as N-methyl-2-pyrrolidone, dimethylsulfoxide or dimethyiformamide, as well as vegetable oils or epoxidised vegetable oils such as epoxidised coconut oil or soybean oil; or water. The solid carriers used, e.g., for dusts and dispersible powders, are normally natural mineral fillers such as calcite, talcum, kaolin, montmorillonite or attapulgite. In order to improve the physical properties it is also possible to add highly dispersed silicic acid or highly dispersed absorbent polymers. Suitable granulated adsorptive carriers are porous types, for example pumice, broken brick, sepiolite or bentonite; and suitable nonsorbent carriers are materials such as calcite or sand. In addition, a great number of pregranulated materials of inorganic or organic nature can be used, e.g. especially dolomite or pulverized plant residues. Depending on the nature of the active ingredients to be formulated, suitable surface- active compounds are non-ionic, cationic and/or anionic surfactants having good emulsifying, dispersing and wetting properties. The term "surfactants" will also be understood as comprising mixtures of surfactants. Suitable anionic surfactants can be both water-soluble soaps and water-soluble synthetic surface-active compounds. Suitable soaps are the alkali metal salts, alkaline earth metal salts or unsubstituted or substituted ammonium salts of higher fatty acids (C sub 10 -C sub 22), e.g. the sodium or potassium salts of oleic or stearic acid, or of natural fatty acid mixtures which can be obtained, e.g. from coconut oil or tallow oil. Further suitable surfactants are also the fatty acid methyltaurin salts as well as modified and unmodified phospholipids. More frequently, however, so-called synthetic surfactants are used, especially fatty sulfonates, fatty sulfates, sulfonated benzimidazole derivatives or alkylarylsulfonates. The fatty sulfonates or sulfates are usually in the forms of alkali metal salts, alkaline earth metal salts or unsubstituted or substituted ammonium salts and generally contain a C sub 8 -C sub 22 alkyl radical which also includes the alkyl moiety of acyl radicals, e.g. the sodium or calcium salt of lignosulfonic acid, of dodecylsulfate, or of a mixture of fatty alcohol sulfates obtained from natural fatty acids. These compounds also comprise the salts of sulfuric acid esters and sulfonic acids of fatty alcohol/ethylene oxide adducts. The sulfonated benzimidazole derivatives preferably contain 2 sulfonic acid groups and one fatty acid radical containing about 8 to 22 carbon atoms. Examples of alkylarylsulfonates are the sod i u m , cal ci u m o r triethanolamin e salts of dodecylbenzenesulfonic acid, dibutylnaphthalenesulfonic acid, or of a naphthalenesulfonic acid/formaldehyde condensation product. Also suitable are corresponding phosphates, e.g. salts of the phosphoric acid ester of an adduct of p-nonylphenol with 4 to 14 moles of ethylene oxide. Non-ionic surfactant are preferably polyglycol ether derivatives of aliphatic or cycloaliphatic alcohols, or saturated or unsaturated fatty acids and alkylphenols, said derivatives containing 3 to 30 glycol ether groups and 8 to 20 carbon atoms in the (aliphatic) hydrocarbon moiety and 6 to 18 carbon atoms in the alkyl moiety of the alkylphenols. Further suitable non-ionic surfactants are the water-soluble adducts of polyethylene oxide with polypropylene glycol, ethylenediaminopolypropylene glycol and alkylpolypropylene glycol containing 1 to 10 carbon atoms in the alkyl chain, which adducts contain 20 to 250 ethylene glycol ether groups and 10 to 100 propylene glycol ether groups. These compounds usually contain 1 to 5 ethylene glycol units per propylene glycol unit. Representative examples of non-ionic surfactants are nonylphenolpolyethoxyethanols, casto r oi l po lyglyco l eth e rs , polypropylene/polyethyle ne oxid e adducts , tributylphenoxypolyethoxyethanol, polyethylene glycol and octylphenoxypolyethoxyethanol. Fatty acid esters of polyoxyethylene sorbitan, such as polyoxyethylene sorbitan trioleate, are also suitable non-ionic surfactants. Cationic surfactants are preferably quaternary ammonium salts which contain, as N- substituent, at least one C sub 8 -C sub 22 alkyl radical and, as further substituents, lower unsubstituted or halogenated alkyl, benzyl or hydroxyl-lower alkyl radicals. The salts are preferably in the form of halides, methylsulfates or ethylsulfates, e .g . , stearyltrimethylammonium chloride or benzyidi-(2-chloroethyl)ethylammonium bromide. The surfactants customarily employed in the art of formulation are described, e.g., in "McCutcheon's Detergents and Emulsifiers Annual", MC Publishing Corp. Ridgewood, N.J., 1979; Dr. Helmut Stache, "Tensid Taschenbuch" (Handbook of Surfactants), Carl Hanser Verlag, Munich/Vienna. Another particularly preferred characteristic of an entomocidal composition of the present invention is the persistence of the active ingredient when applied to plants and soil. Possible causes for loss of activity include inactivation by ultra-violet light, heat, leaf exudates and pH. For example, at high pH, particularly in the presence of reductant, δ- endotoxin crystals are solubilized and thus become more accessible to proteolytic inactivation. High leaf pH might also be important, particularly where the leaf surface can be in the range of pH 8-10. Formulation of an entomocidal composition to be used in a method according to the present invention can address these problems by either including additives to help prevent loss of the active ingredient or encapsulating the material in such a way that the active ingredient is protected from inactivation. Encapsulation can be accomplished chemically (McGuire and Shasha, J Econ Entomol 85: 1425-1433, 1992) or biologically (Barnes and Cummings, 1986; EP-A 0 192 319). Chemical encapsulation involves a process in which the active ingredient is coated with a polymer while biological encapsulation involves the expression of the δ-endotoxin genes in a microbe. For biological encapsulation, the intact microbe containing the toxin protein is used as the active ingredient in the formulation. The addition of UV protectants might effectively reduce irradiation damage. Inactivation due to heat could also be controlled by including an appropriate additive. Preferred within the present application are formulations comprising living microorganisms as an active ingredient either in form of the vegetative cell or more preferable in form of spores, if available. Suitable formulations may consist, for example, of polymer gels which are crosslinked with polyvalent cations and comprise these microorganisms. This is described, for example, by D.R. Fravel et al. in Phytopathology, Vol. 75, No. 7, 774-777, 1985 for alginate as the polymer material. It is also known from this publication that carrier materials can be co-used. These formulations are as a rule prepared by mixing solutions of naturally occurring or synthetic gel-forming polymers, for example alginates, and aqueous salt solutions of polyvalent metal ions such that individual droplets form, it being possible for the microorganisms to be suspended in one of the two or in both reaction solutions. Gel formation starts with the mixing in drop form. Subsequent drying of these gel particles is possible. This process is called ionotropic gelling. Depending on the degree of drying, compact and hard particles of polymers which are structurally crosslinked via polyvalent cations and comprise the microorganisms and a carrier present predominantly uniformly distributed are formed. The size of the particles can be up to 5 mm. Compositions based on partly crosslinked polysaccharides which, in addition to a microorganism, for example, can also comprise finely divided silicic acid as the carrier material, crosslinking taking place, for example, via Ca ++ ions, are described in EP-A1-0 097 571. The compositions have a water activity of not more than 0.3. W.J. Cornick et al. describe in a review article [New Directions in Biological Control: Alternatives for Suppressing Agricultural Pests and Diseases, pages 345-372, Alan R. Liss, Inc. (1990)] various formulation systems, granules with vermiculite as the carrier and compact alginate beads prepared by the ionotropic gelling process being mentioned. Such compositions are also disclosed by D.R.Fravel in Pesticide Formulations and Application Systems: 11th Volume, ASTM STP 1112 American Society for Testing and Materials, Philadelphia, 1992, pages 173 to 179 and can be used to formulate the recombinant microorganisms according to the invention. Further methods for formulating living microorganism are described in WO96/02638. The entomocidal compositions to be used in a method according to the invention usually contain from about 0.1 to about 99%, preferably about 0.1 to about 95%, and most preferably from about 3 to about 90% of the active ingredient, from about 1 to about 99.9%, preferably from about 1 to about 99%, and most preferably from about 5 to about 95% of a solid or liquid adjuvant, and from about 0 to about 25%, preferably about 0.1 to about 25%, and most preferably from about 0.1 to about 20% of a surfactant. Whereas commercial products are preferably formulated as concentrates, the end user will normally employ dilute formulations of substantially lower concentration. The entomocidal compositions may also contain further ingredients, such as stabilizers, antifoams, viscosity regulators, binders, tackifiers as well as fertilizers or other active ingredients in order to obtain special effects. It has surprisingly be found that a quantitatively variable combination of two active ingredients, on the one hand a Cry-type or δ-endotoxin protein and on the other hand a VIP- type protein, exhibits a synergistic action that is advantageously suitable for controlling Sesamia species in crop plants and which extends the limits of the action of both toxin proteins from two points of view: Firstly, the rates of application of the compound of the Cry-type toxin protein and of the VIP- type proteins are reduced while retaining an equally good action. Secondly, the combined mixture also achieves a high degree of pest control where both individual substances have become completely ineffective when unduly low rates are applied. This allows an increased safety upon use. The compositions according to the invention are valuable for preventive and/or curative treatment in the field of pest control even at low rates of application while being well tolerated by and non-toxic to warm-blooded species, fish and plants and have a very favourable biocidal spectrum. The compositions according to the invention are active against all or individual development stages of Sesamia pests. The insecticidal action of the compounds according to the invention can become obvious either directly, i.e. by destroying the pests immediately or only after some time has elapsed. Accordingly, the invention further relates to a insecticidal composition comprising as an active ingredient a Cry-type toxin protein and a VIP-type protein, preferably in a synergistically effective amount together with a agronomically acceptable carrier. Preferred is a composition comprising a combination of a Cryl-type protein and a VIP-type protein. A synergistic effect is always present when the action of the combination of the active ingredient of the Cry-type toxin protein with the VIP-type proteins exceeds the total of the action of the active ingredients applied individually. However, not only quantitative means are to be applied in assessing a synergistic activity, but also qualitative means such as, for example, a widening of the acitivity spectrum . The said composition can be provided in form of a chemical mixture comprising the toxin proteins in an essentially pure form or in form of a mixture comprising at least one of the toxin proteins as part of a microorganism or a transgenic plant. In a specific embodiment of the invention, one of the active ingredients may be applied to the plant directly by, for example, leaf application as described herein previously, whereas the second active principle may be provided by the plant itself upon expression of a previously transformed gene encoding the said second principle. A further object of the invention relates to the use of a recombinant microorganisms comprising a toxin gene encoding a toxin protein of Bacillus thuringiensis, but especially a Cryl-type protein, in a method of controlling crop plants against damages caused by Sesamia species, which recombinant organism can either be applied directly to the plant to be protected or the recombinantly produced toxin protein can first be isolated from the recombinant microorganism and formulated in the above described manner before being applied to the crop plant to be protected. The recombinant microorganism may also contain a toxin gene encoding a VIP-type toxin protein as disclosed in the European Application EP-A 0 690 916 and the PCT International Application no EP95/03826, or a combination of genes encoding at least a Cry-type toxin and a VIP-type toxin, respectively. For recombinant production of the toxin protein in a host organism, the coding sequence may be inserted into an expression cassette designed for the chosen host and introduced into the host where it is recombinantly produced. The choice of specific regulatory sequences such as promoter, signal sequence, 5' and 3' untranslated sequences, and enhancer appropriate for the chosen host is within the level of skill of the routineer in the art. The resultant molecule, containing the individual elements linked in proper reading frame, may be inserted into a vector capable of being transformed into the host cell. Suitable expression vectors and methods for recombinant production of proteins are well known for host organisms such as E. coli (see, e.g. Studier and Moffatt, J. Mol. Biol. 189: 1 13 (1986); Brosius, DNA 8: 759 (1989)), yeast (see, e.g., Schneider and Guarente, Meth. Enzymol. 194: 373 (1991 )) and insect cells (see, e.g., Luckow and Summers, Bio/Technol. 6: 47 (1988)). Specific examples include plasmids such as pBluescript (Stratagene, La Jolla, CA), pFLAG (International Biotechnologies, Inc., New Haven, CT), pTrcHis (Invitrogen, La Jolla, CA), and baculovirus expression vectors, e.g., those derived from the genome of Autographica californica nuclear polyhedrosis virus (AcMNPV). A preferred baculovirus/insect system is pVI11392/Sf21 cells (Invitrogen, La Jolla, CA). The recombinantly produced toxin protein can be isolated and purified using a variety of standard techniques. The actual techniques which may be used will vary depending upon the host organism used, whether the toxin protein is designed for secretion, and other such factors familiar to the skilled artisan (see, e.g. chapter 16 of Ausubel, F. et al., "Current Protocols in Molecular Biology", pub. by John Wiley & Sons, Inc. (1994). A further object of the invention relates to the use of transgenic plants comprising and expressing a toxin gene encoding a toxin protein of Bacillus thuringiensis, but especially a Cryl-type toxin protein, in an amount sufficient to provide control against Sesamia species, in a method of protecting crop plants against damages caused by Sesamia pests. Especially preferred are transgenic plants expressing a CrylA(b) toxin protein of Bacillus thuringiensis. The invention also relates to the use of transgenic plants comprising a toxin gene encoding a VIP-type protein as described in EP-A 0 690 916 and the PCT International Application no EP95/03826, herein incorporated by reference in its entirety. The invention also relates to the use of transgenic plants comprising and expressing a toxin gene encoding a toxin protein of Bacillus thuringiensis, but especially a Cry-type toxin protein, and also comprising and expressing a toxin gene encoding a VIP- type protein in an amount sufficient to provide control against Sesamia species. A host plant expressing the said toxin genes will have enhanced resistance to insect attack of Sesamia species and will be thus better equipped to withstand crop losses associated with such attack. In one preferred embodiment, expression of one or more Bt δ-endotoxins in a transgenic plant is accompanied by the expression of one or more VIP-type proteins. This co-expression of more than one insecticidal principle in the same transgenic plant can be achieved by genetically engineering a plant to contain and express all the genes necessary. Alternatively, a plant, Parent 1 , can be genetically engineered for the expression of VIP-type proteins. A second plant, Parent 2, can be genetically engineered for the expression of Bt δ-endotoxin. By crossing Parent 1 with Parent 2, progeny plants are obtained which express all the genes introduced into Parents 1 and 2. Particularly preferred Bt δ- endotoxins are those disclosed in EP-A 0618976, herein incorporated by reference. Also comprised by the present invention is the use of recombinant microorganisms or transgenic plants comprising a gene encoding DNA molecules which hybridizes to a DNA molecule encoding a toxin protein of Bacillus species, but preferably to an oligonucleotide probe obtainable from said DNA molecule comprising a contiguous portion of the coding sequence for the said toxin protein at least 10 nucleotides in length, under moderately stringent conditions. The invention preferably comprises the use of recombinant microorganisms or transgenic plants comprising a gene encoding DNA molecules which hybridizes to a DNA molecule encoding a toxin protein of Bacillus thuringiensis or B cereus especially to a DNA molecule encoding a Cry-type protein or to a toxin gene encoding a VIP-type toxin protein, preferably to a CrylA(b) protein. Factors that effect the stability of hybrids determine the stringency of the hybridization. One such factor is the melting temperature T m which can be easily calculated according to the formula provided in DNA PROBES, George H. Keller and Mark M. Manak , Macmillan Publishers Ltd, 1993, Section one: Molecular Hybridization Technology; page 8 ff. The preferred hybridization temperature is in the range of about 25°C below the calculated melting temperature T m and preferably in the range of about 12-15°C below the calculated melting temperature T m and in the case of oligonucleotides in the range of about 5-10°C below the melting temperature T m . The invention further relates to a commercial bag comprising seed of a transgenic plant comprising at least a toxin gene encoding a toxin protein of Bacillus thuringiensis, preferably a Cry-type toxin protein, more preferably a Cryl-type toxin protein, but most preferably a CrylA-type toxin protein and expressing the said toxin protein in an amount sufficient to provide control against Sesamia species, together with lable instructions for the use thereof for control of Sesamia pests in crop plants. Preferred within this invention is a commercial bag comprising seed of a transgenic plant comprising as an active ingredient a gene encoding at least a Cry-type toxin protein and a VIP-type protein, preferably in a synergistically effective amount. Especially preferred is a combination of a CrylA(b) toxin protein with a VIP-type protein. The further object of the invention is a commercial bag comprising an insecticidal composition according to the invention together with lable instructions for the use thereof for control of Sesamia pests in crop plants. By plant is meant any plant species which can be genetically transformed by methods known in the art, but especially those plants that are host plants for Sesamia species including, but not limited to, the following species of plants: maize, wheat, barley, rye, oats, rice, sorghum, millet and related crops, forage grasses (orchardgrass, fescue, and the like), and sugar cane. Methods known in the art for plant transformation are discussed below. Host plants include, but are not limited to, those species previously listed as target crops. It has been discovered that the codon usage of a native Bacillus thuringiensis toxin gene is significantly different from that which is typical of a plant gene. In particular, the codon usage of a native Bacillus thuringiensis gene is very different from that of a maize gene. As a result, the mRNA from this gene may not be efficiently utilized. Codon usage might influence the expression of genes at the level of translation or transcription or mRNA processing. To optimize a toxin gene for expression in plants, for example in maize, the codon usage is optimized by using the codons which are most preferred in maize (maize preferred codons) in the synthesis of a synthetic gene which encodes the same protein as found for the native toxin gene sequence. The optimized maize preferred codon usage is effective for expression of high levels of the Bt insecticidal protein. Further details for constructing maize-optimized synthetic toxin genes can be found in WO 93/07278, herein incorporated by reference in its entirety. Toxin genes derived from microorganisms may also differ from plant genes. Plant genes differ from genes found in microorganisms in that their transcribed RNA does not possess defined ribosome binding site sequence adjacent to the initiating methionine. Consequently, microbial genes can be enhanced by the inclusion of a eukaryotic consensus translation initiator at the ATG. Clontech (1993/1994 catalog, page 210) has suggested the sequence GTCGACCATGGTC as a consensus translation initiator for the expression of the E. coli uidA gene in plants. Further, Joshi (Nucl Acids Res 15: 6643-6653 (1987)) has compared many plant sequences adjacent to the ATG and suggests the consensus TAAACAATGGCT. In situations where difficulties are encountered in the expression of microbial ORFs in plants, inclusion of one of these sequences at the initiating ATG may improve translation. In such cases the last three nucleotides of the consensus may not be appropriate for inclusion in the modified sequence due to their modification of the second AA residue. Preferred sequences adjacent to the initiating methionine may differ between different plant species. By surveying the sequence of maize genes present in the GenBank/EMBL database it can be discerned which nucleotides adjacent to the ATG should be modified to enhance translation of the toxin gene introduced into maize. In addition, it has been shown that removal of illegitimate splice sites can enhance expression and stability of introduced genes. Genes cloned from non-plant sources and not optimized for expression in plants may contain motifs which can be recognized in plants as 5' or 3' splice sites. Consequently, the transcription process can be prematurely terminated, generating truncated or deleted mRNA. The toxin genes can be engineered to remove these illegitimate splice sites using the techniques well known in the art. It is well known that many δ-endotoxin proteins from Bacillus thuringiensis are actually expressed as protoxins. These protoxins are solubilized in the alkaline environment of the insect gut and are proteolytically converted by proteases into a toxic core fragment (Hόfte and Whiteley, Microbiol. Rev. 53: 242-255 (1989)). For δ-endotoxin proteins of the Cryl class, the toxic core fragment is localized in the N-terminal half of the protoxin. It is within the scope of the present invention that genes encoding either the full-length protoxin form or the truncated toxic core fragment of the novel toxin protein can be used in plant transformation vectors to confer insecticidal properties upon the host plant. The recombinant DNA molecules can be introduced into the plant cell in a number of art-recognized ways. Those skilled in the art will appreciate that the choice of method might depend on the type of plant, i.e. monocot or dicot, targeted for transformation. Suitable methods of transforming plant cells include microinjection (Crossway et al., BioTechniques 4:320-334 (1986)), electroporation (Riggs et al, Proc. Natl. Acad. Sci. USA 83:5602-5606 (1986), Agrobacterium-med ateό transformation (Hinchee et al., Biotechnology 6:915-921 (1988)), direct gene transfer (Paszkowski et al., EMBO J. 3:2717-2722 (1984)), and ballistic particle acceleration using devices available from Agracetus, Inc., Madison, Wisconsin and Dupont, Inc., Wilmington, Delaware (see, for example, Sanford et al., U.S. Patent 4,945,050; and McCabe et al., Biotechnology 6:923-926 (1988)). See also, Weissinger et al., Annual Rev. Genet. 22:421-477 (1988); Sanford et al., Particulate Science and Technology 5:27-37 91 987)(onion) ; Christou et al . , Plant Physiol . 87:671-674 (1988)(soybean); McCabe et al., Bio/Technology 6:923-926 (1988)(soybean); Datta et al., Bio/Technology 8:736-740 (1990)(rice); Klein et al ., Proc. Natl. Acad. Sci. USA, 85:4305-4309 (1988)(maize); Klein et al., Bio/Technology 6:559-563 (1988)(maize); Klein et al., Plant Physiol. 91:440-444 (1988)(maize); Fromm et al., Bio/Technology 8:833-839 (1990); and Gordon-Kamm et al., Plant Cell 2:603-618 (1990)(maize); Svab et al. Proc. Natl. Acad. Sci. USA 87: 8526-8530 (1990) (tobacco chloroplast); Koziel et al. (Biotechnology ϋ: 194-200 (1993)) (maize); Shimamoto et al. Nature 338: 274-277 (1989) (rice); Christou et al. Biotechnology 9: 957-962 (1991 ) (rice); European Patent Application EP 0 332 581 (orchardgrass and other Pooideae); Vasil et al. (Biotechnology J .: 1553-1558 (1993) (wheat); Weeks et al. (Plant Physiol. 102: 1077-1084 (1993) (wheat); Wan et al (Plant Physiol 104: 37-48 (1994) (barley); Umbeck et al, (Bio/Technology 5: 263-266 (1987) (cotton). One particularly preferred set of embodiments for the introduction of recombinant DNA molecules into maize by microprojectile bombardment can be found in WO 93/07278, herein incorporated by reference in its entirety. An additional preferred embodiment is the protoplast transformation method for maize as disclosed in European Patent Application EP 0 292 435, hereby incorporated by reference in its entirety. The genetic properties engineered into the transgenic seeds and plants described above are passed on by sexual reproduction or vegetative growth and can thus be maintained and propagated in progeny plants. Generally said maintenance and propagation make use of known agricultural methods developed to fit specific purposes such as tilling, sowing or harvesting. Specialized processes such as hydroponics or greenhouse technologies can also be applied. As the growing crop is vulnerable to attack and damages caused by insects or infections as well as to competition by weed plants, measures are undertaken to control weeds, plant diseases, insects, nematodes, and other adverse conditions to improve yield. These include mechanical measures such a tillage of the soil or removal of weeds and infected plants, as well as the application of agrochemicals such as herbicides, fungicides, gametocides, nematicides, growth regulants, ripening agents and insecticides. Use of the advantageous genetic properties of the transgenic plants and seeds according to the invention can further be made in plant breeding which aims at the development of plants with improved properties such as tolerance of pests, herbicides, or stress, improved nutritional value, increased yield, or improved structure causing less loss from lodging or shattering. The various breeding steps are characterized by well-defined human intervention such as selecting the lines to be crossed, directing pollination of the parental lines, or selecting appropriate progeny plants. Depending on the desired properties different breeding measures are taken. The relevant techniques are well known in the art and include but are not limited to hybridization, inbreeding, backcross breeding, multiline breeding, variety blend, interspecific hybridization, aneuploid techniques, etc. Hybridization techniques also include the sterilization of plants to yield male or female sterile plants by mechanical, chemical or biochemical means. Cross pollination of a male sterile plant with pollen of a different line assures that the genome of the male sterile but female fertile plant will uniformly obtain properties of both parental lines. Thus, the transgenic seeds and plants according to the invention can be used for the breeding of improved plant lines which for example increase the effectiveness of conventional methods such as herbicide or pestidice treatment or allow to dispense with said methods due to their modified genetic properties. Alternatively new crops with improved stress tolerance can be obtained which, due to their optimized genetic "equipmenf, yield harvested product of better quality than products which were not able to tolerate comparable adverse developmental conditions. In seeds production germination quality and uniformity of seeds are essential product characteristics, whereas germination quality and uniformity of seeds harvested and sold by the farmer is not important. As it is difficult to keep a crop free from other crop and weed seeds, to control seedborne diseases, and to produce seed with good germination, fairly extensive and well-defined seed production practices have been developed by seed producers, who are experienced in the art of growing, conditioning and marketing of pure seed. Thus, it is common practice for the farmer to buy certified seed meeting specific quality standards instead of using seed harvested from his own crop. Propagation material to be used as seeds is customarily treated with a protectant coating comprising herbicides, insecticides, fungicides, bactericides, nematicides, molluscicides or mixtures thereof. Customarily used protectant coatings comprise compounds such as captan, carboxin, thiram (TMTD ® ), methalaxyl (Apron*), and pirimiphos-methyl (Actellic*). If desired these compounds are formulated together with further carriers, surfactants or application- promoting adjuvants customarily employed in the art of formulation to provide protection against damage caused by bacterial, fungal or animal pests. The protectant coatings may be applied by impregnating propagation material with a liquid formulation or by coating with a combined wet or dry formulation. Other methods of application are also possible such as treatment directed at the buds or the fruit. It is a further aspect of the present invention to provide new agricultural methods such as the methods examplified above which are characterized by the use of transgenic plants, transgenic plant material, or transgenic seed according to the present invention to provide control against Sesamia species. To breed progeny from plants transformed according to the method of the present invention, a method such as that which follows may be used: maize plants produced as described in the examples set forth below are grown in pots in a greenhouse or in soil, as is known in the art, and permitted to flower. Pollen is obtained from the mature tassel and used to pollinate the ears of the same plant, sibling plants, or any desirable maize plant. Similarly, the ear developing on the transformed plant may be pollinated by pollen obtained from the same plant, sibling plants, or any desirable maize plant. Transformed progeny obtained by this method may be distinguished from non-transformed progeny by the presence of the introduced gene(s) and/or accompanying DNA (genotype), or the phenotype conferred. The transformed progeny may similarly be selfed or crossed to other plants, as is normally done with any plant carrying a desirable trait. Similariy, tobacco or other transformed plants produced by this method may be selfed or crossed as is known in the art in order to produce progeny with desired characteristics. Similarly, other transgenic organisms produced by a combination of the methods known in the art and this invention may be bred as is known in the art in order to produce progeny with desired characteristics. The so produced seeds and plants can be introduced into a plant cultivation scheme desinged to protect crop plants against damage cause by Sesamia species. It is long knwon that control of the second generation of Sesamia species is difficult to achieve by application of insecticides because the larvae are usually located at the bottom of the full-grown plant and are thus difficult to reach by insecticide spraying. It is therefore advisable to control the diapause population in winter and the first generation of the Sesamia species in spring and thus to reduce the population of the second generation of insects. In winter, the diapause population can be controlled by turn of soil and simultaneous grinding of the remaining plant residues (plant stump, roots) after harvest. In spring, the first generation can be controlled by application of insecticides. As a result the second generation is reduced and can be controlled with less effort. It is thus a further aspect of the present invention to provide an agricultural method for controlling the first and second generation of Sesamia insects, which method combines state of the art methods with those developed within the scope of this invention. In particular, the agricultural method according to the invention comprises combining mechanical, chemical and genetic engineering means in order to achieve a full control of Sesamia in crop plants. The agricultural method for fully controlling Sesamia species in crop plants according to the invention comprises the use of seeds or plants to which a toxin protein of a Bacillus species, but preferably a Cryl-type toxin protein and/or a VIP-type toxin protein, has been applied directly or indirectly as an active ingredient. Direct application of the said toxin proteins to the seed or plant may be accomplished by treating the said seed or plants with a composition according to the invention as described hereinbefore. Alternatively, the active ingredients can be applied to the seed or plant to be protected indirectly, that is by expressing one or more genes encoding at least a Cry-type toxin protein, preferably a Cryl- type protein, and most preferably a CrylA(b) protein and/or a VIP-type protein within the said seed or plant, preferably in a synergistically effective amount. Direct and indirect application of the active ingredients according to the invention may be combined such that either a VIP-type or a Cry-type protein is expressed within the plant while the other protein is applied to the plant externally. The transgenic expression of a a VIP-type and/or a Cry-type protein within the plant may also be combined with a chemical treatment of said plant using any one of the commonly applied insecticides. The invention is thus further directed to an agricultural method for protecting plants against damage caused by Sesamia species comprising a combination of steps (2) and (3) with any one of steps (1 ) or (4): (1) control of diapause population by mechanical grinding of the plant residues after harvest (2) control of the first generation of Sesamia species by one of the methods according to the invention (3) control of the second generation of Sesamia species by one of the methods according to the invention. (4) control of the diapause population, the first and/or the second generation by treating them with a commonly applied insecticide. A preferred embodiment of the present invention is the use of plants transformed according to the invention in an agricultural method for controlling Sesamia species by reducing the population of the first generation and, preferably also the population of the second generation of Sesamia species. Also preferred is the combination of transgenic plants with the application of compositions comprising a biological compound as defined above or a commonly applied insecticide. EXAMPLES The following examples further describe the materials and methods used in carrying out the invention. They are offered by way of illustration, and not by way of limitation. EXAMPLE 1 : General Methods DNA manipulations were done using procedures that are standard in the art. These procedures can often be modified and/or substituted without substantively changing the result. Except where other references are identified, most of these procedures are described in Sambrook et al., Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, second edition, 1989. EXAMPLE 2: Plant Transformation 2.1 Transformation Vector Plant transformation is accomplished using plant transformation vectors pCIB 4431 and pCIB 3064, the construction of which is described in WO 93/07278 and in Koziel et al (1993) [Biotechnology Vol 11 , 194-200], the disclosure of which are incorporated herein by reference. pCIB4431 is a vector designed to transform maize. It contains two chimeric synthetic Bt crylA(b) endotoxin genes expressible in maize. These genes are the PEP carboxylase promoter/synthetic-ctyMfb) and a pollen promoter/synthetic-cr Mfb,). pCIB 4431 containing the synthetic crylA(b) gene provided as SEQ ID NO: 1 was deposited September 21 , 1992 with the Agricultural Research Service, Patent Culture Collection (NRRL), Northern Regional Research Center, 1815 North University Street, Peoria, Illinois 61604, U.S.A. under accession no NRRL #B-18998. pCIB 3064 contains a plant expressible bar gene (615 bp), which was originally cloned from Streptomyces hygroscopicus [Thompson et al (1987) EMBO J 6, 2519-2523]. It encodes a phosphinotricin acetyltransferase (PAT), conferring tolerance to phosphinotricin. The bar gene is under the control of the CaMV 35S promoter and terminator [OW et al (1987) Proc Natl Acad Sci USA 84, 4870-4874] to provide resistance to phosphinotricin. EXAMPLE 3: Production of transgenic maize plants containing the synthetic maize CrylA(b) gene The example below utilizes a Biolistic device to introduce DNA coated particles into maize cells, from which transformed plants are generated. 3.1 Tissue Immature maize embryos, approximately 1.5-2.5 mm in length, were excised from an ear of genotype 6N615 14-15 days after pollination. The mother plant was grown in the greenhouse. Before excision, the ear was surface sterilized with 20% Clorox for 20 minutes and rinse 3 times with sterile water. Individual embryos were plated scutellum side up in a 2 cm square area, 36 embryos to a plate, on the callus initiation medium, 2DG4 + 5 chloramben medium (N6 major salts, B5 minor salts, MS iron, 2% sucrose, with 5 mg/l chloramben, 20 mg/l glucose, and 10 ml G4 additions (Table 1) added after autoclaving. TABLE 1 - G4 Additions 3.2 Preparation of DNA for delivery The microcarrier was prepared essentially according to the instructions supplied with the Biolistic device. While vortexing 50 μl 1.0 μm gold microcarrier, 5 μl of pCIB4431 (1.23 μg/μl) [#898] + 2 μl pCIB3064 (0.895 μg/μl) [#456] was added followed by 50 μl 2.5 M CaCl2, then 20 μl 0.1 M spermidine (free base, TC grade). The resulting mixture was vortexed 3 minutes and microfuged for 10 sec. The supernatant was removed and the microcarriers washed 2 times with 250 μl of 100% EtOH (HPLC grade) by vortexing briefly, centrifuging and removing the supernatant. The microcarriers are resuspended in 65 μl 100% EtOH. 3.3 Bombardment Tissue was bombarded using the PDS-1000He Biolistics device. The tissue was placed on the shelf 8 cm below the stopping screen shelf. The tissue was shot one time with the DNA/gold microcarrier solution, 10 μl dried onto the macrocarrier. The stopping screen used was hand punched using 10x10 stainless steel mesh screen. Rupture discs of 1550 psi value were used. After bombardment, the embryos were cultured in the dark at 25° C. 3.4 Callus formation Embryos were transferred to callus initiation medium with 3 mg/l PPT 1 day after bombardment. Embryos were scored for callus initiation at 2 and 3 weeks after bombardment. Any responses were transferred to callus maintenance medium, 2DG4 + 0.5 2,4-D medium with 3 mg/L PPT. Callus maintenance medium is N6 major salts, B5 minor salts, MS iron, 2% sucrose, with 0.5 mg/l 2,4-D, 20 mg/l glucose, and 10 ml G4 additions added after autoclaving. Embryogenic callus was subcultured every 2 weeks to fresh maintenance medium containing 3 mg/L PPT. All callus was incubated in the dark at 25°C. The Type I callus formation response was 15%. Every embryo which produced callus was cultured as an individual event giving rise to an individual line. 3.5 Regeneration After 12 weeks on selection, the tissue was removed from callus maintenance medium with PPT and was placed on regeneration medium. Regeneration medium is 0.25MS3S5BA (0.25 mg/l 2,4 D, 5 mg/l BAP, MS salts, 3% sucrose) for 2 weeks followed by subculture to MS3S medium for regeneration of plants. After 4 to 10 weeks, plants were removed and put into GA 7's. 3.6 Backcrossing Regenerated transgenic plants are back-crossed into a different genetic background [2N217AF; 6Y021 ] resulting in Events AB01 [2N217AF(Bt)] and AB10 [6Y021 (Bt)], which are hemizygous for the Bt trait. Non-transforemd Inbred lines 2N217AF [CG01] and 6Y021 [CG10] are used as controls in the Sesamia Assay described below in Example 4. EXAMPLE 4: Sesamia Assay Parameters recorded: 24/48 hours old larvae of Sesamia nonagrioides [MCB] were allowed to feed on maize leaves. Larvae had not previously been feeding. 72 and 120/152 hours later the number of larvae alive and development instar of each one were recorded. The kind of feeding injuries on leaf plant was observed in each case. Treatments: Four different maize "events" were used (AB01 , AB10, CG01 , CG10). Leaves were exised and used in the feeding experiments as described below. Number of larvae tested: Groups of 5 larvae were put inside translucent plastic containers with several pieces of maize leaves. Containers were cylindrical, diameter 5,4 cm and 3 cm high. Sixteen groups of 5 larvae each (80 larvae) were used for each "event". So, a total of 320 MCB larvae were used for all the evaluation. This was carried out in 2 steps. In the first step 24 hours old larvae were used; in the second step 48 hours old larvae. Experimental conditions: Temperature 25±1°C, Photoperiod: 16L/8D Summary of results: Percentage of mortality after 72 hours (mean ± standard error): AB01 : 84±8% (n=15, n is the number of containers with 5 larvae) AB10: 87±7% (n=15, n is the number of containers with 5 larvae) CG10: 2,5±1 ,7% (n=16, n is the number of containers with 5 larvae) CG01 : 3,8±2,7% (n=16, n is the number of containers with 5 larvae) Percentage of mortality after 120/152 hours (mean ± standard error): AB01 : 100% (n=15, n is the number of containers with 5 larvae) AB10: 100% (n=15, n is the number of containers with 5 larvae) CG10: 14+3% (n=16, n is the number of containers with 5 larvae) CG01 : 14+5% (n=16, n is the number of containers with 5 larvae) Development: Since most of larvae on AB01 and AB10 died before first observation (72h.), no host effect on larval development could be observed. However, there were some indications of larval development delay in AB01 and AB10. Injuries on excised maize leaves: Two kind of injuries were clearly distinguished in maize leaves. Leaf pieces coded as AB01 and AB10 showed small holes in the upper epidermis whereas those coded as CG10 and CG01 showed wide areas without upper epidermis. Larvae on AB01 and AB10 scarcely ate and no excrements were observed in rearing containers. On the contrary, larvae on CG01 and CG10 ate big areas of upper epidermis and abundant excrements in rearing container was observed. Conclusion: The results of the Seamia assay show a strong effect of AB01 and AB10 on larval mortality and larval feeding. With the methodology used in the present trials no differences between AB01 and AB10 were detected. Injuries in AB01 and AB10 were much lower than in CG01 and CG10. EXAMPLE 5: EFFECTS OF Vip3A ON NEONATE Sesamia nonagrioides LARVAE. Effects of Vip3A on neonate larvae of the Mediterranean Corn Borer Sesamia nonagrioides. CG00526 is the maize genotype used as negative control. It is an inbred line, which has been described by Koziel et al. (1993), Bio/Technology 11 , pp. 194-200. The gene encoding the Vip3A protein was transformed into the CG00526 genotype by biolistics. The crosses CG00526 x 891 and 892 refer to crosses of transformation events (891 and 892) with the parental line CG00526. Two of the events obtained expressing the Vip3A protein have been used for the insect bioassay (positive segregants). Positive segregants are plants that inherited the vip3A gene. Negative segregants are T1 plants that did not inherit the vip3A gene, therefore they do not express the Vip3A protein. SEQUENCE LISTING (1) GENERAL INFORMATION: (A) NAME: CIBA-GEIGY AG (B) STREET: Klybeckstr. 141 (C) CITY: Basel (E) COUNTRY: Switzerland (F) POSTAL CODE (ZIP) : 4002 (G) TELEPHONE: +41 61 69 11 11 (H) TELEFAX: + 41 61 696 79 76 (I) TELEX: 962 991 (ii) TITLE OF INVENTION: Method of Controlling Insect Pests (iii) NUMBER OF SEQUENCES: 55 (iv) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentln Release #1.0, Version #1.30B (2) INFORMATION FOR SEQ ID NO:l: (i) SEQUENCE CHARACTERISTICS: (A) LENG7IH: 6049 base pairs (B) TYPE: nucleic acid (C) STRANDEE-NESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: EMA (genα ic) (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus cereus (B) STRAIN: AB78 (C) INDIVIDUAL ISOLATE: NRRL B-21058 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1082..2467 (D) OTHER INFORMATION: /product= "VIP2A(a) " (ix) FEATURE: (A) NAME/KEY: ιnisc_feature (B) LOCATION: 2475. .5126 (D) OTHER INFORMATION: /note= "Coding sequence for the 100 kd VTPlA(a) protein. This coding sequence is repeated in SEQ ID NO:4 and translated separately. " (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: ATCGATACAA TGTTGTTTTA CTTAGACCGG TAGTCTCTGT AATTTGTTTA ATGCTATATT 60 CTTΓACTΓTG ATACΆTTT A ATAGCCATTT C^CCTTATC AGTATGTTTT TGTGGTCTTC 120 CTCCTTTTTT TCCACGAGCT CTAGCTGCGT TTAATCCTGT TTTGGTACGT TOGCTAATAA 180 TATCTCTTTC TAATTCTGCA ATACTTGCCA TCATTCGAAA GAAGAATTTC CCCATAGCAT 240 TAGAGGTATC AATGTTGTCA TGAATAGAAA TAAAATCTAC ACCTAGCTCT TTGAATTTTT 300 (.ΛCTTAACTC AATTAGGTGT TTTGTAGAGC GAGAAATTCG ATCAAGITTG TAAACAACTA 360 TCTTATCGCC TTTACGTAAT ACTTTTAGCA AC CTTCGAG TTGAGGGCGC TCTTTTTTTA 420 TTCC -TTAT TTTCTCCTGA TATAGCCTTT CTACACCATA TTOTTGCAAA GC-ATCTATTT 480 GCATATCGAG ATTI GTTCT TCTGTOCTGA CACGAGCATA ACCAAAAATC AAATTGGTTT 540 CΑCTTCCTAT CTAAATATAT CTATTAAAAT AGCACCAAAA ACCTTATTAA ATTAAAATAA 600 GGAACTTTGT TTTTGGATAT GGATTTTGGT ACTCAATATG G-ATGAGTTTT TAAα3-TT-T 660 GTTAAAAAAC AAACAAGTGC CATAAACGGT OTITITrGGG ATGACATAAT AAATAATCTG 720 TTTGATTAAC (_TAACCTTGT ATCCTTACAG α_X_AGTTTTA TTTCTACTTC AACTGACT3A 780 ATATGAAAAC AACATGAAGG TTTCATAAAA TTTATATATT 1TCCATAACG GATGCTCTAT 840 CTTΓAGGTΓA AGTTAAATT ATAAGAAAAA AACAAACGGA GGGAGTGAAA AAAAGCATCT 900 TCTCTATAAT TTTACAGGCT CTTTAATAAG AAGGGGGGAG ATTAGATAAT AAATATGAAT 960 ATCTATCTAT AATTGTTTGC TTCTACAATA ACTTATCTAA CΓΓTCATATA CAACAACAAA 1020 ACAGACTAAA TCX-AGATTGT ATATTCATTT TCAGTTGTTC CTTTATAAAA TAATTTCATA 1080 A ATG AAA AGA ATG GAG GGA AAG TTG TTT ATG GTG TCA AAA AAA TTA 1126 Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu 1 5 10 15 CAA GTA GTT ACT AAA ACT GTA TTG CTT AGT ACA GTT TTC TCT ATA TCT 1174 Gin Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser He Ser 20 25 30 TTA TTA AAT AAT GAA GTG ATA AAA GCT GAA CAA TTA AAT ATA AAT TCT 1222 Leu Leu Asn Asn Glu Val He Lys Ala Glu Gin Leu Asn He Asn Ser 35 40 45 CAA AGT AAA TAT ACT AAC TTG CAA AAT CTA AAA ATC ACT GAC AAG GTA 1270 Gin Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Thr Asp Lys Val 50 55 60 GAG GAT TTT AAA GAA GAT AAG GAA AAA GCG AAA GAA TGG GGG AAA GAA 1318 Glu Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu 65 70 75 AAA GAA AAA GAG TGG AAA CTA ACT GCT ACT GAA AAA GGA AAA ATG AAT 1366 Lys Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn 80 85 90 95 AAT TTT TTA GAT AAT AAA AAT GAT ATA AAG ACA AAT TAT AAA GAA ATT 1414 Asn Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He 100 105 110 ACT TTT TCT ATG GCA GGC TCA TTT GAA GAT GAA ATA AAA GAT TTA AAA 1462 Thr Phe Ser Met Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys 115 120 125 GAA ATT GAT AAG ATG TTT GAT AAA ACC AAT CTA TCA AAT TCT ATT ATC 1510 Glu He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He 130 135 140 ACC TAT AAA AAT GTG GAA CCG ACA ACA ATT GGA TTT AAT AAA TCT TTA 1558 Thr Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu 145 150 155 ACA GAA GGT AAT ACG ATT AAT TCT GAT GCA ATG GCA CAG TTT AAA GAA 1606 Thr Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu 160 165 170 175 CAA TTT TTA GAT AGG GAT ATT AAG TTT GAT AGT TAT CTA GAT ACG CAT 1654 Gin Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His 180 185 190 TTA ACT GCT CAA CAA GTT TCC AGT AAA GAA AGA GTT ATT TTG AAG GTT 1702 Leu Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val 195 200 205 ACG GTT CCG AGT GGG AAA GGT TCT ACT ACT CCA ACA AAA GCA GGT GTC 1750 Thr Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val 210 215 220 ATT TTA AAT AAT AGT GAA TAC AAA ATG CTC ATT GAT AAT GGG TAT ATG 1798 He Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met 225 230 235 GTC CAT GTA GAT AAG GTA TCA AAA GTG GTG AAA AAA GGG GTG GAG TGC 1846 Val His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys 240 245 250 255 TTA CAA ATT GAA GGG ACT TTA AAA AAG AGT CTT GAC TTT AAA AAT GAT 1894 Leu Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp 260 265 270 ATA AAT GCT GAA GCG CAT AGC TGG GGT ATG AAG AAT TAT GAA GAG TGG 1942 He Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp 275 280 285 GCT AAA GAT TTA ACC GAT TCG CAA AGG GAA GCT TTA GAT GGG TAT GCT 1990 Ala Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala 290 295 300 AGG CAA GAT TAT AAA GAA ATC AAT AAT TAT TTA AGA AAT CAA GGC GGA 2038 Arg Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly 305 310 315 AGT GGA AAT GAA AAA CTA GAT GCT CAA ATA AAA AAT ATT TCT GAT GCT 2086 Ser Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala 320 325 330 335 TTA GGG AAG AAA CCA ATA CCG GAA AAT ATT ACT GTG TAT AGA TGG TGT 2134 Leu Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys 340 345 350 GGC ATG CCG GAA TTT GGT TAT CAA ATT AGT GAT CCG TTA CCT TCT TTA 2182 Gly Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu 355 360 365 AAA GAT TTT GAA GAA CAA TTT TTA AAT ACA ATC AAA GAA GAC AAA GGA 2230 Lys Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly 370 375 380 TAT ATG AGT ACA AGC TTA TCG AGT GAA CGT CTT GCA GCT TTT GGA TCT 2278 Tyr Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser 385 390 395 AGA AAA ATT ATA TTA CGA TTA CAA GTT CCG AAA GGA AGT ACG GGT GCG 2326 Arg Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala 400 405 410 415 TAT TTA ACT GCC ATT GGT GGA TTT GCA AGT GAA AAA GAG ATC CTA CTT 2374 Tyr Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu 420 425 430 GAT AAA GAT AGT AAA TAT CAT ATT GAT AAA GTA ACA GAG GTA ATT ATT 2422 Asp Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He 435 440 445 AAA GGT GTT AAG CGA TAT GTA GTG GAT GCA ACA TTA TTA ACA AAT 2467 Lys Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 450 455 460 TAAGGAGATG AAAAATATGA AGAAAAAGTT AGCAAGTGTT GTAACGTGTA CGTTATTAGC 2527 TCCTATGTTT TTGAATGGAA ATGTGAATGC TGTTTACGCA GACAGCAAAA CAAATCAAAT 2587 TTCTACAACA CAGAAAAATC AACAGAAAGA GATGGACCGA AAAGGATTAC TTGGGTATTA 2647 TTTCAAAGGA AAAGATTTTA GTAATCTTAC TATGTTTGCA CCGACACGTG ATAGTACTCT 2707 TATTTATGAT CAACAAACAG CAAATAAACT ATTAGATAAA AAACAACAAG AATATCAGTC 2767 TATTCGTTGG ATTGGTTTGA TTCAGAGTAA AGAAACGGGA GATTTCACAT TTAACTTATC 2827 TGAGGATGAA C&GGCAATTA TAGAAATCAA TGGGAAAATT ATTTCTAATA AAGGGAAAGA 2887 AAAGCAAGTT C?ICCATTTAG AAAAAGGAAA ATTAGTTCCA ATCAAAATAG AGTATCAATC 2947 AGATACAAAA TTTAATATTG ACAGTAAAAC ATTTAAAGAA CTTAAATTAT TTAAAATAGA 3007 TAGTCAAAAC CAACCCCAGC AAGTCCAGCA AGATGAACTG AGAAATCCTG AATTTAACAA 3067 GAAAGAATCA CAGGAATTCT TAGCGAAACC ATCGAAAATA AATCTTT CA CTCAAAAAAT 3127 GAAAAGGGAA ATTGATGAAG ACACGGATAC GGATGGGGAC TCTATTCCTG ACCTTTGGGA 3187 AGAAAATGGG TATACGATTC ACAATAGAAT α_CTGTAAAG TC 2ACGATT CTCTAGCAAG 3247 TAAAGGGTAT ACGAAATTTG TTICAAATCC ACTAGAAAGT CACACAGTTG GTCATCCTTA 3307 TACAGATTAT GAAAAGGCAG CAAGAGATCT AGATTTGTCA AATGCAAAGG AAACGTTTAA 3367 CCCATTGGTA GCTGCTI IC CAAGTGTGAA TGTTAGTATG GAAAAGGTGA TATTATCACC 3427 AAATGAAAAT TTATCCAATA GTGTAGAGTC TCATTCATCC ACGAATTGGT CTTATACAAA 3487 TACAGAAGGT GCTTCTGTTG AAGCGGGGAT TGGACCAAAA GGTATTTCGT TCXSGAGTTAG 3547 CGTAAACTAT CAAC.ACICTG AAACAGTTGC ACAAGAATGG GGAACATCTA CAGGAAATAC 3607 TTCGCAATTC AATACGGCTT CAGCGGGATA TTTAAATGCA AATCTTCGAT ATAACAATGT 3667 AGGAACTGGT GCCATCTACG ATGTAAAACC TACAACAAGT TTTGTATTAA ATAACGATAC 3727 TATCGCAACT ATTACGGCGA AATCTAATTC TACAGCCTTA AATATATCTC CTGGAGAAAG 3787 TTACCCGAAA AAAGGACAAA ATGGAATCGC AATAACATCA ATCGATGATT TTAATTCCCA 3847 TCCGATTACA TTAAATAAAA AACAAGTAGA TAATCTGCTA AATAATAAAC CTATGATGTT 3907 GGAAACAAAC CAAACAGATG C _TTTATAA GATAAAAGAT ACACATGGAA ATATAGTAAC 3967 T03CGGAGAA TGGAATGGTG TCATACAACA AATCAAGGCT AAAACAGCGT CTATTATTGT 4027 GGATGATGGG GAACGTGTAG CAGAAAAACG TGTAGOGGCA AAAGATTATG AAAATCCAGA 4087 AGATAAAACA CCGTCTTTAA CTTTAAAAGA TCCCCTGAAG CTTTCATATC CAGATGAAAT 4147 AAAAGAAATA GAGGGATTAT TATATTATAA AAACAAACCG ATATACGAAT CGAGCGTTAT 4207 GACTTACTTA GATGAAAATA CAGCAAAAGA AGTGACCAAA CAATTAAATG ATACCACTGG 4267 GAAATTTAAA GATGTAAGTC ATTTATATGA TGTAAAACTG ACTCCAAAAA TGAATGTTAC 4327 AATCAAATTG TCTATACTTT AT3ATAATGC TGAGTCTAAT GATAACTCAA TTGGTAAATG 4387 GACAAACACA AATATTGTTT C&GGTGGAAA TAACGGAAAA AAACAATATT CTTCTAATAA 4447 TCCGGATGCT AATTTGACAT TAAATACAGA TCCTCAAGAA AAATTAAATA AAAATCGTGA 4507 CTATTATATA AGTTTATATA TCAAGTCAGA AAAAAACACA CAATCTGAGA TTACTATAGA 4567 TGGGGAGATT TATCCGATCA CTACAAAAAC AGTCAATGTG AATAAAGACA ATTACAAAAG 4627 ATTAGATATT ATAGCTCATA ATATAAAAAG TAATCCAATT TCTTCACTTC ATATTAAAAC 4687 GAATGATGAA ATAACTTTAT TTTGGGATGA TATTTCTATA ACAGATGTAG CATCAATAAA 4747 ACCGGAAAAT TTAACAGATT CAGAAATTAA ACAGATTTAT AGTAGGTATG GTATTAAGTT 4807 AGAAGATGGA ATCCTTATTG ATAAAAAAGG TGGGATTCAT TATCGTGAAT TTATTAATGA 4867 AGCTAGTTTT AATATTGAAC CATTGCAAAA TTATGTGACC AAATATGAAG TTACTTATAG 4927 TAGTGAGTTA GGACCAAACG TGAGTGACAC ACTTGAAAGT GATAAAATTT ACAAGGATGG 4987 GACAATTAAA TTTGATTTTA CCAAATATAG TAAAAATGAA CAAGGATTAT TTTATGACAG 5047 TGGATTAAAT TC -GACTTTA AAATTAATGC TATTACTTAT GATGGTAAAG AGATGAATGT 5107 TTΓTCATAGA TATAATAAAT AGTTATTATA TCTATGAAGC TC _TGCTAAA GATAGTGTAA 5167 AAGTTAATAT A-JTCTAGGAT TGTAATAAAA GTAATGGAAT TGATATCGTA CTTTGGAGTG 5227 GGGGATACTT TCTAAATAGT TCTATCAGAA A-.ATTAGACT AAGAAAAGTT ACTACCCCCA 5287 CITGAAAATG AAGATTCAAC TGATTACAAA <_AACCTGTTA AATATTATAA GGTTTTAACA 5347 AAATATTAAA CTCTTTATGT TAATACTCTA ATATAAAGAG TTTAATTGTA TTCAAATGAA 5407 GCTITCCCAC AAAATTAGAC TGATTATCTA ATGAAATAAT CAGTCTAATT TTGTAGAACA 5467 GGTCTGGTAT TATTGTACGT GGTCACTAAA AGATATCTAA TATTATTGGG CAAGGCGTTC 5527 CATGATTGAA TCCTCGAATG TCTTGCCCTT TTCATTTATT TAAGAAGGAT TGTGGAGAAA 5587 TTATGCTTTA GATAATGAAG AAAGACTTCA CTTCTAATTT TTGATGTTAA ATAAATCAAA 5647 ATTTGGCGAT TCAl-ΑTTGTT TAATCCACTG ATAAAACATA CICGAGTGTT CTTAAAAAAT 5707 CAGCTTTTTT CTTTATAAAA TTTTGCTTAG CGTACGAAAT TCGTGTTTTG TTGGTGGGAC 5767 CCCATGCCCA TC-5-ACTTAAG AGTAAATTAG TAATGAACTT TCGTTCATCT GGATTAAAAT 5827 AACX-TCAAAT TAGGACATGT TTTTAAAAAT AAGCAGACCA AATAAGCCTA GAATAGGTAT 5887 CATTTTTAAA AATTATGCTG CTTTCTTTTG TTTTCCAAAT CCATTATACT CATAAGCAAC 5947 ACCCATAATG TCAAAGACTG TTTTTCTCTC ATATCGATAA GCTTGATATC GAATTCCTGC 6007 AGCCCGGGGG ATCCACTAGT TCTAGAGCGG CCGCCACCGC GG 6049 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 462 amino acids (B) TYPE: amino acid (D) ' TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu Gin 1 5 10 15 Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser He Ser Leu 20 25 30 Leu Asn Asn Glu Val He Lys Ala Glu Gin Leu Asn He Asn Ser Gin 35 40 45 Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu 50 55 60 Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys 65 70 75 80 Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn 85 90 95 Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr 100 105 110 Phe Ser Met Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu 115 120 125 He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr 130 135 140 Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr 145 150 155 160 Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin 165 170 175 Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 180 185 190 Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr 195 200 205 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He 210 215 220 Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val 225 230 235 240 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu 245 250 255 Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He 260 265 270 Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala 275 280 285 Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg 290 295 300 Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser 305 310 315 320 Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu 325 330 335 Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly 340 345 350 Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys 355 360 365 Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr 370 375 380 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg 385 390 395 400 Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr 405 410 415 Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp 420 425 430 Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He Lys 435 440 445 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 450 455 460 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LEM3TH: 20 amino acids (B) TYPE: amino acid (C) STRANDECNESS: single (D) TOPOLOGY: linear (ii) I iLECULE TYPE: peptide (ix) FEATURE: 35 - (A) NAME/KEY: Peptide (B) LOCATION: 1..20 (D) OTHER INFORMATION: /note= "Signal peptide for vacuolar targetting" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: Ser Ser Ser Ser Phe Ala Asp Ser Asn Pro He Arg Val Thr Asp Arg 1 5 10 15 Ala Ala Ser Thr 20 (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2655 base pairs (B) TYPE: nucleic acid (C) STRANDEE.NESS: single (D) TOPOLOGY: linear (ii) MOI-ECULE TYPE: DNA (genαmic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus cereus (B) STRAIN: AB78 (C) INDIVTEOAL ISOLATE: NRRL B-21058 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..2652 (D) OTHER INFORMATION: /product= "100 kDa protein VIPlA(a)' /note= "This sequence is identical to the portion of SEQ ID NO:l between and including nucleotide 2475 to 5126." (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: ATG AAA AAT ATG AAG AAA AAG TTA GCA AGT GTT GTA ACG TGT AOG TTA 48 Met Lys Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu 465 470 475 TTA GCT CCT ATG TTT TTG AAT GGA AAT GTG AAT GCT GTT TAC GCA GAC 96 Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Tyr Ala Asp 480 485 490 AGC AAA ACA AAT CAA ATT TCT ACA ACA CAG AAA AAT CAA CAG AAA GAG 144 Ser Lys Thr Asn Gin He Ser Thr Thr Gin Lys Asn Gin Gin Lys Glu 495 500 505 510 ATG GAC CGA AAA GGA TTA CTT GGG TAT TAT TTC AAA GGA AAA GAT TIT 192 Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 515 520 525 AGT AAT CTT ACT ATG TTT GCA CCG ACA CGT GAT AGT ACT CTT ATT TAT 240 Ser Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Ser Thr Leu He Tyr 530 535 540 GAT CAA CAA ACA GCA AAT AAA CTA TTA GAT AAA AAA CAA CAA GAA TAT 288 Asp Gin Gin Thr Ala Asn Lys Leu Leu Asp Lys Lys Gin Gin Glu Tyr 545 550 555 CAG TCT ATT CGT TGG ATT GGT TTG ATT CAG AGT AAA GAA ACG GGA GAT 336 Gin Ser He Arg Trp He Gly Leu He Gin Ser Lys Glu Ttir Gly Asp 560 565 570 TTC ACA TTT AAC TTA TCT GAG GAT GAA CAG GCA ATT ATA GAA ATC AAT 384 Phe Thr Phe Asn Leu Ser Glu Asp Glu Gin Ala He He Glu He Asn 575 580 585 590 GGG AAA ATT ATT TCT AAT AAA GGG AAA GAA AAG CAA GTT GTC CAT TTA 432 Gly Lys He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val His Leu 595 600 605 GAA AAA GGA AAA TTA GTT CCA ATC AAA ATA GAG TAT CAA TCA GAT ACA 480 Glu Lys Gly Lys Leu Val Pro He Lys He Glu Tyr Gin Ser Asp Thr 610 615 620 AAA TTT AAT ATT GAC AGT AAA ACA TTT AAA GAA CTT AAA TTA TTT AAA 528 Lys Phe Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu Phe Lys 625 630 635 ATA GAT AGT CAA AAC CAA CCC CAG CAA GTC CAG CAA GAT GAA CTG AGA 576 He Asp Ser Gin Asn Gin Pro Gin Gin Val Gin Gin Asp Glu Leu Arg 640 645 650 AAT CCT GAA TTT AAC AAG AAA GAA TCA CAG GAA TTC TTA GCG AAA CCA 624 Asn Pro Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Pro 655 660 665 670 TCG AAA ATA AAT CTT TTC ACT CAA AAA ATG AAA AGG GAA ATT GAT GAA 672 Ser Lys He Asn Leu Phe Thr Gin Lys Met Lys Arg Glu He Asp Glu 675 680 685 GAC ACG GAT ACG GAT GGG GAC TCT ATT CCT GAC CTT TGG GAA GAA AAT 720 Asp Thr Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn 690 695 700 GGG TAT ACG ATT CAA AAT AGA ATC GCT GTA AAG TGG GAC GAT TCT CTA 768 Gly Tyr Thr He Gin Asn Arg He Ala Val Lys Trp Asp Asp Ser Leu 705 710 715 GCA AGT AAA GGG TAT ACG AAA TTT GTT TCA AAT CCA CTA GAA AGT CAC 816 Ala Ser Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Glu Ser His 720 725 730 ACA GTT GGT GAT CCT TAT ACA GAT TAT GAA AAG GCA GCA AGA GAT CTA 864 Thr Val Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu 735 740 745 750 GAT TTG TCA AAT GCA AAG GAA ACG TTT AAC CCA TTG GTA GCT GCT TTT 912 Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe 755 760 765 CCA AGT GTG AAT GTT AGT ATG GAA AAG GTG ATA TTA TCA CCA AAT GAA 960 Pro Ser Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu 770 775 780 AAT TTA TCC AAT AGT GTA GAG TCT CAT TCA TCC ACG AAT TGG TCT TAT 1008 Asn Leu Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr 785 790 795 ACA AAT ACA GAA GGT GCT TCT GTT GAA GCG GGG ATT GGA CCA AAA GGT 1056 Thr Asn Thr Glu Gly Ala Ser Val Glu Ala Gly He Gly Pro Lys Gly 800 805 810 ATT TCG TTC GGA GTT AGC GTA AAC TAT CAA CAC TCT GAA ACA GTT GCA 1104 He Ser Phe Gly Val Ser Val Asn Tyr Gin His Ser Glu Tϊir Val Ala 815 820 825 830 CAA GAA TGG GGA ACA TCT ACA GGA AAT ACT TCG CAA TTC AAT ACG GCT 1152 Gin Glu Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala 835 840 845 TCA GCG GGA TAT TTA AAT GCA AAT GTT CGA TAT AAC AAT GTA GGA ACT 1200 Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr 850 855 860 GGT GCC ATC TAC GAT GTA AAA CCT ACA ACA AGT TTT GTA TTA AAT AAC 1248 Gly Ala He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn 865 870 875 GAT ACT ATC GCA ACT ATT ACG GCG AAA TCT AAT TCT ACA GCC TTA AAT 1296 Asp Thr He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Asn 880 885 890 ATA TCT CCT GGA GAA AGT TAC CCG AAA AAA GGA CAA AAT GGA ATC GCA 1344 He Ser Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gin Asn Gly He Ala 895 900 905 910 ATA ACA TCA ATG GAT GAT TTT AAT TCC CAT CCG ATT ACA TTA AAT AAA 1392 He Thr Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn"Lys 915 920 925 AAA CAA GTA GAT AAT CTG CTA AAT AAT AAA CCT ATG ATG TTG GAA ACA 1440 Lys Gin Val Asp Asn Leu Leu Asn Asn Lys Pro Met Met Leu Glu Thr 930 935 940 AAC CAA ACA GAT GGT GTT TAT AAG ATA AAA GAT ACA CAT GGA AAT ATA 1488 Asn Gin Thr Asp Gly Val Tyr Lys He Lys Asp Thr His Gly Asn He 945 950 955 GTA ACT GGC GGA GAA TGG AAT GGT GTC ATA CAA CAA ATC AAG GCT AAA 1536 Val Thr Gly Gly Glu Trp Asn Gly Val He Gin Gin He Lys Ala Lys 960 965 970 ACA GCG TCT ATT ATT GTG GAT GAT GGG GAA CCT GTA GCA GAA AAA CGT 1584 Thr Ala Ser He He Val Asp Asp Gly Glu Arg Val Ala Glu Lys Arg 975 980 985 990 CTA GCG GCA AAA GAT TAT GAA AAT CCA GAA GAT AAA ACA CCG TCT TTA 1632 Val Ala Ala Lys Asp Tyr Glu Asn Pro Glu Asp Lys Thr Pro Ser Leu 995 1000 1005 ACT TTA AAA GAT GCC CTG AAG CTT TCA TAT CCA GAT GAA ATA AAA GAA 1680 Thr Leu Lys Asp Ala Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu 1010 1015 1020 ATA GAG GGA TTA TTA TAT TAT AAA AAC AAA CCG ATA TAC GAA TCG AGC 1728 He Glu Gly Leu Leu Tyr Tyr Lys Asn Lys Pro He Tyr Glu Ser Ser 1025 1030 1035 GTT ATG ACT TAC TTA GAT GAA AAT ACA GCA AAA GAA GTG ACC AAA CAA 1776 Val Met Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Thr Lys Gin 1040 1045 1050 TTA AAT GAT ACC ACT GGG AAA TTT AAA GAT GTA AGT CAT TTA TAT GAT 1824 Leu Asn Asp Thr Thr Gly Lys Phe Lys Asp Val Ser His Leu Tyr Asp 1055 1060 1065 1070 GTA AAA CTG ACT CCA AAA ATG AAT GTT ACA ATC AAA TTG TCT ATA CTT 1872 Val Lys Leu Thr Pro Lys Met Asn Val Thr He Lys Leu Ser He Leu 1075 1080 1085 TAT GAT AAT GCT GAG TCT AAT GAT AAC TCA ATT GGT AAA TGG ACA AAC 1920 Tyr Asp Asn Ala Glu Ser Asn Asp Asn Ser He Gly Lys Trp Thr Asn 1090 1095 1100 ACA AAT ATT GTT TCA GGT GGA AAT AAC GGA AAA AAA CAA TAT TCT TCT 1968 Thr Asn He Val Ser Gly Gly Asn Asn Gly Lys Lys G n Tyr Ser Ser 1105 1110 1115 AAT AAT CCG GAT GCT AAT TTG ACA TTA AAT ACA GAT GCT CAA GAA AAA 2016 Asn Asn Pro Asp Ala Asn Leu Thr Leu Asn Thr Asp Ala Gin Glu Lys 1120 1125 1130 TTA AAT AAA AAT CGT GAC TAT TAT ATA AGT TTA TAT ATG AAG TCA GAA 2064 Leu Asn Lys Asn Arg Asp Tyr Tyr He Ser Leu Tyr Met Lys Ser Glu 1135 1140 1145 1150 AAA AAC ACA CAA TCT GAG ATT ACT ATA GAT GGG GAG ATT TAT CCG ATC 2112 Lys Asn Thr Gin Cys Glu He Thr He Asp Gly Glu He Tyr Pro He 1155 1160 1165 ACT ACA AAA ACA GTG AAT GTG AAT AAA GAC AAT TAC AAA AGA TTA GAT 2160 Thr Thr Lys Thr Val Asn Val Asn Lys Asp Asn Tyr Lys Arg Leu Asp 1170 1175 1180 ATT ATA GCT CAT AAT ATA AAA ACT AAT CCA ATT TCT TCA CTT CAT ATT 2208 He He Ala His Asn He Lys Ser Asn Pro He Ser Ser Leu His He 1185 1190 1195 AAA ACG AAT GAT GAA ATA ACT TTA TTT TGG GAT GAT ATT TCT ATA ACA 2256 Lys Thr Asn Asp Glu He Thr Leu Phe Trp Asp Asp He Ser He Thr 1200 1205 1210 GAT GTA GCA TCA ATA AAA CCG GAA AAT TTA ACA GAT TCA GAA ATT AAA 2304 Asp Val Ala Ser He Lys Pro Glu Asn Leu Thr Asp Ser Glu He Lys 1215 1220 1225 1230 CAG ATT TAT AGT AGG TAT GGT ATT AAG TTA GAA GAT GGA ATC CTT ATT 2352 Gin He Tyr Ser Arg Tyr Gly He Lys Leu Glu Asp Gly He Leu He 1235 1240 1245 GAT AAA AAA GGT GGG ATT CAT TAT GGT GAA TTT ATT AAT GAA GCT ACT 2400 Asp Lys Lys Gly Gly He His Tyr Gly Glu Phe He Asn Glu Ala Ser 1250 1255 1260 TTT AAT ATT GAA CCA TTG CAA AAT TAT GTG ACC AAA TAT GAA GTT ACT 2448 Phe Asn He Glu Pro Leu Gin Asn Tyr Val Thr Lys Tyr Glu Val Thr 1265 1270 1275 TAT AGT AGT GAG TTA GGA CCA AAC GTG ACT GAC ACA CTT GAA AGT GAT 2496 Tyr Ser Ser Glu Leu Gly Pro Asn Veil Ser Asp Thr Leu Glu Ser Asp 1280 1285 1290 AAA ATT TAC AAG GAT GGG ACA ATT AAA TTT GAT TTT ACC AAA TAT AGT 2544 Lys He Tyr Lys Asp Gly Thr He Lys Phe Asp Phe Thr Lys Tyr Ser 1295 1300 1305 1310 AAA AAT GAA CAA GGA TTA TTT TAT GAC AGT GGA TTA AAT TGG GAC TTT 2592 Lys Asn Glu Gin Gly Leu Phe Tyr Asp Ser Gly Leu Asn Trp Asp Phe 1315 1320 1325 AAA ATT AAT GCT ATT ACT TAT GAT GCT AAA GAG ATG AAT GTT TTT CAT 2640 Lys He Asn Ala He Thr Tyr Asp Gly Lys Glu Met Asn Val Phe His 1330 1335 1340 AGA TAT AAT AAA TAG 2655 Arg Tyr Asn Lys 1345 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 884 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Met Lys Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu 1 5 10 15 Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Tyr Ala Asp 20 25 30 Ser Lys Thr Asn Gin He Ser Thr Thr Gin Lys Asn Gin Gin Lys Glu 35 40 45 Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 50 55 60 Ser Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Ser Thr Leu He Tyr 65 70 75 80 Asp Gin Gin Thr Ala Asn Lys Leu Leu Asp Lys Lys Gin Gin Glu Tyr 85 90 95 Gin Ser He Arg Trp He Gly Leu He Gin Ser Lys Glu Thr Gly Asp 100 105 110 Phe Thr Phe Asn Leu Ser Glu Asp Glu Gin Ala He He Glu He Asn 115 120 125 Gly Lys He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val His Leu 130 135 140 Glu Lys Gly Lys Leu Val Pro He Lys He Glu Tyr Gin Ser Asp Thr 145 150 155 160 Lys Phe Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu Phe Lys 165 170 175 He Asp Ser Gin Asn Gin Pro Gin Gin Val Gin Gin Asp Glu Leu Arg 180 185 190 Asn Pro Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Pro 195 200 205 Ser Lys He Asn Leu Phe Thr Gin Lys Met Lys Arg Glu He Asp Glu 210 215 220 Asp Thr Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn 225 230 235 240 Gly Tyr Thr He Gin Asn Arg He Ala Val Lys Trp Asp Asp Ser Leu 245 250 255 Ala Ser Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Glu Ser His 260 265 270 Thr Val Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu 275 280 285 Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe 290 295 300 Pro Ser Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu 305 310 315 320 Asn Leu Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr 325 330 335 Thr Asn Thr Glu Gly Ala Ser Val Glu Ala Gly He Gly Pro Lys Gly 340 345 350 He Ser Phe Gly Val Ser Val Asn Tyr Gin His Ser Glu Thr Val Ala 355 360 365 Gin Glu Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala 370 375 380 Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg Ty Asn Asn Val Gly Thr 385 390 395 400 Gly Ala He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn 405 410 415 Asp Thr He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Asn 420 425 430 He Ser Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gin Asn Gly He Ala 435 440 445 He Thr Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn Lys 450 455 460 Lys Gin Val Asp Asn Leu Leu Asn Asn Lys Pro Met Met Leu Glu Thr 465 470 475 480 Asn Gin Thr Asp Gly Val Tyr Lys He Lys Asp Thr His Gly Asn He 485 490 495 Val Thr Gly Gly Glu Trp Asn Gly Val He Gin Gin He Lys Ala Lys 500 505 510 Thr Ala Ser He He Val Asp Asp Gly Glu Arg Val Ala Glu Lys Arg 515 520 525 Val Ala Ala Lys Asp Tyr Glu Asn Pro Glu Asp Lys Thr Pro Ser Leu 530 535 540 Thr Leu Lys Asp Ala Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu 545 550 555 560 He Glu Gly Leu Leu Tyr Tyr Lys Asn Lys Pro He Tyr Glu Ser Ser 565 570 575 Val Met Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Thr Lys Gin 580 585 590 Leu Asn Asp Thr Thr Gly Lys Phe Lys Asp Val Ser His Leu Tyr Asp 595 600 605 Val Lys Leu Thr Pro Lys Met Asn Val Thr He Lys Leu Ser He Leu 610 615 620 Tyr Asp Asn Ala Glu Ser Asn Asp Asn Ser He Gly Lys Trp Thr Asn 625 630 635 640 Thr Asn He Val Ser Gly Gly Asn Asn Gly Lys Lys Gin Tyr Ser Ser 645 650 655 Asn Asn Pro Asp Ala Asn Leu Thr Leu Asn Thr Asp Ala Gin Glu Lys 660 665 670 Leu Asn Lys Asn Arg Asp Tyr Tyr He Ser Leu Tyr Met Lys Ser Glu 675 680 685 Lys Asn Thr Gin Cys Glu He Thr He Asp Gly Glu He Tyr Pro He 690 695 700 Thr Thr Lys Thr Val Asn Val Asn Lys Asp Asn Tyr Lys Arg Leu Asp 705 710 715 720 He He Ala His Asn He Lys Ser Asn Pro He Ser Ser Leu His He 725 730 735 Lys Thr Asn Asp Glu He Thr Leu Phe Trp Asp Asp He Ser He Thr 740 745 750 Asp Val Ala Ser He Lys Pro Glu Asn Leu Thr Asp Ser Glu He Lys 755 760 765 Gin He Tyr Ser Arg Tyr Gly He Lys Leu Glu Asp Gly He Leu He 770 775 780 Asp Lys Lys Gly Gly He His Tyr Gly Glu Phe He Asn Glu Ala Ser 785 790 795 800 Phe Asn He Glu Pro Leu Gin Asn Tyr Val Thr Lys Tyr Glu Val Thr 805 810 815 Tyr Ser Ser Glu Leu Gly Pro Asn Val Ser Asp Thr Leu Glu Ser Asp 820 825 830 Lys He Tyr Lys Asp Gly Thr He Lys Phe Asp Phe Thr Lys Tyr Ser 835 840 845 Lys Asn Glu Gin Gly Leu Phe Tyr Asp Ser Gly Leu Asn Trp Asp Phe 850 855 860 Lys He Asn Ala He Thr Tyr Asp Gly Lys Glu Met Asn Val Phe His 865 870 875 880 Arg Tyr Asn Lys (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2004 base pairs (B) TYPE: nucleic acid (C) STOANDEE-NESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: ENA (genomic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus cereus (B) STRAIN: AB78 (C) INDIVIDUAL ISOLATE: NRRL B-21058 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..2001 (D) OTHER INFORMATION: /product= "80 kDa protein VTPlA(a) " /note= "This sequence is identical to that found in SEQ ID NO:l between and including nucleotide positions 3126 and 5126" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6: ATG AAA AGG GAA ATT GAT GAA GAC ACG GAT ACG GAT GGG GAC TCT ATT 48 Met Lys Arg Glu He Asp Glu Asp Thr Asp Thr Asp Gly Asp Ser He 885 890 895 900 CCT GAC CTT TGG GAA GAA AAT GGG TAT ACG ATT CAA AAT AGA ATC GCT 96 Pro Asp Leu Trp Glu Glu Asn Gly Tyr Thr He Gin Asn Arg He Ala 905 910 915 CTA AAG TGG GAC GAT TCT CTA GCA AGT AAA GGG TAT ACG AAA TTT GTT 144 Val Lys Trp Asp Asp Ser Leu Ala Ser Lys Gly Tyr Thr Lys Phe Val 920 925 930 TCA AAT CCA CTA GAA AGT CAC ACA GTT GGT GAT CCT TAT ACA GAT TAT 192 Ser Asn Pro Leu Glu Ser His Thr Val Gly Asp Pro Tyr Thr Asp Tyr 935 940 945 GAA AAG GCA GCA AGA GAT CTA GAT TTG TCA AAT GCA AAG GAA ACG TTT 240 Glu Lys Ala Ala Arg Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr Phe 950 955 960 AAC CCA TTG GTA GCT GCT TTT CCA AGT GTG AAT GTT AGT ATG GAA AAG 288 Asn Pro Leu Val Ala Ala Phe Pro Ser Val Asn Val Ser Met Glu Lys 965 970 975 980 GTG ATA TTA TCA CCA AAT GAA AAT TTA TCC AAT AGT GTA GAG TCT CAT 336 Val He Leu Ser Pro Asn Glu Asn Leu Ser Asn Ser Val Glu Ser His 985 990 995 TCA TCC ACG AAT TGG TCT TAT ACA AAT ACA GAA GGT GCT TCT GTT GAA 384 Ser Ser Thr Asn Trp Ser Tyr Thr Asn Thr Glu Gly Ala Ser Val Glu 1000 1005 1010 GCG GGG ATT GGA CCA AAA GCT ATT TCG TTC GGA GTT AGC GTA AAC TAT 432 Ala Gly He Gly Pro Lys Gly He Ser Phe Gly Val Ser Val Asn Tyr 1015 1020 1025 CAA CAC TCT GAA ACA GTT GCA CAA GAA TGG GGA ACA TCT ACA GGA AAT 480 Gin His Ser Glu Thr Val Ala Gin Glu Trp Gly Thr Ser Thr Gly Asn 1030 1035 1040 ACT TCG CAA TTC AAT ACG GCT TCA GCG GGA TAT TTA AAT GCA AAT GTT 528 Thr Ser Gin Phe Asn Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn Val 1045 1050 1055 1060 CGA TAT AAC AAT GTA GGA ACT GGT GCC ATC TAC GAT GTA AAA CCT ACA 576 Arg Tyr Asn Asn Val Gly Thr Gly Ala He Tyr Asp Val Lys Pro Thr 1065 1070 1075 ACA AGT TTT GTA TTA AAT AAC GAT ACT ATC GCA ACT ATT ACG GCG AAA 624 Thr Ser Phe Veil Leu Asn Asn Asp Thr He Ala Thr He Thr Ala Lys 1080 1085 1090 TCT AAT TCT ACA GCC TTA AAT ATA TCT CCT GGA GAA AGT TAC CCG AAA 672 Ser Asn Ser Thr Ala Leu Asn He Ser Pro Gly Glu Ser Tyr Pro Lys 1095 1100 1105 AAA GGA CAA AAT GGA ATC GCA ATA ACA TCA ATG GAT GAT TTT AAT TCC 720 Lys Gly Gin Asn Gly He Ala He Thr Ser Met Asp Asp Phe Asn Ser 1110 1115 1120 CAT CCG ATT ACA TTA AAT AAA AAA CAA CTA GAT AAT CTG CTA AAT AAT 768 His Pro He Thr Leu Asn Lys Lys Gin Val Asp Asn Leu Leu Asn Asn 1125 1130 1135 1140 AAA CCT ATG ATG TTG GAA ACA AAC CAA ACA GAT GGT GTT TAT AAG ATA 816 Lys Pro Met Met Leu Glu Thr Asn Gin Thr Asp Gly Val Tyr Lys He 1145 1150 1155 AAA GAT ACA CAT GGA AAT ATA GTA ACT GGC GGA GAA TGG AAT GGT GTC 864 Lys Asp Thr His Gly Asn He Val Thr Gly Gly Glu Trp Asn Gly Val 1160 1165 1170 ATA CAA CAA ATC AAG GCT AAA ACA GCG TCT ATT ATT CTG GAT GAT GGG 912 He Gin Gin He Lys Ala Lys Thr Ala Ser He He Val Asp Asp Gly 1175 1180 1185 GAA CGT GTA GCA GAA AAA CGT GTA GCG GCA AAA GAT TAT GAA AAT CCA 960 Glu Arg Val Ala Glu Lys Arg Val Ala Ala Lys Asp Tyr Glu Asn Pro 1190 1195 1200 GAA GAT AAA ACA CCG TCT TTA ACT TTA AAA GAT GCC CTG AAG CTT TCA 1008 Glu Asp Lys Thr Pro Ser Leu Thr Leu Lys Asp Ala Leu Lys Leu Ser 1205 1210 1215 1220 TAT CCA GAT GAA ATA AAA GAA ATA GAG GGA TTA TTA TAT TAT AAA AAC 1056 Tyr Pro Asp Glu He Lys Glu He Glu Gly Leu Leu Tyr Tyr Lys Asn 1225 1230 1235 AAA CCG ATA TAC GAA TCG AGC GTT ATS ACT TAC TTA GAT GAA AAT ACA 1104 Lys Pro He Tyr Glu Ser Ser Val Met Thr Tyr Leu Asp Glu Asn Thr 1240 1245 1250 GCA AAA GAA GTG ACC AAA CAA TTA AAT GAT ACC ACT GGG AAA TTT AAA 1152 Ala Lys Glu Val Thr Lys Gin Leu Asn Asp Thr Thr Gly Lys Phe Lys 1255 1260 1265 GAT GTA AGT CAT TTA TAT GAT GTA AAA CTG ACT CCA AAA ATG AAT GTT 1200 Asp Val Ser His Leu Tyr Asp Val Lys Leu Thr Pro Lys Met Asn Val 1270 1275 1280 ACA ATC AAA TTG TCT ATA CTT TAT GAT AAT GCT GAG TCT AAT GAT AAC 1248 Thr He Lys Leu Ser He Leu Tyr Asp Asn Ala Glu Ser Asn Asp Asn 1285 1290 1295 1300 TCA ATT GGT AAA TGG ACA AAC ACA AAT ATT GTT TCA GCT GGA AAT AAC 1296 Ser He Gly Lys Trp Thr Asn Thr Asn He Val Ser Gly Gly Asn Asn 1305 1310 1315 GGA AAA AAA CAA TAT TCT TCT AAT AAT CCG GAT GCT AAT TTG ACA TTA 1344 Gly Lys Lys Gin Tyr Ser Ser Asn Asn Pro Asp Ala Asn Leu Thr Leu 1320 1325 1330 AAT ACA GAT GCT CAA GAA AAA TTA AAT AAA AAT CCT GAC TAT TAT ATA 1392 Asn Thr Asp Ala Gin Glu Lys Leu Asn Lys Asn Arg Asp Tyr Tyr He 1335 1340 1345 AGT TTA TAT ATG AAG TCA GAA AAA AAC ACA CAA TCT GAG ATT ACT ATA 1440 Ser Leu Tyr Met Lys Ser Glu Lys Asn Thr Gin Cys Glu He Thr He 1350 1355 1360 GAT GGG GAG ATT TAT CCG ATC ACT ACA AAA ACA GTG AAT GTG AAT AAA 1488 Asp Gly Glu He Tyr Pro He Thr Thr Lys Thr Val Asn Val Asn Lys 1365 1370 1375 1380 GAC AAT TAC AAA AGA TTA GAT ATT ATA GCT CAT AAT ATA AAA AGT AAT 1536 Asp Asn Tyr Lys Arg Leu Asp He He Ala His Asn He Lys Ser Asn 1385 1390 1395 CCA ATT TCT TCA CTT CAT ATT AAA ACG AAT GAT GAA ATA ACT TTA TTT 1584 Pro He Ser Ser Leu His He Lys Thr Asn Asp Glu He Thr Leu Phe 1400 1405 1410 TGG GAT GAT ATT TCT ATA ACA GAT CTA GCA TCA ATA AAA CCG GAA AAT 1632 Trp Asp Asp He Ser He Thr Asp Val Ala Ser He Lys Pro Glu Asn 1415 1420 1425 TTA ACA GAT TCA GAA ATT AAA CAG ATT TAT ACT AGG TAT GCT ATT AAG 1680 Leu Thr Asp Ser Glu He Lys Gin He Tyr Ser Arg Tyr Gly He Lys 1430 1435 1440 TTA GAA GAT GGA ATC CTT ATT GAT AAA AAA GGT GGG ATT CAT TAT GGT 1728 Leu Glu Asp Gly He Leu He Asp Lys Lys Gly Gly He His Tyr Gly 1445 1450 1455 1460 GAA TTT ATT AAT GAA GCT AGT TTT AAT ATT GAA CCA TTG CCA AAT TAT 1776 Glu Phe He Asn Glu Ala Ser Phe Asn He Glu Pro Leu Pro Asn Tyr 1465 1470 1475 GTG ACC AAA TAT GAA GTT ACT TAT AGT AGT GAG TTA GGA CCA AAC GTG 1824 Val Thr Lys Tyr Glu Val Thr Tyr Ser Ser Glu Leu Gly Pro Asn Val 1480 1485 1490 AGT GAC ACA CTT GAA AGT GAT AAA ATT TAC AAG GAT GGG ACA ATT AAA 1872 Ser Asp Thr Leu Glu Ser Asp Lys He Tyr Lys Asp Gly Thr He Lys 1495 1500 1505 TTT GAT TTT ACC AAA TAT ACT AAA AAT GAA CAA GGA TTA TTT TAT GAC 1920 Phe Asp Phe Thr Lys Tyr Ser Lys Asn Glu Gin Gly Leu Phe Tyr Asp 1510 1515 1520 ACT GGA TTA AAT TGG GAC TTT AAA ATT AAT GCT ATT ACT TAT GAT GGT 1968 Ser Gly Leu Asn Trp Asp Phe Lys He Asn Ala He Thr Tyr Asp Gly 1525 1530 1535 1540 AAA GAG ATG AAT GTT TTT CAT AGA TAT AAT AAA TAG 2004 Lys Glu Met Asn Val Phe His Arg Tyr Asn Lys 1545 1550 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 667 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) IO ECULE. TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: Met Lys Arg Glu He Asp Glu Asp Thr Asp Thr Asp Gly Asp Ser He 1 5 10 15 Pro Asp Leu Trp Glu Glu Asn Gly Tyr Thr He Gin Asn Arg He Ala 20 25 30 Val Lys Trp Asp Asp Ser Leu Ala Ser Lys Gly Tyr Thr Lys Phe Val 35 40 45 Ser Asn Pro Leu Glu Ser His Thr Val Gly Asp Pro Tyr Thr Asp Tyr 50 55 60 Glu Lys Ala Ala Arg Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr Phe 65 70 75 80 Asn Pro Leu Val Ala Ala Phe Pro Ser Val Asn Val Ser Met Glu Lys 85 90 95 Val He Leu Ser Pro Asn Glu Asn Leu Ser Asn Ser Val Glu Ser His 100 105 110 Ser Ser Thr Asn Trp Ser Tyr Thr Asn Thr Glu Gly Ala Ser Val Glu 115 120 125 Ala Gly He Gly Pro Lys Gly He Ser Phe Gly Val Ser Val Asn Tyr 130 135 140 Gin His Ser Glu Thr Val Ala Gin Glu Trp Gly Thr Ser Thr Gly Asn 145 150 155 160 Thr Ser Gin Phe Asn Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn Val 165 170 175 Arg Tyr Asn Asn Val Gly Thr Gly Ala He Tyr Asp Val Lys Pro Thr 180 185 190 Thr Ser Phe Val Leu Asn Asn Asp Thr He Ala Thr He Thr Ala Lys 195 200 205 Ser Asn Ser Thr Ala Leu Asn He Ser Pro Gly Glu Ser Tyr Pro Lys 210 215 220 Lys Gly Gin Asn Gly He Ala He Thr Ser Met Asp Asp Phe Asn Ser 225 230 235 240 His Pro He Thr Leu Asn Lys Lys Gin Val Asp Asn Leu Leu Asn Asn 245 250 255 Lys Pro Met Met Leu Glu Thr Asn Gin Thr Asp Gly Val Tyr Lys He 260 265 270 Lys Asp Thr His Gly Asn He Val Thr Gly Gly Glu Trp Asn Gly Val 275 280 285 He Gin Gin He Lys Ala Lys Thr Ala Ser He He Val Asp Asp Gly 290 295 300 Glu Arg Val Ala Glu Lys Arg Val Ala Ala Lys Asp Tyr Glu Asn Pro 305 310 315 320 Glu Asp Lys Thr Pro Ser Leu Thr Leu Lys Asp Ala Leu Lys Leu Ser 325 330 335 Tyr Pro Asp Glu He Lys Glu He Glu Gly Leu Leu Tyr Tyr Lys Asn 340 345 350 Lys Pro He Tyr Glu Ser Ser Val Met Thr Tyr Leu Asp Glu Asn Thr 355 360 365 Ala Lys Glu Val Thr Lys Gin Leu Asn Asp Thr Thr Gly Lys Phe Lys 370 375 380 Asp Val Ser His Leu Tyr Asp Val Lys Leu Thr Pro Lys Met Asn Val 385 390 395 400 Thr He Lys Leu Ser He Leu Tyr Asp Asn Ala Glu Ser Asn Asp Asn 405 410 415 Ser He Gly Lys Trp Thr Asn Thr Asn He Val Ser Gly Gly Asn Asn 420 425 430 Gly Lys Lys Gin Tyr Ser Ser Asn Asn Pro Asp Ala Asn Leu Thr Leu 435 440 445 Asn Thr Asp Ala Gin Glu Lys Leu Asn Lys Asn Arg Asp Tyr Tyr He 450 455 460 Ser Leu Tyr Met Lys Ser Glu Lys Asn Thr Gin Cys Glu He Thr He 465 470 475 480 Asp Gly Glu He Tyr Pro He Thr Thr Lys Thr Val Asn Val Asn Lys 485 490 495 Asp Asn Tyr Lys Arg Leu Asp He He Ala His Asn He Lys Ser Asn 500 505 510 Pro He Ser Ser Leu His He Lys Thr Asn Asp Glu He Thr Leu Phe 515 520 525 Trp Asp Asp He Ser He Thr Asp Val Ala Ser He Lys Pro Glu Asn 530 535 540 Leu Thr Asp Ser Glu He Lys Gin He Tyr Ser Arg Tyr Gly He Lys 545 550 555 560 Leu Glu Asp Gly He Leu He Asp Lys Lys Gly Gly He His Tyr Gly 565 570 575 Glu Phe He Asn Glu Ala Ser Phe Asn He Glu Pro Leu Pro Asn Tyr 580 585 590 Val Thr Lys Tyr Glu Val Thr Tyr Ser Ser Glu Leu Gly Pro Asn Val 595 600 605 Ser Asp Thr Leu Glu Ser Asp Lys He Tyr Lys Asp Gly Thr He Lys 610 615 620 Phe Asp Phe Thr Lys Tyr Ser Lys Asn Glu Gin Gly Leu Phe Tyr Asp 625 630 635 640 Ser Gly Leu Asn Trp Asp Phe Lys He Asn Ala He Thr Tyr Asp Gly 645 650 655 Lys Glu Met Asn Val Phe His Arg Tyr Asn Lys 660 665 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) M0L-3CULE TYPE: peptide (iii) HYPOTHETICAL: NO (v) FRAGMENT TYPE: N-terminal (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus cereus (B) STRAIN: AB78 (C) INDIVIDUAL ISOLATE: NRRL B-21058 (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATION: 1..16 (D) OTHER INFORMATION: /note= "N-terminal sequence of protein purified from strain AB78" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Lys Arg Glu He Asp Glu Asp Thr Asp Thr Asx Gly Asp Ser He Pro 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) --TRANDEI-NESS: single (D) TOPOLOGY: linear (ii) MOI-J-CULE TYPE : EΪIA (genomic) (iii ) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (ix) FEATURE: (A) NAME/KEY: misc__feature (B) LOCATION: 1..21 (D) OTHER INFORMATION: /note= "Oligonucleotide probe based on amino acids 3 to 9 of SEQ ID NO:8, using codon usage of Bacillus thuringiensis" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9: GAAATTGATC AAGATACNGA T 21 (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE OiARACTERISTICS: (A) LEN3TH: 14 amino acids (B) TYPE: amino acid (C) STRANDET-NESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (v) FRAGMENT TYPE: N-terrr rial (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus thuringiensis (B) STRAIN: AB88 (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATICN: 1..14 (D) OTHER INFORMATION: /note= "N-terminal amino acid sequence of protein known as anion exchange fraction 23 (smaller) " (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Xaa Glu Pro Phe Val Ser Ala Xaa Xaa Xaa Gin Xaa Xaa Xaa 1 5 10 (2) INFORMATION FOR SEQ ID NO:11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 -utiino acids (B) TYPE: amino acid (C) STRANDEE-NESS: single (D) TOPOLOGY: N-terminal (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus thuringiensis (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11: Xaa Glu Tyr Glu Asn Val Glu Pro Phe Val Ser Ala Xaa 1 5 10 (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE C-HARACTERISTICS: (A) L-EN3TΗ: 14 amino acids (B) TYPE: amino acid (C) STRANDEI-NESS: single (D) TOPOLOGY: N-terminal (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus thurigiensis (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: Met Asn Lys Asn Asn Thr Lys Leu Pro Thr Arg Ala Leu Pro 1 5 10 (2) INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) M ECULE TYPE: peptide (iii) HYPOTHETICAL: NO (v) FRAGMENT TYPE: N-terminal (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus thuringiensis (B) STRAIN: AB88 (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATION: 1..15 (D) OTHER INFORMATION: /note= "N-terminal amino acid sequence of 35 kDa VIP active against Agrotis ipsilon" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 13 : Ala Leu Ser Glu Asn Thr Gly Lys Asp Gly Gly Tyr He Val Pro 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEENESS: single (D) TOPOLOGY: N-termirial (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus thuringiensis (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: Met Asp Asn Asn Pro Asn He Asn Glu 1 5 (2) INFORMATION FOR SEQ ID N0:15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) l^LE-U E TYPE: peptide (iii) HYPOTHETICAL: NO (v) FRAGMENT TYPE: N-te__minal (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATION: 1..9 (D) OTHER INFORMATION: /note= "N-terminal sequence of 80 kDa delta-endotoxin" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:15: Met Asp Asn Asn Pro Asn He Asn Glu 1 5 (2) INFORMATION FOR SEQ ID NO:16: (i) SEQUENCE CHARACTERISTICS: (A) LE-MGTH: 11 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii ) MOI-ECULE TYPE: peptide (iii) HYPOTHETICAL : NO (v) FRAGMENT TYPE : N-te inal (vi) ORIGINAL SOURCE: (A) ORGANISM: Bacillus thuringiensis (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATION: 1..11 (D) OTHER INFORMATION: /note= "N-terminal sequence from 60 kDa delta-endotoxin" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16: Met Asn Val Leu Asn Ser Gly Arg Thr Thr He 1 5 10 (2) INFORMATION FOR SEQ ID NO:17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2655 base pairs (B) TYPE: nucleic acid (C) STRANDEE-NESS: single (D) TOPOLOGY: linear (ii) I lLECULE TYPE: ENA (genomic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (ix) FEATURE: (A) NAME/KEY: misc_feature (B) LOCATION: 1..2652 (D) OTHER INFORMATION: /note= "Maize optimized ENA sequence for 100 kd VTPlA(a) protein from AB78" ( i) SEQUENCE DESCRIPTION: SEQ ID NO:17: ATGAAGAACA TGAAGAAGAA GCTGGCCAGC GTOGTCACCT GCACCCTGCT GGCCCCCATC 60 TTCCTGAACG GCAACGTGAA CX_CXX_TGTAC GCCGACAGCA AGACCAACCA GATCAGCACC 120 ACCCAGAAGA ACCAGCAGAA GGAGATGGAC CGCAAGGGCC TGCTGGGCTA CTACTTCAAG 180 GGCAAGGACT TCAGCAACCT GACCATGTTC GCCCCCACGC GTGACAGCAC CCTGATCTAC 240 GACCAGCAGA CCG CAACAA GCTGCTGGAC AAGAAGCAGC AGGAGTACCA GAGCATCCGC 300 TGGATCGGCC TCATCCAGAG CAAGGAGACC GGCXSACTTCA CCTTCAACCT GAGCGAGGAC 360 GAGCAGGCCA TCATCGAGAT CAACGGCAAG ATCATCAGCA ACAAGGGCAA GGAGAAGCAG 420 GTCGTGCACC TGGAGAAGGG CAAGCTQGTG CX-CATCAAGA TCGAGTACCA GAGCGACACC 480 AAGTTCAACA TCGACAGCAA GACCTTCAAG GAGCTGAAGC TTTTCAAGAT CGACAGCCAG 540 AACCAGCCCC AGCAGK3TGCA GCAGGACGAG C-TO-GCAACC CCGAGTTCAA (.AAGAAGGAG 600 AGCCAGGACT TCCTGGCCAA GCCCAGCAAG ATCAACCTCT TCACCCAGCA GATCAAGCGC 660 GAGATCGACG AGGACACCGA CACCGACGGC GAC1AGCATCC CCGACCTGTG GGAGGAGAAC 720 GGCTACACCA TCCAGAACCG CATCGCCGTG AAGTCGGACG ACAGCCTGGC TAGCAAGGGC 780 TACACCAAGT TCGTGAGCAA CCCCCTGGAG AGCCACACCG TX_α_X_X_ACCC CTACACCGAC- 840 TAD3AGAAGG CCX3-XX-GCGA CC GGACCTG AGCAACGCCA AGGAGACCTT CAACOCCCTG 900 GTGCCCGCCT TCCCCAGCCT GAACGTGAGC ATQGAGAAGG TGATCCTGAG CCCCAACGAG 960 AACCTGAGCA AC.AGCGTGGA GAGCCACTCG AGCACCAACT GGAGCTACAC CAACACCGAG 1020 GGCGCCAGCG TC<_AGGCCGG CATCGGTCCC AAGGGCATCA GCTTCGGCGT GAGCGTGAAC 1080 TACCAGCACA GO-AGACCCT GC3CCCAGGAG TGGGGCACCA GCACCGQCAA CACCAGCCAG 1140 TTCAACACCG CCAGCGCCGG CTACCTGAAC GCCAACGTGC GCTACAACAA CGTX.GGCACC 1200 QGCGCCATCT ACX-ACGTGAA GCCCACCACC AGCTTCGTGC TGAACAACGA CACCATCGCC 1260 ACCATCACCG CCAAGTCGAA TTCCACCGCC CTGAACATCA GCCCCCiGCGA GAGCTACCCC 1320 AAGAAGGGCC AGAACGGCAT O-CCATCACC AGCATGGACG ACTTCAACAG CCACCCCATC 1380 ACCCTGAACA AGAAGCAGGT GGAC.AACCTG CTGAACAACA AGCCCATGAT GCTQGAGACC 1440 AACCAGACCG ACX.GCGTCTA CAAGATCAAG GACACCCACG GCAACATCCT GACCQGCGGC 1500 GAGTCGAACG GCGTGATCCA GCAGATCAAG GCCAAGACCG CCAGCATCAT CGTCGACGAC 1560 GGCGAGCGCG TGGCCGAGAA GCGCGTGGCC GCCAAGGACT ACGAGAACCC O-AGGACAAG 1620 ACCCCCAGCC TGACCCTGAA GC^CGCCCTG AAGCTGAGCT ACCCCGACGA GATCAAGGAG 1680 ATCGAGGGCC TCCTCTACTA CAAGAACAAG CCCATCTACG AGAGCAGCGT GATGACCTAT 1740 CTAGACGAGA ACACCGCCAA GGAGGTGACC AAGCAGCTGA ACGACACCAC OIX-CAAGTTC 1800 AAGGACGTGA GC.CACCTGTA CGACGTGAAG CTGACCCCCA AGATGAACCT GACCATCAAG 1860 CTCΆGCATCC TCTACGACAA CGCCGAGAGC AACGACAACA GCATCGGCAA GTGGACCAAC 1920 ACCAACATCG TGAGCGGCGG CAACAACGGC AAGAAGCAGT ACAGCAGCAA CΑACCCCGAC 1980 GCC-AACCTGA CCCTGAACAC CGACGCCCAG GAGAAGCTGA ACAAGAACCG CGACTACTAC 2040 ATCAGCCTGT ACATGAAGAG CGAGAAGAAC ACCCAGTGCG AGATCACCAT CGACGGCGAG 2100 ATATACCCCA TCACCACCAA GkCCQTGΑAC GTGAACAAGG ACAACTACAA GCGCCTGGAC 2160 ATCATCGCCC ACAACATCAA GAGCAACCCC ATCAGCAGCC TGCACATCAA C_ACCAACGAC 2220 GAGATCACCC TCTTCTGGGA CGACATATCG ATTACCGACG TCGCCAGCAT CAAGCCCGAG 2280 AACCTGACCG ACAGCGAGAT CAAGCAGATA TACAGTCGCT ACGGCATCAA GCTGGAGGAC 2340 GGCATCCTGA TCGACAAGAA GGGCCGCATC CACTACGGCG AGTTCATCAA CGAGGCCAGC 2400 TTCAACATCG AGCCCCTGCA GAACTACGTG ACCAACTACG AGGTGACCTA CAGCAGCGAG 2460 CTGGGCCCCA ACGTGAGCGA CACCCTGGAG AGCGACAAGA TTTACAAGGA CGGCACCATC 2520 AAGTTCGACT TCACCAACTA CAGCAAGAAC GAGCAGGGCC TGTTCTACGA CAGCGGCCTG 2580 AACTGGGACT TCAAGATCAA CX-CCATCACC TACGACGGCA AGGAGATGAA α_TGTTCCAC 2640 CGCTACAACA AGTAG 2655 (2 ) INFORMATION FOR SEQ ID NO: 18 : (i ) SEQUENCE CHARACTERISTICS : (A) LE_SK_TH: 2004 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS : single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: I_NA (genαmic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (ix) FEATURE: (A) NAME/KEY: misc_feature (B) LOCATION: 1..2004 (D) OTHER INFORMATION: /note= "Maize optimized ENA sequence for VTPlA(a) 80 kd protein from AB78" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: ATCAAGCGCG AGATCGACGA GGACACCGAC ACCGACGGCG ACAGCATCCC O-ACCTGTGG 60 GAGGAGAACG GCTACACCAT CCAGAACCGC ATCGCCGTCA AGTGGGACGA CAGCCTGGCT 120 AGCAAGGGCT ACACCAAGTT ( -X-TGAGCAAC CCCCTCGAGA GCCACACCGT GGGCGACCCC 180 TACACCGACT ACGAGAAGGC CGCCCGCGAC CTCGACCTGA GCAACGCCAA GGAGACCTTC 240 AACCCCCTGG TX-X3-X-X3CCTT CCCCAGCGTG AACGTGAGCA Tra_AGAAGCT GATCCTGAGC 300 CCCAACGAGA ACCTGAGCAA CAGCGTGGAG AGCCACTCGA GCACCAACTG GAGCTACACC 360 AACACCGAGG GCGCCAGCGT GGAGGCCGGC ATCGGTCCCA AGGGCATCAG CTTCGGCGTG 420 AGCGTGAACT AC-CAGCACAG OC-AGACOGTG GCCCAGGACT GGGGCACCAG CA__C«_K_AAC 480 ACCAGCCAGT TCAACACCGC ( -AGCXΞCOGGC TACCTGAACG CCAACGTGCG CTACAACAAC 540 GTGGGCACCG GCGCCATCTA CGACGTGAAG CCCACCACCA GCTTCGTGCT GAACAACGAC 600 ACCATCGCCA CCATCACCGC <_AAGTCGAAT TCCACCGCCC TCAACATCAG (_CCCGGCGAG 660 AGCTACCCCA AGAAGGGCCA GAACCGCATC GCCATCACCA GCATQGACGA CTTCAACAGC 720 CACCCCATCA CCCTGAACAA GAAGCAGGTG GM PAΩCTGC TCAACAACAA GCCCATGATG 780 CTGGAGACCA ACCAGACCGA ∞GCGTCTAC AAGATCAAGG A ^CCCACGG CAACATCGTG 840 ACCGGCGGCG AGTGGAACGG CGTCATCCAG CAGATCAAGG CCAAGACCGC CAGCATCATC 900 GTCGACGACG GCGAGCGCGT GGCOGAGAAG CGCC?TGGCCG CCAAGGACTA O-AGAACCCC 960 GAGGACAAGA CCCCCAGCCT GACCCTGAAG CΪACGCCCTGA AGCTGAGCTA CCCCGACGAG 1020 ATCAAGGAGA TCGAGGGCCT GCTCTACTAC AAGAACAAGC CX-ATCTACGA GAGCAGCGTG 1080 ATGACCTATC TAGACGAGAA C.ACCGCCAAG GAGGTGACCA AGCAGCTGAA CGACACCACC 1140 GGCAAGTTCA AGGACGTGAG C-CACCTCTAC GACX.TGAAGC TCiACCCCCAA GATGAACGTG 1200 ACCATCAAGC TGAGCATCCT GTACGACAAC GCCGAGAGCA ACGACAACAG CATCGGCAAG 1260 TCGACCAACA CCAACATCGT GAGCQGCGGC AACAACGGCA AGAAGCAGTA CAQCAGCAAC 1320 AACCCCGACG CCAACCTGAC CCTGAACACC GACGCCCAGG AGAAGCTGAA CAAGAACCGC 1380 GACTACTACA TCAGCCTGTA CATGAAGAGC GAGAAGAACA CXXAGTGCGA GATCACCATC 1440 GACGGCGAGA TATACCCCAT CACCACCAAG ACCGTGAACG TGAACAAGGA CAACTACAAG 1500 CGCCTGGACA TCAT∞CCCA CAACATCAAG AGCAACCCCA TCAGCAGCCT GCACATCAAG 1560 ACCAACGACG AGATCACCCT GTTCTGGGAC GACATATCGA TTACCGACGT CGCCAGCATC 1620 AAGCCCGAGA ACCTGACCGA CAC4CGAGATC AAGCAGATAT ACAGTCGCTA OGGCATCAAG 1680 CTGX-AGGACG GCATCCTGAT CGACAAGAAG QGCGGCATCC ACTACGGCGA GTTCATCAAC 1740 GAGGCCAGCT TCAACATCGA GCCCCTGCAG AACTACGTGA CCAAGTACGA GGTCACCTAC 1800 AGCAGCGAGC TC<_GCCCCAA CGTGAGCGAC ACCCTGGAGA GCGACAAGAT TTACAAGGAC 1860 GGCACCATCA AGTTCGACTT CACCAAGTAC AGCAAGAACG AGCAGGGCCT GTTCTAOGAC 1920 AGCGGCCTGA ACTGGGACTT CAAGATCAAC GCCATCACCT ACX_ACGGCAA GGAGATGAAC 1980 GTGTTCCACC GCTACAACAA GTAG 2004 (2) INFORMATION FOR SEQ ID NO:19: (i) SEQUENCE CHARACTERISTICS: (A) LEM-TH: 4074 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) Ϊ ) LECUI_E TYPE: ENA (genomic) ( ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1386 (D) OTHER INFORMATION: /product= "VIP2A(b) from Btt" (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1394..3895 (D) OTHER INFORMATION: /product= "VIPlA(b) from Btt" (ix) FEATURE: (A) NAME/KEY: misc_feature (B) IJOCATION: 1. .4074 (D) OTHER INFORMATION: /note= "Cloned ENA sequence from Btt which contains the genes for both VIPlA(b) and VIP2A(b) " (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19: ATG CAA AGA ATG GAG GGA AAG TTG TTT GTG GTG TCA AAA ACA TTA CAA 48 Met Gin Arg Met Glu Gly Lys Leu Phe Val Val Ser Lys Thr Leu Gin 670 675 680 GTA GTT ACT AGA ACT CTA TTG CTT AGT ACA GTT TAC TCT ATA ACT TTA 96 Val Val Thr Arg Thr Val Leu Leu Ser Thr Val Tyr Ser He Thr Leu 685 690 695 TTA AAT AAT GTA GTG ATA AAA GCT GAC CAA TTA AAT ATA AAT TCT CAA 144 Leu Asn Asn Val Val He Lys Ala Asp Gin Leu Asn He Asn Ser Gin 700 705 710 715 AGT AAA TAT ACT AAC TTG CAA AAT CTA AAA ATC CCT GAT AAT GCA GAG 192 Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Pro Asp Asn Ala Glu 720 725 730 GAT TTT AAA GAA GAT AAG GGG AAA GCG AAA GAA TGG GGG AAA GAG AAA 240 Asp Phe Lys Glu Asp Lys Gly Lys Ala Lys Glu Trp Gly Lys Glu Lys 735 740 745 GGG GAA GAG TGG AGG CCT CCT GCT ACT GAG AAA GGA GAA ATG AAT AAT 288 Gly Glu Glu Trp Arg Pro Pro Ala Thr Glu Lys Gly Glu Met Asn Asn 750 755 760 TTT TTA GAT AAT AAA AAT GAT ATA AAG ACC AAT TAT AAA GAA ATT ACT 336 Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr 765 770 775 TTT TCT ATG GCA GGT TCA TCT GAA GAT GAA ATA AAA GAT TTA GAA GAA 384 Phe Ser Met Ala Gly Ser Cys Glu Asp Glu He Lys Asp Leu Glu Glu 780 785 790 795 ATT GAT AAG ATC TTT GAT AAA GCC AAT CTC TCG ACT TCT ATT ATC ACC 432 He Asp Lys He Phe Asp Lys Ala Asn Leu Ser Ser Ser He He Thr 800 805 810 TAT AAA AAT GTG GAA CCA GCA ACA ATT GGA TTT AAT AAA TCT TTA ACA 480 Tyr Lys Asn Val Glu Pro Ala Thr He Gly Phe Asn Lys Ser Leu Thr 815 820 825 GAA GGT AAT ACG ATT AAT TCT GAT GCA ATG GCA CAG TTT AAA GAA CAA 528 Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin 830 835 840 TTT TTA GGT AAG GAT ATG AAG TTT GAT AGT TAT CTA GAT ACT CAT TTA 576 Phe Leu Gly Lys Asp Met Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 845 850 855 ACT GCT CAA CAA GTT TCC AGT AAA AAA AGA GTT ATT TTG AAG GTT ACG 624 Thr Ala Gin Gin Veil Ser Ser Lys Lys Arg Val He Leu Lys Val Thr 860 865 870 875 GTT CCG ACT GGG AAA GCT TCT ACT ACT CCA ACA AAA GCA GCT GTC ATT 672 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He 880 885 890 TTA AAC AAT AAT GAA TAC AAA ATG CTC ATT GAT AAT GGG TAT GTG CTC 720 Leu Asn Asn Asn Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Val Leu 895 900 905 CAT CTA GAT AAG GTA TCA AAA GTA GTA AAA AAA GGG ATG GAG TGC TTA 768 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Met Glu Cys Leu 910 915 920 CAA GTT GAA GGG ACT TTA AAA AAG ACT CTC GAC TTT AAA AAT GAT ATA 816 Gin Val Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He 925 930 935 AAT GCT GAA GCG CAT AGC TGG GGG ATG AAA ATT TAT GAA GAC TGG GCT 864 Asn Ala Glu Ala His Ser Trp Gly Met Lys He Tyr Glu Asp Trp Ala 940 945 950 955 AAA AAT TTA ACC GCT TCG CAA AGG GAA GCT TTA GAT GGG TAT GCT AGG 912 Lys Asn Leu Thr Ala Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg 960 965 970 CAA GAT TAT AAA GAA ATC AAT AAT TAT TTG CGC AAT CAA GGC GGG ACT 960 Gin Asp V Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser 975 980 985 GGA AAT GAA AAG CTG GAT GCC CAA TTA AAA AAT ATT TCT GAT GCT TTA 1008 Gly Asn Glu Lys Leu Asp Ala Gin Leu Lys Asn He Ser Asp Ala Leu 990 995 1000 GGG AAG AAA CCC ATA CCA GAA AAT ATT ACC GTG TAT AGA TGG TGT GGC 1056 Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly 1005 1010 1015 ATG CCG GAA TTT GCT TAT CAA ATT ACT GAT CCG TTA CCT TCT TTA AAA 1104 Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser I_eu Lys 1020 1025 1030 1035 GAT TTT GAA GAA CAA TTT TTA AAT ACA ATT AAA GAA GAC AAA GGG TAT 1152 Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr 1040 1045 1050 ATG AGT ACA AGC TTA TCG AGT GAA CGT CTT GCA GCT TTT GGA TCT AGA 1200 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg 1055 1060 1065 AAA ATT ATA TTA CGC TTA CAA GTT CCG AAA GGA ACT ACG GGG GCG TAT 1248 Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr 1070 1075 1080 TTA AGT GCC ATT GCT GGA TTT GCA ACT GAA AAA GAG ATC CTA CTT GAT 1296 Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp 1085 1090 1095 AAA GAT AGT AAA TAT CAT ATT GAT AAA GCA ACA GAG GTA ATC ATT AAA 1344 Lys Asp Ser Lys Tyr His He Asp Lys Ala Thr Glu Val He He Lys 1100 1105 1110 1115 GGT GTT AAG CGA TAT CTA GTG GAT GCA ACA TTA TTA ACA AAT 1386 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 1120 1125 TAAGGAG ATG AAA AAT ATG AAG AAA AAG TTA GCA ACT GTT GTA ACC TCT 1435 Met Lys Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys 1 5 10 ATG TTA TTA GCT CCT ATG TTT TTG AAT GGA AAT GTG AAT GCT GTT AAC 1483 Met Leu Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Asn 15 20 25 30 GCG GAT ACT AAA ATA AAT CAG ATT TCT ACA ACG CAG GAA AAC CAA CAG 1531 Ala Asp Ser Lys He Asn Gin He Ser Thr Thr Gin Glu Asn Gin Gin 35 40 45 AAA GAG ATG GAC CGA AAG GGA TTA TTG GGA TAT TAT TTC AAA GGA AAA 1579 Lys Glu Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys 50 55 60 GAT TTT AAT AAT CTT ACT ATG TTT GCA CCG ACA CGT GAT AAT ACC CTT 1627 Asp Phe Asn Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Asn Thr Leu 65 70 75 ATG TAT GAC CAA CAA ACA GCG AAT GCA TTA TTA GAT AAA AAA CAA CAA 1675 Met Tyr Asp Gin Gin Thr Ala Asn Ala I_eu Leu Asp Lys Lys Gin Gin 80 85 90 GAA TAT CAG TCC ATT CCT TGG ATT GCT TTG ATT CAG CGT AAA GAA ACG 1723 Glu Tyr Gin Ser He Arg Trp He Gly Leu He Gin Arg Lys Glu Thr 95 100 105 110 GGC GAT TTC ACA TTT AAC TTA TCA AAG GAT GAA CAG GCA ATT ATA GAA 1771 Gly Asp Phe Thr Phe Asn Leu Ser Lys Asp Glu Gin Ala He He Glu 115 120 125 ATC GAT GGG AAA ATC ATT TCT AAT AAA GGG AAA GAA AAG CAA GTT GTC 1819 He Asp Gly Lys He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val 130 135 140 CAT TTA GAA AAA GAA AAA TTA GTT CCA ATC AAA ATA GAG TAT CAA TCA 1867 His Leu Glu Lys Glu Lys Leu Val Pro He Lys He Glu Tyr Gin Ser 145 150 155 GAT ACG AAA TTT AAT ATT GAT ACT AAA ACA TTT AAA GAA CTT AAA TTA 1915 Asp Thr Lys Phe Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu 160 165 170 TTT AAA ATA GAT AGT CAA AAC CAA TCT CAA CAA GTT CAA CTG AGA AAC 1963 Phe Lys He Asp Ser Gin Asn Gin Ser Gin Gin Val Gin Leu Arg Asn 175 180 185 190 CCT GAA TTT AAC AAA AAA GAA TCA CAG GAA TTT TTA GCA AAA GCA TCA 2011 Pro Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Ala Ser 195 200 205 AAA ACA AAC CTT TTT AAG CAA AAA ATG AAA AGA GAT ATT GAT GAA GAT 2059 Lys Thr Asn Leu Phe Lys Gin Lys Met Lys Arg Asp He Asp Glu Asp 210 215 220 ACG GAT ACA GAT GGA GAC TCC ATT CCT GAT CTT TGG GAA GAA AAT GGG 2107 Thr Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn Gly 225 230 235 TAC ACG ATT CAA AAT AAA GTT GCT GTC AAA TGG GAT GAT TCG CTA GCA 2155 Tyr Thr He Gin Asn Lys Val Ala Val Lys Trp Asp Asp Ser Leu Ala 240 245 250 AGT AAG GGA TAT ACA AAA TTT GTT TCG AAT CCA TTA GAC AGC CAC ACA 2203 Ser Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Asp Ser His Thr 255 260 265 270 GTT GGC GAT CCC TAT ACT GAT TAT GAA AAG GCC GCA AGG GAT TTA GAT 2251 Val Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu Asp 275 280 285 TTA TCA AAT GCA AAG GAA ACG TTC AAC CCA TTG GTA GCT GCT TTT CCA 2299 Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe Pro 290 295 300 AGT GTG AAT GTT AGT ATG GAA AAG GTG ATA TTA TCA CCA AAT GAA AAT 2347 Ser Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu Asn 305 310 315 TTA TCC AAT ACT GTA GAG TCT CAT TCA TCC ACG AAT TGG TCT TAT ACG 2395 Leu Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr Thr 320 325 330 AAT ACA GAA GGA GCT TCC ATT GAA GCT GCT GGC GGT CCA TTA GGC CTT 2443 Asn Thr Glu Gly Ala Ser He Glu Ala Gly Gly Gly Pro Leu Gly I_eu 335 340 345 350 TCT TTT GGC GTG AGT GTT ACT TAT CAA CAC TCT GAA ACA GTT GCA CAA 2491 Ser Phe Gly Val Ser Val Thr Tyr Gin His Ser Glu Thr Val Ala Gin 355 360 365 GAA TGG GGA ACA TCT ACA GGA AAT ACT TCA CAA TTC AAT ACG GCT TCA 2539 Glu Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala Ser 370 375 380 GCG GGA TAT TTA AAT GCA AAT GTT CGG TAT AAC AAT GTA GGG ACT GGT 2587 Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr Gly 385 390 395 GCC ATC TAT GAT GTA AAA CCT ACA ACA ACT TTT GTA TTA AAT AAC AAT 2635 Ala He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn Asn 400 405 410 ACC ATC GCA ACG ATT ACA GCA AAA TCA AAT TCA ACA GCT TTA CGT ATA 2683 Thr He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Arg He 415 420 425 430 TCT CCG GGG GAT AGT TAT CCA GAA ATA GGA GAA AAC GCT ATT GCG ATT 2731 Ser Pro Gly Asp Ser Tyr Pro Glu He Gly Glu Asn Ala He Ala He 435 440 445 ACA TCT ATG GAT GAT TTT AAT TCT CAT CCA ATT ACA TTA AAT AAA CAA 2779 Thr Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn Lys Gin 450 455 460 CAG CTA AAT CAA TTG ATA AAT AAT AAG CCA ATT ATG CTA GAG ACA GAC 2827 Gin Val Asn Gin Leu He Asn Asn Lys Pro He Met Leu Glu Thr Asp 465 470 475 CAA ACA GAT GGT GTT TAT AAA ATA AGA GAT ACA CAT GGA AAT ATT CTA 2875 Gin Thr Asp Gly Val Tyr Lys He Arg Asp Thr His Gly Asn He Val 480 485 490 ACT GGT GGA GAA TGG AAT GGT GTA ACA CAA CAA ATT AAA GCA AAA ACA 2923 Thr Gly Gly Glu Trp Asn Gly Val Thr Gin Gin He Lys Ala Lys Thr 495 500 505 510 GCG TCT ATT ATT GTG GAT GAC GGG AAA CAG CTA GCA GAA AAA CCT GTG 2971 Ala Ser He He Val Asp Asp Gly Lys Gin Val Ala Glu Lys Arg Val 515 520 525 GCG GCA AAA GAT TAT GGT CAT CCA GAA GAT AAA ACA CCA CCT TTA ACT 3019 Ala Ala Lys Asp Tyr Gly His Pro Glu Asp Lys Thr Pro Pro Leu Thr 530 535 540 TTA AAA GAT ACC CTG AAG CTT TCA TAC CCA GAT GAA ATA AAA GAA ACT 3067 I_eu Lys Asp Thr Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu Thr 545 550 555 AAT GGA TTG TTG TAC TAT GAT GAC AAA CCA ATC TAT GAA TCG AGT GTC 3115 Asn Gly Leu Leu Tyr Tyr Asp Asp Lys Pro He Tyr Glu Ser Ser Val 560 565 570 ATG ACT TAT CTG GAT GAA AAT ACG GCA AAA GAA GTC AAA AAA CAA ATA 3163 Met Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Lys Lys Gin He 575 580 585 590 AAT GAT ACA ACC GGA AAA TTT AAG GAT CTA AAT CAC TTA TAT GAT GTA 3211 Asn Asp Thr Thr Gly Lys Phe Lys Asp Val Asn His Leu Tyr Asp Val 595 600 605 AAA CTG ACT CCA AAA ATG AAT TTT ACG ATT AAA ATG GCT TCC TTG TAT 3259 Lys Leu Thr Pro Lys Met Asn Phe Thr He Lys Met Ala Ser Leu Tyr 610 615 620 GAT GGG GCT GAA AAT AAT CAT AAC TCT TTA GGA ACC TGG TAT TTA ACA 3307 Asp Gly Ala Glu Asn Asn His Asn Ser Leu Gly Thr Trp Tyr Leu Thr 625 630 635 TAT AAT GTT GCT GCT GGA AAT ACT GGG AAG AGA CAA TAT CCT TCA GCT 3355 Tyr Asn Val Ala Gly Gly Asn Thr Gly Lys Arg Gin Tyr Arg Ser Ala 640 645 650 CAT TCT TGT GCA CAT GTA GCT CTA TCT TCA GAA GCG AAA AAG AAA CTA 3403 His Ser Cys Ala His Val Ala Leu Ser Ser Glu Ala Lys Lys Lys Leu 655 660 665 670 AAT CAA AAT GCG AAT TAC TAT CTT AGC ATG TAT ATG AAG GCT GAT TCT 3451 Asn Gin Asn Ala Asn Tyr Tyr Leu Ser Met Tyr Met Lys Ala Asp Ser 675 680 685 ACT ACG GAA CCT ACA ATA GAA GTA GCT GGG GAA AAA TCT GCA ATA ACA 3499 Thr Thr Glu Pro Thr He Glu Val Ala Gly Glu Lys Ser Ala He Thr 690 695 700 ACT AAA AAA GTA AAA TTA AAT AAT CAA AAT TAT CAA AGA GTT GAT ATT 3547 Ser Lys Lys Val Lys Leu Asn Asn Gin Asn Tyr Gin Arg Val Asp He 705 710 715 TTA GTG AAA AAT TCT GAA AGA AAT CCA ATG GAT AAA ATA TAT ATA AGA 3595 Leu Val Lys Asn Ser Glu Arg Asn Pro Met Asp Lys He Tyr He Arg 720 725 730 GGA AAT GGC ACG ACA AAT GTT TAT GGG GAT GAT GTT ACT ATC CCA GAG 3643 Gly Asn Gly Thr Thr Asn Val Tyr Gly Asp Asp Val Thr He Pro Glu 735 740 745 750 CTA TCA GCT ATA AAT CCG GCT AGT CTA TCA GAT GAA GAA ATT CAA GAA 3691 Val Ser Ala He Asn Pro Ala Ser Leu Ser Asp Glu Glu He Gin Glu 755 760 765 ATA TTT AAA GAC TCA ACT ATT GAA TAT GGA AAT CCT AGT TTC GTT GCT 3739 He Phe Lys Asp Ser Thr He Glu Tyr Gly Asn Pro Ser Phe Val Ala 770 775 780 GAT GCC GTA ACA TTT AAA AAT ATA AAA CCT TTA CAA AAT TAT CTA AAG 3787 Asp Ala Val Thr Phe Lys Asn He Lys Pro Leu Gin Asn Tyr Val Lys 785 790 795 GAA TAT GAA ATA TAT CAT AAA TCT CAT CGA TAT GAA AAG AAA ACG GTC 3835 Glu Tyr Glu He Tyr His Lys Ser His Arg Tyr Glu Lys Lys Thr Val 800 805 810 TTT GAT ATC ATG GGT GTT CAT TAT GAG TAT AGT ATA GCT AGG GAA CAA 3883 Phe Asp He Met Gly Val His Tyr Glu Tyr Ser He Ala Arg Glu Gin 815 820 825 830 AAG AAA GCC GCA TAATTTTAAA AATAAAACTC G-TAGAGTTT ATTTAGCATG 3935 Lys Lys Ala Ala CTATTTΓTAA GAATAATCAA TATGTTGAAC CGTTTGTAGC TGTTTTGGAA GGGAATTTCA 3995 TTTTATTTGG TCTCTTAACT TGATGGGCAT GGGATATGTT CAGCATCCAA GCGTTTNQGG 4055 GGTTANAAAA TCCAATTTT 4074 (2) INFORMATIC-N FOR SEQ ID NO:20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 462 amino acids (B) TYPE: amino acid (D) TOTOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:20: Met Gin Arg Met Glu Gly Lys Leu Phe Val Val Ser Lys Thr Leu Gin 1 5 10 15 Val Val Thr Arg Thr Val Leu Leu Ser Thr Val Tyr Ser He Thr Leu 20 25 30 Leu Asn Asn Val Val He Lys Ala Asp Gin Leu Asn He Asn Ser Gln 35 40 45 Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Pro Asp Asn Ala Glu 50 55 60 Asp Phe Lys Glu Asp Lys Gly Lys Ala Lys Glu Trp Gly Lys Glu Lys 65 70 75 80 Gly Glu Glu Trp Arg Pro Pro Ala Thr Glu Lys Gly Glu Met Asn Asn 85 90 95 Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr 100 105 110 Phe Ser Met Ala Gly Ser Cys Glu Asp Glu He Lys Asp Leu Glu Glu 115 120 125 He Asp Lys He Phe Asp Lys Ala Asn Leu Ser Ser Ser He He Thr 130 135 140 Tyr Lys Asn Val Glu Pro Ala Thr He Gly Phe Asn Lys Ser Leu Thr 145 150 155 160 Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin 165 170 175 Phe Leu Gly Lys Asp Met Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 180 185 190 Thr Ala Gin Gin Val Ser Ser Lys Lys Arg Val He Leu Lys Val Thr 195 200 205 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He 210 215 220 Leu Asn Asn Asn Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Val Leu 225 230 235 240 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Met Glu Cys Leu 245 250 255 Gin Val Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He 260 265 270 Asn Ala Glu Ala His Ser Trp Gly Met Lys He Tyr Glu Asp Trp Ala 275 280 285 Lys Asn Leu Thr Ala Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg 290 295 300 Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser 305 310 315 320 Gly Asn Glu Lys Leu Asp Ala Gin Leu Lys Asn He Ser Asp Ala Leu 325 330 335 Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly 340 345 350 Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys 355 360 365 Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr 370 375 380 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg 385 390 395 400 Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr 405 410 415 Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp 420 425 430 Lys Asp Ser Lys Tyr His He Asp Lys Ala Thr Glu Val He He Lys 435 440 445 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 450 455 460 (2) INFORMATION FOR SEQ ID NO:21: (i) SEQUENCE CHARACTERISTICS: (A) LEN3TH: 834 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21: Met Lys Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Met Leu 1 5 10 15 Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Asn Ala Asp 20 25 30 Ser Lys He Asn Gin He Ser Thr Thr Gin Glu Asn Gin Gin Lys Glu 35 40 45 Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 50 55 60 Asn Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Asn Thr Leu Met Tyr 65 70 75 80 Asp Gin Gin Thr Ala Asn Ala Leu Leu Asp Lys Lys Gin Gin Glu Tyr 85 90 95 Gin Ser He Arg Trp He Gly Leu He Gin Arg Lys Glu Thr Gly Asp 100 105 110 Phe Thr Phe Asn Leu Ser Lys Asp Glu Gin Ala He He Glu He Asp 115 120 125 Gly Lys He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val His Leu 130 135 140 Glu Lys Glu Lys Leu Val Pro He Lys He Glu Tyr Gin Ser Asp Thr 145 150 155 160 Lys Phe Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu Phe Lys 165 170 175 He Asp Ser Gin Asn Gin Ser Gin Gin Val Gin Leu Arg Asn Pro Glu 180 185 190 Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Ala Ser Lys Thr 195 200 205 Asn Leu Phe Lys Gin Lys Met Lys Arg Asp He Asp Glu Asp Thr Asp 210 215 220 Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn Gly Tyr Thr 225 230 235 240 He Gin Asn Lys Val Ala Val Lys Trp Asp Asp Ser Leu Ala Ser Lys 245 250 255 Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Asp Ser His Thr Val Gly 260 265 270 Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu Asp Leu Ser 275 280 285 Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe Pro Ser Val 290 295 300 Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu Asn Leu Ser 305 310 315 320 Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr Thr Asn Thr 325 330 335 Glu Gly Ala Ser He Glu Ala Gly Gly Gly Pro Leu Gly Leu Ser Phe 340 345 350 Gly Val Ser Val Thr Tyr Gin His Ser Glu Thr Val Ala Gin Glu Trp 355 360 365 Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala Ser Ala Gly 370 375 380 Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr Gly Ala He 385 390 395 400 Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn Asn Thr He 405 410 415 Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Arg He Ser Pro 420 425 430 Gly Asp Ser Tyr Pro Glu He Gly Glu Asn Ala He Ala He Thr Ser 435 440 445 Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn Lys Gin Gin Val 450 455 460 Asn Gin Leu He Asn Asn Lys Pro He Met Leu Glu Thr Asp Gin Thr 465 470 475 480 Asp Gly Val Tyr Lys He Arg Asp Thr His Gly Asn He Val Thr Gly 485 490 495 Gly Glu Trp Asn Gly Val Thr Gin Gin He Lys Ala Lys Thr Ala Ser 500 505 510 He He Val Asp Asp Gly Lys Gin Val Ala Glu Lys Arg Val Ala Ala 515 520 525 Lys Asp Tyr Gly His Pro Glu Asp Lys Thr Pro Pro Leu Thr Leu Lys 530 535 540 Asp Thr Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu Thr Asn Gly 545 550 555 560 Leu Leu Tyr Tyr Asp Asp Lys Pro He Tyr Glu Ser Ser Val Met Thr 565 570 575 Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Lys Lys Gin He Asn Asp 580 585 590 Thr Thr Gly Lys Phe Lys Asp Val Asn His Leu Tyr Asp Val Lys Leu 595 600 605 Thr Pro Lys Met Asn Phe Thr He Lys Met Ala Ser Leu Tyr Asp Gly 610 615 620 Ala Glu Asn Asn His Asn Ser Leu Gly Thr Trp Tyr Leu Thr Tyr Asn 625 630 635 640 Val Ala Gly Gly Asn Thr Gly Lys Arg Gin Tyr Arg Ser Ala His Ser 645 650 655 Cys Ala His Val Ala Leu Ser Ser Glu Ala Lys Lys Lys Leu Asn Gin 660 665 670 Asn Ala Asn Tyr Tyr Leu Ser Met Tyr Met Lys Ala Asp Ser Thr Thr 675 680 685 Glu Pro Thr He Glu Val Ala Gly Glu Lys Ser Ala He Thr Ser Lys 690 695 700 Lys Val Lys Leu Asn Asn Gin Asn Tyr Gin Arg Val Asp He Leu Val 705 710 715 720 Lys Asn Ser Glu Arg Asn Pro Met Asp Lys He Tyr He Arg Gly Asn 725 730 735 Gly Thr Thr Asn Val Tyr Gly Asp Asp Val Thr He Pro Glu Val Ser 740 745 750 Ala He Asn Pro Ala Ser Leu Ser Asp Glu Glu He Gin Glu He Phe 755 760 765 Lys Asp Ser Thr He Glu Tyr Gly Asn Pro Ser Phe Val Ala Asp Ala 770 775 780 Val Thr Phe Lys Asn He Lys Pro Leu Gin Asn Tyr Val Lys Glu Tyr 785 790 795 800 Glu He Tyr His Lys Ser His Arg Tyr Glu Lys Lys Thr Val Phe Asp 805 810 815 He Met Gly Val His Tyr Glu Tyr Ser He Ala Arg Glu Gin Lys Lys 820 825 830 Ala Ala (2) INFORMATION FOR SEQ ID NO:22: (i) SEQUENCE CHARACTERIOTICS: (A) L-5N3TH: 4041 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: ENA (genσmic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..4038 (D) OTHER INFORMATION: /product= "VTPlA(a) /VIP2A(a) fusion product" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:22: ATG AAA AGA ATG GAG GGA AAG TTG TTT ATG GTG TCA AAA AAA TTA CAA 48 Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu Gin 835 840 845 850 GTA GTT ACT AAA ACT GTA TTG CTT ACT ACA GTT TTC TCT ATA TCT TTA 96 Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser He Ser Leu 855 860 865 TTA AAT AAT GAA GTG ATA AAA GCT GAA CAA TTA AAT ATA AAT TCT CAA 144 Leu Asn Asn Glu Val He Lys Ala Glu Gin Leu Asn He Asn Ser Gin 870 875 880 AGT AAA TAT ACT AAC TTG CAA AAT CTA AAA ATC ACT GAC AAG GTA GAG 192 Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu 885 890 895 GAT TTT AAA GAA GAT AAG GAA AAA GCG AAA GAA TGG GGG AAA GAA AAA 240 Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys 900 905 910 GAA AAA GAG TGG AAA CTA ACT GCT ACT GAA AAA GGA AAA ATG AAT AAT 288 Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn 915 920 925 930 TTT TTA GAT AAT AAA AAT GAT ATA AAG ACA AAT TAT AAA GAA ATT ACT 336 Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr 935 940 945 TTT TCT ATG GCA GGC TCA TTT GAA GAT GAA ATA AAA GAT TTA AAA GAA 384 Phe Ser Met Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu 950 955 960 ATT GAT AAG ATG TTT GAT AAA ACC AAT CTA TCA AAT TCT ATT ATC ACC 432 He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr 965 970 975 TAT AAA AAT GTG GAA CCG ACA ACA ATT GGA TTT AAT AAA TCT TTA ACA 480 Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr 980 985 990 GAA GCT AAT ACG ATT AAT TCT GAT GCA ATG GCA CAG TTT AAA GAA CAA 528 Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin 995 1000 1005 1010 TTT TTA GAT AGG GAT ATT AAG TTT GAT AGT TAT CTA GAT ACG CAT TTA 576 Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 1015 1020 1025 ACT GCT CAA CAA GTT TCC AGT AAA GAA AGA GTT ATT TTG AAG GTT ACG 624 Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr 1030 1035 1040 GTT CCG AGT GGG AAA GGT TCT ACT ACT CCA ACA AAA GCA GGT GTC ATT 672 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He 1045 1050 1055 TTA AAT AAT AGT GAA TAC AAA ATG CTC ATT GAT AAT GGG TAT ATG GTC 720 Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val 1060 1065 1070 CAT GTA GAT AAG GTA TCA AAA GTG GTG AAA AAA GGG GTG GAG TGC TTA 768 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu 1075 1080 1085 1090 CAA ATT GAA GGG ACT TTA AAA AAG ACT CTT GAC TTT AAA AAT GAT ATA 816 Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He 1095 1100 1105 AAT GCT GAA GCG CAT AGC TGG GGT ATG AAG AAT TAT GAA GAG TGG GCT 864 Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala 1110 1115 1120 AAA GAT TTA ACC GAT TCG CAA AGG GAA GCT TTA GAT GGG TAT GCT AGG 912 Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg 1125 1130 1135 CAA GAT TAT AAA GAA ATC AAT AAT TAT TTA AGA AAT CAA GGC GGA ACT 960 Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser 1140 1145 1150 GGA AAT GAA AAA CTA GAT GCT CAA ATA AAA AAT ATT TCT GAT GCT TTA 1008 Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu 1155 1160 1165 1170 GGG AAG AAA CCA ATA CCG GAA AAT ATT ACT GTG TAT AGA TGG TCT GGC 1056 Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly 1175 1180 1185 ATG CCG GAA TTT GCT TAT CAA ATT AGT GAT CCG TTA COT TCT TTA AAA 1104 Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys 1190 1195 1200 GAT TTT GAA GAA CAA TTT TTA AAT ACA ATC AAA GAA GAC AAA GGA TAT 1152 Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr 1205 1210 1215 ATG AGT ACA AGC TTA TCG AGT GAA CGT CTT GCA GCT TTT GGA TCT AGA 1200 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg 1220 1225 1230 AAA ATT ATA TTA CGA TTA CAA GTT CCG AAA GGA AGT ACG GCT GCG TAT 1248 Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr 1235 1240 1245 1250 TTA AGT GCC ATT GGT GGA TTT GCA ACT GAA AAA GAG ATC CTA CTT GAT 1296 Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp 1255 1260 1265 AAA GAT AGT AAA TAT CAT ATT GAT AAA GTA ACA GAG GTA ATT ATT AAA 1344 Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He Lys 1270 1275 1280 GGT GTT AAG CGA TAT GTA GTG GAT GCA ACA TTA TTA ACA AAT ATG AAA 1392 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn Met Lys 1285 1290 1295 AAT ATG AAG AAA AAG TTA GCA ACT GTT GTA ACG TGT ACG TTA TTA GCT 1440 Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu Leu Ala 1300 1305 1310 CCT ATG TTT TTG AAT GGA AAT GTG AAT GCT GTT TAC GCA GAC AGC AAA 1488 Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Tyr Ala Asp Ser Lys 1315 1320 1325 1330 ACA AAT CAA ATT TCT ACA ACA CAG AAA AAT CAA CAG AAA GAG ATG GAC 1536 Thr Asn Gin He Ser Thr Thr Gin Lys Asn Gin Gin Lys Glu Met Asp 1335 1340 1345 CGA AAA GGA TTA CTT GGG TAT TAT TTC AAA GGA AAA GAT TTT ACT AAT 1584 Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe Ser Asn 1350 1355 1360 CTT ACT ATG TTT GCA CCG ACA CGT GAT AGT ACT CTT ATT TAT GAT CAA 1632 Leu Thr Met Phe Ala Pro Thr Arg Asp Ser Thr Leu He Tyr Asp Gin 1365 1370 1375 CAA ACA GCA AAT AAA CTA TTA GAT AAA AAA CAA CAA GAA TAT CAG TCT 1680 Gin Thr Ala Asn Lys Leu Leu Asp Lys Lys Gin Gin Glu Tyr Gin Ser 1380 1385 1390 ATT CGT TGG ATT GGT T G ATT CAG ACT AAA GAA ACG GGA GAT TTC ACA 1728 He Arg Trp He Gly Leu He Gin Ser Lys Glu Thr Gly Asp Phe Thr 1395 1400 1405 1410 TTT AAC TTA TCT GAG GAT GAA CAG GCA ATT ATA GAA ATC AAT GGG AAA 1776 Phe Asn Leu Ser Glu Asp Glu Gin Ala He He Glu He Asn Gly Lys 1415 1420 1425 ATT ATT TCT AAT AAA GGG AAA GAA AAG CAA GTT GTC CAT TTA GAA AAA 1824 He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val His Leu Glu Lys 1430 1435 1440 GGA AAA TTA GTT CCA ATC AAA ATA GAG TAT CAA TCA GAT ACA AAA TTT 1872 Gly Lys Leu Val Pro He Lys He Glu Tyr Gin Ser Asp Thr Lys Phe 1445 1450 1455 AAT ATT GAC AGT AAA ACA TTT AAA GAA CTT AAA TTA TTT AAA ATA GAT 1920 Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu Phe Lys He Asp 1460 1465 1470 AGT CAA AAC CAA CCC CAG CAA GTC CAG CAA GAT GAA CTG AGA AAT CCT 1968 Ser Gin Asn Gin Pro Gin Gin Val Gin Gin Asp Glu Leu Arg Asn Pro 1475 1480 1485 1490 GAA TTT AAC AAG AAA GAA TCA CAG GAA TTC TTA GCG AAA CCA TCG AAA 2016 Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Pro Ser Lys 1495 1500 1505 ATA AAT CTT TTC ACT CAA AAA ATG AAA AGG GAA ATT GAT GAA GAC ACG 2064 He Asn Leu Phe Thr Gin Lys Met Lys Arg Glu He Asp Glu Asp Thr 1510 1515 1520 GAT ACG GAT GGG GAC TCT ATT CCT GAC CTT TGG GAA GAA AAT GGG TAT 2112 Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn Gly Tyr 1525 1530 1535 ACG ATT CAA AAT AGA ATC GCT GTA AAG TGG GAC GAT TCT CTA GCA AGT 2160 Thr He Gin Asn Arg He Ala Val Lys Trp Asp Asp Ser Leu Ala Ser 1540 1545 1550 AAA GGG TAT ACG AAA TTT GTT TCA AAT CCA CTA GAA AGT CAC ACA GTT 2208 Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Glu Ser His Thr Val 1555 1560 1565 1570 GGT GAT CCT TAT ACA GAT TAT GAA AAG GCA GCA AGA GAT CTA GAT TTG 2256 Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu Asp Leu 1575 1580 1585 TCA AAT GCA AAG GAA ACG TTT AAC CCA TTG GTA GCT GCT TTT CCA AGT 2304 Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe Pro Ser 1590 1595 1600 GTG AAT GTT AGT ATG GAA AAG GTG ATA TTA TCA CCA AAT GAA AAT TTA 2352 Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu Asn Leu 1605 1610 1615 TCC AAT AGT GTA GAG TCT CAT TCA TCC ACG AAT TGG TCT TAT ACA AAT 2400 Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr Thr Asn 1620 1625 1630 ACA GAA GGT GCT TCT GTT GAA GCG GGG ATT GGA CCA AAA GCT ATT TCG 2448 Thr Glu Gly Ala Ser Val Glu Ala Gly He Gly Pro Lys Gly He Ser 1635 1640 1645 1650 TTC GGA GTT AGC GTA AAC TAT CAA CAC TCT GAA ACA GTT GCA CAA GAA 2496 Phe Gly Val Ser Val Asn Tyr Gin His Ser Glu Thr Val Ala Gin Glu 1655 1660 1665 TGG GGA ACA TCT ACA GGA AAT ACT TCG CAA TTC AAT ACG GCT TCA GCG 2544 Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala Ser Ala 1670 1675 1680 GGA TAT TTA AAT GCA AAT GTT CGA TAT AAC AAT GTA GGA ACT GGT GCC 2592 Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr Gly Ala 1685 1690 1695 ATC TAC GAT GTA AAA CCT ACA ACA ACT TTT GTA TTA AAT AAC GAT ACT 2640 He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn Asp Thr 1700 1705 1710 ATC GCA ACT ATT ACG GCG AAA TCT AAT TCT ACA GCC TTA AAT ATA TCT 2688 He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Asn He Ser 1715 1720 1725 1730 CCT GGA GAA AGT TAC CCG AAA AAA GGA CAA AAT GGA ATC GCA ATA ACA 2736 Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gin Asn Gly He Ala He Thr 1735 1740 1745 TCA ATG GAT GAT TTT AAT TCC CAT CCG ATT ACA TTA AAT AAA AAA CAA 2784 Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn Lys Lys Gin 1750 1755 1760 CTA GAT AAT CTG CTA AAT AAT AAA CCT ATG ATG TTG GAA ACA AAC CAA 2832 Val Asp Asn Leu Leu Asn Asn Lys Pro Met Met Leu Glu Thr Asn Gin 1765 1770 1775 ACA GAT GGT GTT TAT AAG ATA AAA GAT ACA CAT GGA AAT ATA CTA ACT 2880 Thr Asp Gly Val Tyr Lys He Lys Asp Thr His Gly Asn He Val Thr 1780 1785 1790 GGC GGA GAA TGG AAT GGT GTC ATA CAA CAA ATC AAG GCT AAA ACA GCG 2928 Gly Gly Glu Trp Asn Gly Val He Gin Gin He Lys Ala Lys Thr Ala 1795 1800 1805 1810 TCT ATT ATT GTG GAT GAT GGG GAA CCT GTA GCA GAA AAA CGT GTA GCG 2976 Ser He He Val Asp Asp Gly Glu Arg Val Ala Glu Lys Arg Val Ala 1815 1820 1825 GCA AAA GAT TAT GAA AAT CCA GAA GAT AAA ACA CCG TCT TTA ACT TTA 3024 Ala Lys Asp Tyr Glu Asn Pro Glu Asp Lys Thr Pro Ser Leu Thr Leu 1830 1835 1840 AAA GAT GCC CTG AAG CTT TCA TAT CCA GAT GAA ATA AAA GAA ATA GAG 3072 Lys Asp Ala Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu He Glu 1845 1850 1855 GGA TTA TTA TAT TAT AAA AAC AAA CCG ATA TAC GAA TCG AGC GTT ATG 3120 Gly Leu Leu Tyr Tyr Lys Asn Lys Pro He Tyr Glu Ser Ser Val Met 1860 1865 1870 ACT TAC TTA GAT GAA AAT ACA GCA AAA GAA GTG ACC AAA CAA TTA AAT 3168 Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Thr Lys Gin Leu Asn 1875 1880 1885 1890 GAT ACC ACT GGG AAA TTT AAA GAT CTA AGT CAT TTA TAT GAT GTA AAA 3216 Asp Thr Thr Gly Lys Phe Lys Asp Val Ser His Leu Tyr Asp Val Lys 1895 1900 1905 CTG ACT CCA AAA ATG AAT GTT ACA ATC AAA TTG TCT ATA CTT TAT GAT 3264 Leu Thr Pro Lys Met Asn Val Thr He Lys Leu Ser He Leu Tyr Asp 1910 1915 1920 AAT GCT GAG TCT AAT GAT AAC TCA ATT GGT AAA TGG ACA AAC ACA AAT 3312 Asn Ala Glu Ser Asn Asp Asn Ser He Gly Lys Trp Thr Asn Thr Asn 1925 1930 1935 ATT GTT TCA GGT GGA AAT AAC GGA AAA AAA CAA TAT TCT TCT AAT AAT 3360 He Val Ser Gly Gly Asn Asn Gly Lys Lys Gin Tyr Ser Ser Asn Asn 1940 1945 1950 CCG GAT GCT AAT TTG ACA TTA AAT ACA GAT GCT CAA GAA AAA TTA AAT 3408 Pro Asp Ala Asn Leu Thr Leu Asn Thr Asp Ala Gin Glu Lys Leu Asn 1955 1960 1965 1970 AAA AAT CGT GAC TAT TAT ATA AGT TTA TAT ATG AAG TCA GAA AAA AAC 3456 Lys Asn Arg Asp Tyr Tyr He Ser Leu Tyr Met Lys Ser Glu Lys Asn 1975 1980 1985 ACA CAA TGT GAG ATT ACT ATA GAT GGG GAG ATT TAT CCG ATC ACT ACA 3504 Thr Gin Cys Glu He Thr He Asp Gly Glu He Tyr Pro He Thr Thr 1990 1995 2000 AAA ACA GTG AAT GTG AAT AAA GAC AAT TAC AAA AGA TTA GAT ATT ATA 3552 Lys Thr Val Asn Val Asn Lys Asp Asn Tyr Lys Arg Leu Asp He He 2005 2010 2015 GCT CAT AAT ATA AAA AGT AAT CCA ATT TCT TCA CTT CAT ATT AAA ACG 3600 Ala His Asn He Lys Ser Asn Pro He Ser Ser Leu His He Lys Thr 2020 2025 2030 AAT GAT GAA ATA ACT TTA TTT TGG GAT GAT ATT TCT ATA ACA GAT GTA 3648 Asn Asp Glu He Thr Leu Phe Trp Asp Asp He Ser He Thr Asp Val 2035 2040 2045 2050 GCA TCA ATA AAA CCG GAA AAT TTA ACA GAT TCA GAA ATT AAA CAG ATT 3696 Ala Ser He Lys Pro Glu Asn Leu Thr Asp Ser Glu He Lys Gin He 2055 2060 2065 TAT AGT AGG TAT GGT ATT AAG TTA GAA GAT GGA ATC CTT ATT GAT AAA 3744 Tyr Ser Arg Tyr Gly He Lys Leu Glu Asp Gly He Leu He Asp Lys 2070 2075 2080 AAA GGT GGG ATT CAT TAT GCT GAA TTT ATT AAT GAA GCT AGT TTT AAT 3792 Lys Gly Gly He His Tyr Gly Glu Phe He Asn Glu Ala Ser Phe Asn 2085 2090 2095 ATT GAA CCA TTG CAA AAT TAT GTG ACC AAA TAT GAA GTT ACT TAT AGT 3840 He Glu Pro Leu Gin Asn Tyr Val Thr Lys Tyr Glu Val Thr Tyr Ser 2100 2105 2110 ACT GAG TTA GGA CCA AAC GTG AGT GAC ACA CTT GAA ACT GAT AAA ATT 3888 Ser Glu Leu Gly Pro Asn Val Ser Asp Thr Leu Glu Ser Asp Lys He 2115 2120 2125 2130 TAC AAG GAT GGG ACA ATT AAA TTT GAT TTT ACC AAA TAT ACT AAA AAT 3936 Tyr Lys Asp Gly Thr He Lys Phe Asp Phe Thr Lys Tyr Ser Lys Asn 2135 2140 2145 GAA CAA GGA TTA TTT TAT GAC AGT GGA TTA AAT TGG GAC TTT AAA ATT 3984 Glu Gin Gly Leu Phe Tyr Asp Ser Gly Leu Asn Trp Asp Phe Lys He 2150 2155 2160 AAT GCT ATT ACT TAT GAT GGT AAA GAG ATG AAT GTT TTT CAT AGA TAT 4032 Asn Ala He Thr Tyr Asp Gly Lys Glu Met Asn Val Phe His Arg Tyr 2165 2170 2175 AAT AAA TAG 4041 Asn Lys 2180 (2) INFORMATION FOR SEQ ID NO:23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1346 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MDI-ECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:23: Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu Gin 1 5 10 15 Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser He Ser Leu 20 25 30 Leu Asn Asn Glu Val He Lys Ala Glu Gin Leu Asn He Asn Ser Gin 35 40 45 Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu 50 55 60 Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys 65 70 75 80 Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn 85 90 95 Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr 100 105 110 Phe Ser Met Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu 115 120 125 He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr 130 135 140 Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr 145 150 155 160 Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin 165 170 175 Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 180 185 190 Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr 195 200 205 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He 210 215 220 Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val 225 230 235 240 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu 245 250 255 Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He 260 265 270 Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala 275 280 285 Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala leu Asp Gly Tyr Ala Arg 290 295 300 Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser 305 310 315 320 Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu 325 330 335 Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly 340 345 350 Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys 355 360 365 Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr 370 375 380 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg 385 390 395 400 Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr 405 410 415 Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp 420 425 430 Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He Lys 435 440 445 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn Met Lys 450 455 460 Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu Leu Ala 465 470 475 480 Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Tyr Ala Asp Ser Lys 485 490 495 Thr Asn Gin He Ser Thr Thr Gin Lys Asn Gin Gin Lys Glu Met Asp 500 505 510 Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe Ser Asn 515 520 525 Leu Thr Met Phe Ala Pro Thr Arg Asp Ser Thr Leu He Tyr Asp Gin 530 535 540 Gin Thr Ala Asn Lys Leu Leu Asp Lys Lys Gin Gin Glu Tyr Gin Ser 545 550 555 560 He Arg Trp He Gly Leu He Gin Ser Lys Glu Thr Gly Asp Phe Thr 565 570 575 Phe Asn Leu Ser Glu Asp Glu Gin Ala He He Glu He Asn Gly Lys 580 585 590 He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val His leu Glu Lys 595 600 605 Gly Lys Leu Val Pro He Lys He Glu Tyr Gin Ser Asp Thr Lys Phe 610 615 620 Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu Phe Lys He Asp 625 630 635 640 Ser Gin Asn Gin Pro Gin Gin Val Gin Gin Asp Glu Leu Arg Asn Pro 645 650 655 Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Pro Ser Lys 660 665 670 He Asn Leu Phe Thr Gin Lys Met Lys Arg Glu He Asp Glu Asp Thr 675 680 685 Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn Gly Tyr 690 695 700 Thr He Gin Asn Arg He Ala Val Lys Trp Asp Asp Ser Leu Ala Ser 705 710 715 720 Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Glu Ser His Thr Val 725 730 735 Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu Asp Leu 740 745 750 Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe Pro Ser 755 760 765 Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu Asn Leu 770 775 780 Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr Thr Asn 785 790 795 800 Thr Glu Gly Ala Ser Val Glu Ala Gly He Gly Pro Lys Gly He Ser 805 810 815 Phe Gly Val Ser Val Asn Tyr Gin His Ser Glu Thr Val Ala Gin Glu 820 825 830 Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala Ser Ala 835 840 845 Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr Gly Ala 850 855 860 He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn Asp Thr 865 870 875 880 He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Asn He Ser 885 890 895 Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gin Asn Gly He Ala He Thr 900 905 910 Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn Lys Lys Gin 915 920 925 Val Asp Asn Leu Leu Asn Asn Lys Pro Met Met Leu Glu Thr Asn Gin 930 935 940 Thr Asp Gly Val Tyr Lys He Lys Asp Thr His Gly Asn He Val Thr 945 950 955 960 Gly Gly Glu Trp Asn Gly Val He Gin Gin He Lys Ala Lys Thr Ala 965 970 975 Ser He He Val Asp Asp Gly Glu Arg Val Ala Glu Lys Arg Val Ala 980 985 990 Ala Lys Asp Tyr Glu Asn Pro Glu Asp Lys Thr Pro Ser Leu Thr Leu 995 1000 1005 Lys Asp Ala Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu He Glu 1010 1015 1020 Gly Leu Leu Tyr Tyr Lys Asn Lys Pro He Tyr Glu Ser Ser Val Met 1025 1030 1035 1040 Thr y Leu Asp Glu Asn Thr Ala Lys Glu Val Thr Lys Gin Leu Asn 1045 1050 1055 Asp Thr Thr Gly Lys Phe Lys Asp Val Ser His Leu Tyr Asp Val Lys 1060 1065 1070 Leu Thr Pro Lys Met Asn Val Thr He Lys Leu Ser He Leu Tyr Asp 1075 1080 1085 Asn Ala Glu Ser Asn Asp Asn Ser He Gly Lys Trp Thr Asn Thr Asn 1090 1095 1100 He Val Ser Gly Gly Asn Asn Gly Lys Lys Gin Tyr Ser Ser Asn Asn 1105 1110 1115 1120 Pro Asp Ala Asn Leu Thr Leu Asn Thr Asp Ala Gin Glu Lys Leu Asn 1125 1130 1135 Lys Asn Arg Asp Tyr Tyr He Ser Leu Tyr Met Lys Ser Glu Lys Asn 1140 1145 1150 Thr Gin Cys Glu He Thr He Asp Gly Glu He Ty Pro He Thr Thr 1155 1160 1165 Lys Thr Val Asn Val Asn Lys Asp Asn Tyr Lys Arg Leu Asp He He 1170 1175 1180 Ala His Asn He Lys Ser Asn Pro He Ser Ser Leu His He Lys Thr 1185 1190 1195 1200 Asn Asp Glu He Thr Leu Phe Trp Asp Asp He Ser He Thr Asp Val 1205 1210 1215 Ala Ser He Lys Pro Glu Asn Leu Thr Asp Ser Glu He Lys Gin He 1220 1225 1230 Tyr Ser Arg Tyr Gly He Lys Leu Glu Asp Gly He Leu He Asp Lys 1235 1240 1245 Lys Gly Gly He His Tyr Gly Glu Phe He Asn Glu Ala Ser Phe Asn 1250 1255 1260 He Glu Pro Leu Gin Asn Tyr Val Thr Lys Tyr Glu Val Thr Tyr Ser 1265 1270 1275 1280 Ser Glu Leu Gly Pro Asn Val Ser Asp Thr Leu Glu Ser Asp Lys He 1285 1290 1295 Tyr Lys Asp Gly Thr He Lys Phe Asp Phe Thr Lys Tyr Ser Lys Asn 1300 1305 1310 Glu Gin Gly Leu Phe Tyr Asp Ser Gly Leu Asn Trp Asp Phe Lys He 1315 1320 1325 sn Ala He Thr Tyr Asp Gly Lys Glu Met Asn Val Phe His Arg Tyr 1330 1335 1340 sn Lys 1345 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1399 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii ) MOLECULE TYPE: DMA (genomic) (ix) FEATURE: (A) NAME/KEY: misc_feature (B) LOCATION: 1. .1386 (D) OTHER INFORMATION: /note= "Maize optimized ENA sequence for VIP2A(a) protein from AB78 " (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 24 : ATGAAGCGCA TGGAGGGCAA GCTGTTCATG GTGAGCAAGA AGCTCCAGGT QGTGACCAAG 60 ACCGTGCTGC TGAGCACCGT GTTCAGCATC AGCX_TGCTGA ACAACGAGCT GATCAAGGCC 120 GAGCAGCTGA ACATCAACAG CCAGAGCAAG TACACCAACC TCCAGAACCT GAAGATCACC 180 GACAAGGTGG AGGACTTCAA QGAGGACAAG GAGAAGGCCA AGGAGTGQGG CAAGGAGAAG 240 GAGAAGGAGT GGAAGCTTAC CGCCACCGAG AAGGGCAAGA TGAACAACTT CCTGGACAAC 300 AAGAACGACA TCAAGACCAA CTACAAGGAG ATCACCTTCA G<_ATQGCCGG CAGCTTCGAG 360 GACGAGATCA AGGACCTGAA GGAGATCGAC AAGATGTTCG ACAAGACCAA CCTGAGCAAC 420 AGCATCATCA CCTACAAGAA CGTGGAGCCC ACCACCATCG GCTTCAACAA GAGC-CTGACC 480 GAGGGCAACA CCATCAACAG CCΛCGCCATG GCCCAGTTCA AGGAGCAGTT CCTGGACCGC 540 GACATCAAGT TCGACAGCTA CCTGGACACC CACCTGACCG CX-CAGCAGCT GAGCAGCAAG 600 GAGCGCGTGA TCCTGAAGGT GACCGTCCCC AGCGGCAAGG GCAGCACCAC CCCCACCAAG 660 GCCGGCGTGA TCCTGAACAA CAGCGAGTAC AAGATGCTGA TCGACAACGG CTACATGGTG 720 CACGTGGACA AGGTGAGCAA GGTGGTGAAG AAGGGCGTGG AGTGCCTCCA GATCGAGGGC 780 ACCCTGAAGA AGAGTCTAGA CTTCAAGAAC GACATCAACG CCGAGGCCCA CAGCTGGGGC 840 ATGAAGAACT AO-AGGAGTG GGCCAAGGAC CTGACCGACA GCCAGCGCGA GGCCCTGGAC 900 GGCTACGCCC GCCAGGACTA CAAGGAGATC AACAACTACC TGCGCAACCA GGGCGGCAGC 960 GGCAACGAGA AGCTGGACGC CCAGATCAAG AACATCAGCG ACGCCCTGGG CAAGAAGCCC 1020 ATCCCCGAGA ACATCACCGT GTACCGCTGG TGCX-GCATGC CCGAGTICGG CTACCAGATC 1080 AGCGACCCCC TGCCCAGCCT GAAGGACTTC GAGGAGCAGT TCCTGAACAC CATCAAGGAG 1140 GACAAGGGCT ACATGAGCAC CAGCCTGAGC AGCGAGCGCC TCGCCGCCTT CXIGCAGCCGC 1200 AAGATCATCC TCCGCCTGCA GGTGCCCAAG GGCAGCACCG GCGCCTACCT GAC-CGCCATC 1260 GGα_GCTTCG CCAGCGAGAA QGAGATCCTG CTGGACAAGG ACAGCAAGTA CCACATCGAC 1320 AAQGTGACCG AGGTGATCAT CAAGGGCGTG AAGCGCTACG TGGTGGACGC CACCCTGCTG 1380 ACCAACTAGA TCTGAGCTC 1399 (2) INFORMATION FOR SEQ ID NO:25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (B) TYPE: amino acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATION: 1..19 (D) OTHER INFORMATION: /note= "Secretion signal peptide to secrete VIP2 out of a cell" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25: Gly Trp Ser Trp He Phe Leu Phe Leu Leu Ser Gly Ala Ala Gly Val 1 5 10 15 His Cys Leu (2) INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LE-NK3TΗ: 2655 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: misc_feature (B) LOCATION: 1..2655 (D) OTHER INFORMATICN: /note= "maize optimized ENA sequence encoding VIPlA(a) " (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 26 : ATGAAGAACA TGAAGAAGAA GCTGGCCAGC GTGGTGACCT GCA-XCTGCT GGCCCCCATG 60 TTCCTGAACG GCAACGTGAA CGCCGTGTAC GCCGACAGCA AGACCAACCA GATCAGCACC 120 ACCCAGAAGA ACCAGCAGAA GGAGATGGAC CGC-AAGGGCC TGCTGGGCTA CTACTTCAAG 180 GGCAAGGACT TCAGCAACCT GACCATGTTC GCCCCCACGC GTGACAGCAC CCTGATCTAC 240 GACCAGCAGA CCGCCAACAA GCV3CTGGAC AAGAAGCAGC AGGAGTACCA GAGCATCCGC 300 TGGATCGGCC TGATCCAGAG CAAQGAGACC GGCGACTTCA CX-TTCAACCT GAGCGAQGAC 360 GAGCAGGCCA TCATCGAGAT CAACGGCAAG ATCATCAGCA ACAAGGGCAA GGAGAAGCAG 420 GTGGTGCACC TGGAGAAGGG CAAGCTGGTG CCCATCAAGA TCGAGTACCA GAGCGACACC 480 AAGTTCAACA TCGACAGCAA GACCTTCAAG GAGCTGAAGC TTTTCAAGAT CGACAGCCAG 540 AACCAGCCCC AGCAGGTGCA GCAGGACGAG (-TGCGCAACC CCGAOTTCAA CAAGAAGGAG 600 AGCCAGGAGT TCCTGGCCAA GCCCAGCAAG ATCAACCTCT TCACCCAGCA CΑTGAAGCGC 660 GAGATCGACG AGGACACCGA CACCGACGGC GACAGCATCC CCGACCTGTG GGAGGAGAAC 720 GGCTACACCA TCCAGAACCG CATCGCCGTG AAGTGGGACG ACAGCCTGGC TAGCAAGGGC 780 TACACCAAGT TCGTGAGCAA CCCCCTGGAG AGCCACACCG TGGGCGACCC CTACACCGAC 840 TACGAGAAGG CCGCCCGCGA CX-TQGACCTG AGCAACGCCA AGGAGACCTT CAACCCCCTG 900 GTGGCCGCCT TCCCCAGCGT GAACGTGAGC ATGGAGAAGG TGATCCTGAG C>CCCAACGAG 960 AACCTGAGCA ACAGCGTGGA GAGCCACTCG AGCACCAACT GGAGCTACAC CAACACCGAG 1020 GGCGCCAGCG TGGAGGCCGG CATCGGTCCC AAGGGCATCA GCTTCGGCGT GAGCGTGAAC 1080 TACCAGCACA GCGAGACCGT GCKX-CAGGAG TGCJGGCACCA GCAO-GGCAA CACCAGCCAG 1140 TTCAACACCG CC.AGCGCCGG CTACCTGAAC GCCAACGTGC GCTACAACAA CGTGGGCACC 1200 GGCGCCATCT ACGACGTGAA GCCCACCACC AGCTTCGTGC TGAACAACGA CACCATCGCC 1260 ACCATCACCG CCAAGTCGAA TTCCACCGCC CTGAACATCA GCCCCGGCGA GAGCTACCCC 1320 AAGAAGGGCC AGAACGGCAT CGCCATCACC AGCATGGACG ACTTCAACAG CCACCCCATC 1380 ACX-CTGAACA AGAAC CAGCT GGACAACCTG CTGAACAACA AGCCCATGAT GCTGGAGACC 1440 AACCAGACCG ACGGCGTCTA CAAGATCAAG GACACCCACG GCAACATCGT GACGGGCGGC 1500 GAGTGGAACG GCGTGATCCA GCAGATCAAG GCCAAGACCG CCAGCATCAT CGTCGACGAC 1560 GGCGAGCGCG TGGCCGAGAA GCX_α_TGGCC G CAAGGACT ACGAGAACCC CGAGGACAAG 1620 ACCCCCAGCC TGACCCTGAA GGACGCCCTG AAGCTGAGCT ACCCCGACGA GATCAAGGAG 1680 ATCX_AGGGCT TGCTCTACTA CAAGAACAAG CCCATCTACG AGAGCAGCGT GATGACCTAT 1740 CTAGACGAGA ACACCGCCAA GGAGGTGACC AAGCAGCTGA ACGACACCAC CGGCAAGTTC 1800 AAGGACGTGA GCCACCTCTA CGACGTGAAG C-TGACCCCCA AGATGAACGT GACCATCAAG 1860 CTGAGCATCC TCTACGACAA CGCCGAGAGC AACGACAACA GCATCGGCAA GTGGACCAAC 1920 ACCAACATCG TGAGCQGCGG (.AACAACGGC AAGAAGCACT ACAGCAGCAA CAACCCCGAC 1980 GCCAACCTGA CCCTGAACAC CGACGCCCAG GAGAAGCTGA ACAAGAACCG CGACTACTAC 2040 ATCAGCCTCT ACATGAAGAG CGAGAAGAAC ACCCAGTGCG AGATCACCAT CGAC.GGCGAG 2100 ATATACCCCA TCACCACCAA GACCGTGAAC GTGAACAAGG ACAACTACAA GCGCCTGGAC 2160 ATCATCGCCC ACAACATCAA GAGCAACCCC ATCAGCAGCC TGCACATCAA GACCAACGAC 2220 GAGATCACCC TGTTCTGGGA CGACATATCG ATTACCGACG TCGCCAGCAT C.AAGCCCGAG 2280 AACCTGACCG ACAGOGAGAT CAAGCAGATA TACAGTCGCT ACGGCATCAA GCTGGAGGAC 2340 «_X_ATCCTGA TCGACAAGAA AGCX.GQCATC CACTACGGCG A__flTCATCAA CGAGGCCAGC 2400 TTCAACATCG AGCCCCTGCA GAACTACGTG ACCAAGTACG AGGTGACCTA CAGCAGCGAG 2460 CTGGGCCCCA AO-TGAGCGA CACCCTGGAG AGCGACAAGA TTTACAAQGA CGGCACCATC 2520 AAGTTCGACT TCACCAAGTA CAGCAAGAAC GAGCAGGGCC TCJTTCTAOGA CAGCGGCCTG 2580 AACTGGGACT TCAAGATCAA CGCCATCACC TACGACGGCA AGGAGATGAA CGTGTTCCAC 2640 CGCTACAACA AGTAG 2655 (2 ) INFORMATION FOR SEQ ID NO : 27 : (i ) SEQUENCE CHARACTERISTICS : (A) LENGTH: 1389 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS : single (D) TOPOLOGY: linear (ii) MOILECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: misc_feature (B) LOCATION: 1..1389 (D) OTHER INFORMATION: /note= "maize optimized ENA sequence encoding VIP2A (a) " (xi ) SEQUENCE DESCRIPTION: SEQ ID NO:27 : ATGAAGCGCA TGGAGGGCAA GCTGTTCATG GIGAGCAAGA AGCTCCAGGT QGTGACCAAG 60 ACCGTGCTGC TGAGCACCGT GTTCAGCATC AC.CCTGCTGA ACAACGAGGT GATCAAGGCC 120 GAGC-AGCTGA ACATCAACAG CCAGAGCAAG TACACCAACC TCCAGAACCT GAAGATCACC 180 C_ACAAGGTGG AGGACTTCAA GGAQGACAAG GAGAAGGCCA AGGAGTGGGG CAAGGAGAAG 240 GAGAAGGAGT GGAAGCTTAC O-CCACCGAG AAGGGCAAGA TGAACAACTT CX_TGGACAAC 300 AAGAACGACA TCAAGACCAA CTACAAGGAG ATCAO-TTCA GCATAGCCGG CAGCTTCGAG 360 GACGAGATCA AGGACCTGAA OSAGATCGAC AAGATGTTCG ACAAGACCAA CCTGAGCAAC 420 AGCATCATCA CCTACAAGAA CGTGGAGCCC ACCACCATCG GCTTCAACAA GAGCCTGACC 480 GAGGGCAACA CCATCAACAG CGACGCCATG GCCCAGTTCA AGGAGCAGTT CX-TGGACCGC 540 GACATCAAGT TCGACAGCTA CX.TGGACACC C-AO-TC-ACCG CCCAGCAGGT GAGCAGCAAG 600 GAGCGCGTGA TCCTGAAGGT GACCGTCCCC AGCGGCAAGG GCAGCACCAC CCCCACCAAG 660 GC.CGGCGTGA TCCTGAACAA CAGCGACTAC AAGATGCTGA TCGACAACGG CTACATGGTG 720 CAO-TGGACA AGGTGAGCAA GGTGGTGAAG AAGGGCGTGG AGTGCOTCCA GATCGAGGGC 780 ACCCTGAAGA AGAGTCTAGA CTTCAAGAAC GACATCAACG CCGAGGCCCA CAGCTGQGGC 840 ATGAAGAACT ACGAGGAGTG GGCCAAGGAC CTGACCGACA GCCAGCGCGA GGCCCTGGAC 900 GGCTACGCCC GCCAGGACTA CAAGGAGATC AACAACTACC TGCGCAACCA GGGCGGCAGC 960 GGCAACGAGA AGCTGGACGC CCAGATCAAG AACATCAGCG ACX.CCCTGGG CAAGAAGCCC 1020 ATCCCCGAGA ACATCACCGT CTACCGCTGG TG033CATGC CCGAGTTCGG CTACCAGATC 1080 AGCGACCCCC TGCCCAGCCT GAAGGACTTC GAGGAGCACT TCCTGAACAC CATCAAGGAG 1140 GAC-AAGGGCT ACATGAGCAC CAGCCTGAGC AGCGAGCGCC TGGCCGCCTT CGGCAGCCGC 1200 AAGATCATCC TGCGCCTGCA QCTGCCCAAG GGCAGCACTG GTGCCTACCT GAGCGCCATC 1260 GO_GGCTTCG CCAGCGAGAA GGAGATCCTG CTGGATAAGG ACAGCAAGTA CCACATCGAC 1320 AAGGTGACCG AGGTGATCAT CAAGGGCGTG AAGCGCTACG TGGTGGAOGC CACCCTGCTG 1380 ACCAACTAG 1389 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2378 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOIOLOGY: linear (ii) MOI-J-CULE TYPE: DMA (genomic) (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 9..2375 (D) OTHER INFORMATION: /note= "Native ENA sequence encoding VIP3A(a) protein from AB88 as contained in pCIB7104" (xi) SEQUENCE DESCRIPTION: SEQ ID O:28: AGATGAAC ATG AAC AAG AAT AAT ACT AAA TTA AGC ACA AGA GCC TTA CCA 50 Met Asn Lys Asn Asn Thr Lys Leu Ser Thr Arg Ala Leu Pro 1 5 10 AGT TTT ATT GAT TAT TTT AAT GGC ATT TAT GGA TTT GCC ACT GGT ATC 98 Ser Phe He Asp Tyr Phe Asn Gly He Tyr Gly Phe Ala Thr Gly He 15 20 25 30 AAA GAC ATT ATG AAC ATG ATT TTT AAA ACG GAT ACA GGT GCT GAT CTA 146 Lys Asp He Met Asn Met He Phe Lys Thr Asp Thr Gly Gly Asp Leu 35 40 45 ACC CTA GAC GAA ATT TTA AAG AAT CAG CAG TTA CTA AAT GAT ATT TCT 194 Thr Leu Asp Glu He Leu Lys Asn Gin Gin Leu Leu Asn Asp He Ser 50 55 60 GGT AAA TTG GAT GGG GTG AAT GGA AGC TTA AAT GAT CTT ATC GCA CAG 242 Gly Lys Leu Asp Gly Val Asn Gly Ser Leu Asn Asp Leu He Ala Gin 65 70 75 GGA AAC TTA AAT ACA GAA TTA TCT AAG GAA ATA TTA AAA ATT GCA AAT 290 Gly Asn Leu Asn Thr Glu Leu Ser Lys Glu He Leu Lys He Ala Asn 80 85 90 GAA CAA AAT CAA GTT TTA AAT GAT GTT AAT AAC AAA CTC GAT GCG ATA 338 Glu Gin Asn Gin Val Leu Asn Asp Val Asn Asn Lys Leu Asp Ala He 95 100 105 110 AAT ACG ATG CTT CGG GTA TAT CTA CCT AAA ATT ACC TCT ATG TTG AGT 386 Asn Thr Met Leu Arg Val Tyr Leu Pro Lys He Thr Ser Met Leu Ser 115 120 125 GAT CTA ATG AAA CAA AAT TAT GCG CTA AGT CTG CAA ATA GAA TAC TTA 434 Asp Val Met Lys Gin Asn Tyr Ala Leu Ser Leu Gin He Glu Tyr Leu 130 135 140 AGT AAA CAA TTG CAA GAG ATT TCT GAT AAG TTG GAT ATT ATT AAT CTA 482 Ser Lys Gin Leu Gin Glu He Ser Asp Lys Leu Asp He He Asn Val 145 150 155 AAT CTA CTT ATT AAC TCT ACA CTT ACT GAA ATT ACA CCT GCG TAT CAA 530 Asn Val Leu He Asn Ser Thr Leu Thr Glu He Thr Pro Ala Tyr Gin 160 165 170 AGG ATT AAA TAT GTG AAC GAA AAA TTT GAG GAA TTA ACT TTT GCT ACA 578 Arg He Lys Tyr Val Asn Glu Lys Phe Glu Glu Leu Thr Phe Ala Thr 175 180 185 190 GAA ACT AGT TCA AAA GTA AAA AAG GAT GGC TCT CCT GCA GAT ATT CTT 626 Glu Thr Ser Ser Lys Val Lys Lys Asp Gly Ser Pro Ala Asp He Leu 195 200 205 GAT GAG TTA ACT GAG TTA ACT GAA CTA GCG AAA AGT GTA ACA AAA AAT 674 Asp Glu Leu Thr Glu Leu Thr Glu Leu Ala Lys Ser Val Thr Lys Asn 210 215 220 GAT GTG GAT GGT TTT GAA TTT TAC CTT AAT ACA TTC CAC GAT GTA ATG 722 Asp Val Asp Gly Phe Glu Phe Tyr Leu Asn Thr Phe His Asp Val Met 225 230 235 GTA GGA AAT AAT TTA TTC GGG CCT TCA GCT TTA AAA ACT GCA TCG GAA 770 Val Gly Asn Asn Leu Phe Gly Arg Ser Ala Leu Lys Thr Ala Ser Glu 240 245 250 TTA ATT ACT AAA GAA AAT GTG AAA ACA ACT GGC ACT GAG GTC GGA AAT 818 Leu He Thr Lys Glu Asn Val Lys Thr Ser Gly Ser Glu Val Gly Asn 255 260 265 270 GTT TAT AAC TTC TTA ATT GTA TTA ACA GCT CTG CAA GCC CAA GCT TTT 866 Val Tyr Asn Phe Leu He Val Leu Thr Ala Leu Gin Ala Gin Ala Phe 275 280 285 CTT ACT TTA ACA ACA TGC CGA AAA TTA TTA GGC TTA GCA GAT ATT GAT 914 Leu Thr Leu Thr Thr Cys Arg Lys Leu Leu Gly Leu Ala Asp He Asp 290 295 300 TAT ACT TCT ATT ATG AAT GAA CAT TTA AAT AAG GAA AAA GAG GAA TTT 962 Tyr Thr Ser He Met Asn Glu His Leu Asn Lys Glu Lys Glu Glu Phe 305 310 315 AGA GTA AAC ATC CTC CCT ACA CTT TCT AAT ACT TTT TCT AAT CCT AAT 1010 Arg Val Asn He Leu Pro Thr Leu Ser Asn Thr Phe Ser Asn Pro Asn 320 325 330 TAT GCA AAA GTT AAA GGA ACT GAT GAA GAT GCA AAG ATG ATT GTG GAA 1058 Tyr Ala Lys Val Lys Gly Ser Asp Glu Asp Ala Lys Met He Val Glu 335 340 345 350 GCT AAA CCA GGA CAT GCA TTG ATT GGG TTT GAA ATT AGT AAT GAT TCA 1106 Ala Lys Pro Gly His Ala Leu He Gly Phe Glu He Ser Asn Asp Ser 355 360 365 ATT ACA CTA TTA AAA GTA TAT GAG GCT AAG CTA AAA CAA AAT TAT CAA 1154 He Thr Val Leu Lys Val Tyr Glu Ala Lys Leu Lys Gin Asn Tyr Gln 370 375 380 GTC GAT AAG GAT TCC TTA TCG GAA GTT ATT TAT GGT GAT ATG GAT AAA 1202 Val Asp Lys Asp Ser Leu Ser Glu Val He Tyr Gly Asp Met Asp Lys 385 390 395 TTA TTG TGC CCA GAT CAA TCT GAA CAA ATC TAT TAT ACA AAT AAC ATA 1250 Leu Leu Cys Pro Asp Gin Ser Glu Gin He Tyr Tyr Thr Asn Asn He 400 405 410 GTA TTT CCA AAT GAA TAT GTA ATT ACT AAA ATT GAT TTC ACT AAA AAA 1298 Val Phe Pro Asn Glu Tyr Val He Thr Lys He Asp Phe Thr Lys Lys 415 420 425 430 ATG AAA ACT TTA AGA TAT GAG GTA ACA GCG AAT TTT TAT GAT TCT TCT 1346 Met Lys Thr Leu Arg Tyr Glu Val Thr Ala Asn Phe Tyr Asp Ser Ser 435 440 445 ACA GGA GAA ATT GAC TTA AAT AAG AAA AAA GTA GAA TCA AGT GAA GCG 1394 Thr Gly Glu He Asp Leu Asn Lys Lys Lys Val Glu Ser Ser Glu Ala 450 455 460 GAG TAT AGA ACG TTA ACT GCT AAT GAT GAT GGG GTG TAT ATG CCG TTA 1442 Glu Tyr Arg Thr Leu Ser Ala Asn Asp Asp Gly Val Tyr Met Pro Leu 465 470 475 GGT GTC ATC AGT GAA ACA TTT TTG ACT CCG ATT AAT GGG TTT GGC CTC 1490 Gly Val He Ser Glu Thr Phe Leu. Thr Pro He Asn Gly Phe Gly Leu 480 485 490 CAA GCT GAT GAA AAT TCA AGA TTA ATT ACT TTA ACA TCT AAA TCA TAT 1538 Gin Ala Asp Glu Asn Ser Arg Leu He Thr Leu Thr Cys Lys Ser Tyr 495 500 505 510 TTA AGA GAA CTA CTG CTA GCA ACA GAC TTA AGC AAT AAA GAA ACT AAA 1586 Leu Arg Glu Leu Leu Leu Ala Thr Asp Leu Ser Asn Lys Glu Thr Lys 515 520 525 TTG ATC GTC CCG CCA AGT GGT TTT ATT AGC AAT ATT CTA GAG AAC GGG 1634 Leu He Val Pro Pro Ser Gly Phe He Ser Asn He Val Glu Asn Gly 530 535 540 TCC ATA GAA GAG GAC AAT TTA GAG CCG TGG AAA GCA AAT AAT AAG AAT 1682 Ser He Glu Glu Asp Asn Leu Glu Pro Trp Lys Ala Asn Asn Lys Asn 545 550 555 GCG TAT GTA GAT CAT ACA GGC GGA GTG AAT GGA ACT AAA GCT TTA TAT 1730 Ala Tyr Val Asp His Thr Gly Gly Val Asn Gly Thr Lys Ala Leu Tyr 560 565 570 GTT CAT AAG GAC GGA GGA ATT TCA CAA TTT ATT GGA GAT AAG TTA AAA 1778 Val His Lys Asp Gly Gly He Ser Gin Phe He Gly Asp Lys Leu Lys 575 580 585 590 CCG AAA ACT GAG TAT CTA ATC CAA TAT ACT GTT AAA GGA AAA CCT TCT 1826 Pro Lys Thr Glu Tyr Val He Gin Tyr Thr Val Lys Gly Lys Pro Ser 595 600 605 ATT CAT TTA AAA GAT GAA AAT ACT GGA TAT ATT CAT TAT GAA GAT ACA 1874 He His Leu Lys Asp Glu Asn Thr Gly Tyr He His Tyr Glu Asp Thr 610 615 620 AAT AAT AAT TTA GAA GAT TAT CAA ACT ATT AAT AAA CGT TTT ACT ACA 1922 Asn Asn Asn Leu Glu Asp Tyr Gin Thr He Asn Lys Arg Phe Thr Thr 625 630 635 GGA ACT GAT TTA AAG GGA GTG TAT TTA ATT TTA AAA AGT CAA AAT GGA 1970 Gly Thr Asp Leu Lys Gly Val Tyr Leu He Leu Lys Ser Gin Asn Gly 640 645 650 GAT GAA GCT TGG GGA GAT AAC TTT ATT ATT TTG GAA ATT ACT CCT TCT 2018 Asp Glu Ala Trp Gly Asp Asn Phe He He Leu Glu He Ser Pro Ser 655 660 665 670 GAA AAG TTA TTA AGT CCA GAA TTA ATT AAT ACA AAT AAT TGG ACG AGT 2066 Glu Lys Leu Leu Ser Pro Glu Leu He Asn Thr Asn Asn Trp Thr Ser 675 680 685 ACG GGA TCA ACT AAT ATT AGC GGT AAT ACA CTC ACT CTT TAT CAG GGA 2114 Thr Gly Ser Thr Asn He Ser Gly Asn Thr Leu Thr Leu Tyr Gin Gly 690 695 700 GGA CGA GGG ATT CTA AAA CAA AAC CTT CAA TTA GAT ACT TTT TCA ACT 2162 Gly Arg Gly He Leu Lys Gin Asn Leu Gin Leu Asp Ser Phe Ser Thr 705 710 715 TAT AGA GTG TAT TTT TCT GTG TCC GGA GAT GCT AAT GTA AGG ATT AGA 2210 Tyr Arg Val Tyr Phe Ser Val Ser Gly Asp Ala Asn Val Arg He Arg 720 725 730 AAT TCT AGG GAA GTG TTA TTT GAA AAA AGA TAT ATG AGC GGT GCT AAA 2258 Asn Ser Arg Glu Val Leu Phe Glu Lys Arg Tyr Met Ser Gly Ala Lys 735 740 745 750 GAT GTT TCT GAA ATG TTC ACT ACA AAA TTT GAG AAA GAT AAC TTT TAT 2306 Asp Val Ser Glu Met Phe Thr Thr Lys Phe Glu Lys Asp Asn Phe Tyr 755 760 765 ATA GAG CTT TCT CAA GGG AAT AAT TTA TAT GGT GGT CCT ATT CTA CAT 2354 He Glu Leu Ser Gin Gly Asn Asn Leu Tyr Gly Gly Pro He Val His 770 775 780 TTT TAC GAT GTC TCT ATT AAG TAA 2378 Phe Tyr Asp Val Ser He Lys 785 (2) INFORMATION FOR SEQ ID NO:29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 789 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29: Met Asn Lys Asn Asn Thr Lys Leu Ser Thr Arg Ala Leu Pro Ser Phe 1 5 10 15 He Asp Tyr Phe Asn Gly He Tyr Gly Phe Ala Thr Gly He Lys Asp 20 25 30 He Met Asn Met He Phe Lys Thr Asp Thr Gly Gly Asp Leu Thr Leu 35 40 45 Asp Glu He leu Lys Asn Gin Gin Leu Leu Asn Asp He Ser Gly Lys 50 55 60 Leu Asp Gly Val Asn Gly Ser Leu Asn Asp Leu He Ala Gin Gly Asn 65 70 75 80 Leu Asn Thr Glu Leu Ser Lys Glu He Leu Lys He Ala Asn Glu Gin 85 90 95 Asn Gin Val Leu Asn Asp Val Asn Asn Lys Leu Asp Ala He Asn Thr 100 105 110 Met Leu Arg Val Tyr Leu Pro Lys He Thr Ser Met Leu Ser Asp Val 115 120 125 Met Lys Gin Asn Tyr Ala Leu Ser Leu Gin He Glu Tyr Leu Ser Lys 130 135 140 Gin Leu Gin Glu He Ser Asp Lys Leu Asp He He Asn Val Asn Val 145 150 155 160 Leu He Asn Ser Thr Leu Thr Glu He Thr Pro Ala Tyr Gin Arg He 165 170 175 Lys Tyr Val Asn Glu Lys Phe Glu Glu Leu Thr Phe Ala Thr Glu Thr 180 185 190 Ser Ser Lys Val Lys Lys Asp Gly Ser Pro Ala Asp He Leu Asp Glu 195 200 205 Leu Thr Glu Leu Thr Glu Leu Ala Lys Ser Val Thr Lys Asn Asp Val 210 215 220 Asp Gly Phe Glu Phe Tyr Leu Asn Thr Phe His Asp Val Met Val Gly 225 230 235 240 Asn Asn Leu Phe Gly Arg Ser Ala Leu Lys Thr Ala Ser Glu Leu He 245 250 255 Thr Lys Glu Asn Val Lys Thr Ser Gly Ser Glu Val Gly Asn Val Tyr 260 265 270 Asn Phe leu He Val Leu Thr Ala Leu Gin Ala Gin Ala Phe Leu Thr 275 280 285 Leu Thr Thr Cys Arg Lys Leu Leu Gly Leu Ala Asp He Asp Tyr Thr 290 295 300 Ser He Met Asn Glu His Leu Asn Lys Glu Lys Glu Glu Phe Arg Val 305 310 315 320 Asn He Leu Pro Thr Leu Ser Asn Thr Phe Ser Asn Pro Asn Tyr Ala 325 330 335 Lys Val Lys Gly Ser Asp Glu Asp Ala Lys Met He Val Glu Ala Lys 340 345 350 Pro Gly His Ala Leu He Gly Phe Glu He Ser Asn Asp Ser He Thr 355 360 365 Val Leu Lys Val Tyr Glu Ala Lys Leu Lys Gin Asn Tyr Gin Val Asp 370 375 380 Lys Asp Ser Leu Ser Glu Val He Tyr Gly Asp Met Asp Lys Leu Leu 385 390 395 400 Cys Pro Asp Gin Ser Glu Gin He Tyr Tyr Thr Asn Asn He Val Phe 405 410 415 Pro Asn Glu Tyr Val He Thr Lys He Asp Phe Thr Lys Lys Met Lys 420 425 430 Thr Leu Arg Tyr Glu Val Thr Ala Asn Phe Tyr Asp Ser Ser Thr Gly 435 440 445 Glu He Asp Leu Asn Lys Lys Lys Val Glu Ser Ser Glu Ala Glu Tyr 450 455 460 Arg Thr Leu Ser Ala Asn Asp Asp Gly Val Tyr Met Pro Leu Gly Val 465 470 475 480 He Ser Glu Thr Phe leu Thr Pro He Asn Gly Phe Gly Leu Gin Ala 485 490 495 Asp Glu Asn Ser Arg Leu He Thr Leu Thr Cys Lys Ser Tyr Leu Arg 500 505 510 Glu Leu Leu Leu Ala Thr Asp Leu Ser Asn Lys Glu Thr Lys Leu He 515 520 525 Val Pro Pro Ser Gly Phe He Ser Asn He Val Glu Asn Gly Ser He 530 535 540 Glu Glu Asp Asn Leu Glu Pro Trp Lys Ala Asn Asn Lys Asn Ala Tyr 545 550 555 560 Val Asp His Thr Gly Gly Val Asn Gly Thr Lys Ala Leu Tyr Val His 565 570 575 Lys Asp Gly Gly He Ser Gin Phe He Gly Asp Lys Leu Lys Pro Lys 580 585 590 Thr Glu Tyr Val He Gin Tyr Thr Val Lys Gly Lys Pro Ser He His 595 600 605 Leu Lys Asp Glu Asn Thr Gly Tyr He His Tyr Glu Asp Thr Asn Asn 610 615 620 Asn Leu Glu Asp Tyr Gin Thr He Asn Lys Arg Phe Thr Thr Gly Thr 625 630 635 640 Asp Leu Lys Gly Val Tyr Leu He Leu Lys Ser Gin Asn Gly Asp Glu 645 650 655 Ala Trp Gly Asp Asn Phe He He Leu Glu He Ser Pro Ser Glu Lys 660 665 670 Leu Leu Ser Pro Glu Leu He Asn Thr Asn Asn Trp Thr Ser Thr Gly 675 680 685 Ser Thr Asn He Ser Gly Asn Thr Leu Thr Leu Tyr Gin Gly Gly Arg 690 695 700 Gly He Leu Lys Gin Asn Leu Gin Leu Asp Ser Phe Ser Thr Tyr Arg 705 710 715 720 Val Tyr Phe Ser Val Ser Gly Asp Ala Asn Val Arg He Arg Asn Ser 725 730 735 Arg Glu Val Leu Phe Glu Lys Arg Tyr Met Ser Gly Ala Lys Asp Val 740 745 750 Ser Glu Met Phe Thr Thr Lys Phe Glu Lys Asp Asn Phe Tyr He Glu 755 760 765 Leu Ser Gin Gly Asn Asn Leu Tyr Gly Gly Pro He Val His Phe Tyr 770 775 780 Asp Val Ser He Lys 785 (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2403 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: misc_feature (B) LOCATION: 11..2389 (D) OTHER INFORMATION: /note= "maize optimized ENA sequence encoding VIP3A (a) " (xi ) SEQUENCE DESCRIPTION: SEQ ID NO : 30 : CX.ATCCACCA ATGAACATGA ACAAGAACAA CACCAAGCTG AGCACCCGCG CCCTGCCGAG 60 CTTCATCGAC TACTTCAACG GCATCTACGG CTTCGCCACC 03CATCAAGG ACATCATGAA 120 CATGATCTTC AAGACCGACA CCGGCGGCGA C-CTGACCCTG GACGAGATCC TGAAGAACCA 180 GCAGCTGCTG AACGACATCA GCGGCAAGCT GGACGGCGTG AAO-GCAGCC TGAACGACCT 240 GATCGCCCAG QGCAACCTGA ACACCGAGCT GAGCAAGGAG ATCCTTAAGA TCGCCAACGA 300 GCAGAACCAG GICCTGAACG ACGTGAACAA CAAGCTGGAC GCCATCAACA CXATGCTGCG 360 CGTGTACCTG CCGAAGATCA CX_AGCATGCT GAGCGACGTG ATGAAGCAGA ACTACGCCCT 420 GAGCCTGCAG ATCGACTACC TGAGCAAGCA GCTGCAGGAG ATCAGCGACA AGCTGGACAT 480 CATCAACGTG AAO_?ICCTGA TCAACAGCAC CCTGACCGAG ATCACCCCGG CCTACCAGCG 540 CATCAAGTAC GTGAACGAGA AGTTCGAAGA GCTGACCTTC GCCACCGAGA CCAGCAGCAA 600 GGTGAAGAAG GACGGCAGCC CGGCCGACAT CCTGGACGAG CTGACCGAGC TGACCGAGCT 660 GGCCAAGAGC GTGACCAAGA ACX_ACGTGGA CQGCTTCGAG TTCTACCTGA ACACCTTCCA 720 CGACGTGATG GTGGGCAACA ACCTGTTCGG C_CGCAGCGCC CTGAAGACCG CX_AGCGAGCT 780 GATCACCAAG GAGAACGTGA AGACCAGCGG CAGCGAGGTG GGCAACGTGT ACAACTTCCT 840 GATCGTGCTG ACCGCCCTGC AGGCCCAGGC CTTCCTGACC CTGACCACCT GTCGCAAGCT 900 GCTGGGCCTG GCCGACATCG ACTACACCAG CATCATGAAC GAGC.ACTTGA ACAAGGAGAA 960 GGAGGAGTTC CX-CGTGAACA TCCTGCCGAC CCTGAGCAAC ACCTTCAGCA ACCCGAACTA 1020 α-CCAAGGTG AAGGGCAGCG A(-GAGGACGC CAAGATGATC GTGGAGGCTA AGCCGGGCCA 1080 CGCGTTGATC GGCTΓCGAGA TCAGCAACGA C-AGCATCACC GTGCTGAAGG TGTACGAGGC 1140 CAAGCTGAAG CAGAACTACC AGGTGGACAA GGACAGCTTG AGCGAGGTGA TCTACGGCGA 1200 CATGGACAAG CTGCTGTGTC CGGACCAGAG CGAGCAAATC TACTACACCA ACAACATCGT 1260 GITCCCGAAC GAGTACGTGA TCACCAAGAT CGACTTCACC AAGAAGATGA AGACCCTGCG 1320 CTACGAGGTG ACCGCCAACT TCTACGACAG CAGCACCGGC GAGATCGACC TGAACAAGAA 1380 GAAGGTGGAG AGCAGCGAGG CCGAGTACCG CACCCTGAGC GCGAACGACG ACGGCGTCTA 1440 CATGCCACTG GGCGTGATCA GCGAGACCTT CCTGACCCCG ATCAACGGCT TTGGCCTGCA 1500 GGCCGACGAG AACAGCCGCC TGATCACCCT GACCTGTAAG AGCTACCTGC C4CGAGCTGCT 1560 GCTAGCCACC GACCTGAGCA ACAAGGAGAC CAAGCTGATC GTGCCACCGA GCGGCTTCAT 1620 CAGCAACATC GTGGAGAACG GCAGCATCGA GGAGGACAAC CTGGAGCCGT GGAAGGCCAA 1680 CAACAAGAAC GCCTACGTGG ACCACACCGG CGGCGTGAAC GGCACCAAGG CCCTGTACGT 1740 GCACAAGGAC GGCGGCATCA GCC_AGTTCAT C_QGCGACAAG CTGAAGCCGA ACΑCCGAGTA 1800 CGTGATCCAG TACACCGTGA AGQ3CAAGCC ATCX-ATK-AC CTGAAGGACG AGAACACCGG 1860 CTACATCCAC TACGAGGACA CCAACAACAA CCTGGAQGAC TACCAGACCA TCAACAAGCG 1920 CTTCACCACC GGCACCGACC TGAAGGGCGT GTACCTGATC CTGAAGAGCC AGAACGGCGA 1980 CGAGGCCTGG QSCGACAACT TCATCATCCT QGAGATCAGC CCGAGCGAGA AGCTGCTGAG 2040 CX-CGGAGCTG ATCAACACCA ACAACTGGAC CAGCACCGGC AGCACCAACA TCAGCGGCAA 2100 CACCCTGACC CTGTACCAGG GCGGCCGCGG CATCCTGAAG CAGAACCTGC AGCTGGACAG 2160 CTTCAGCACC TAO-GCGTGT ACTTCAGCCT GAGCGGCGAC GCX-AACGTGC GCATCCGCAA 2220 CAGCCGCGAG GTGCTGTTCG AGAAGAGCTA CATGAGCGGC GCCAAGGACG TGAGCGAGAT 2280 GTTCACCACC AAGTTCGAGA AGGACAACTT CTACATCGAG CTGAGCCAGG GCAACAACCT 2340 GTACGGCGGC CCGATCGTGC ACTTCTACGA CGTGAGCATC AACTTAACGT AGAGCTCAGA 2400 TCT 2403 (2) INFORMATION FOR SEQ ID NO:31: (i) SEQUENCE (-HARACTΕRISTICS: (A) LENGTH: 2612 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: ENA (genomic) (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) IJOCATICN: 118 . .2484 (D) OTHER INFORMATION: /note= "Native ENA sequence encoding VIP3A(b) from AB424" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:31: ATTGAAATTG ATAAAAAGTT ATGAGTGTTT AATAATCAGT AATTACCAAT AAAGAATTAA 60 GAATACAACT TTACAAGAAA TAAGTGTTAC AAAAAATAGC TGAAAAGGAA GATGAAC 117 ATG AAC AAG AAT AAT ACT AAA TTA AGC ACA AGA GCC TTA CCA ACT TTT 165 Met Asn Lys Asn Asn Thr Lys Leu Ser Thr Arg Ala Leu Pro Ser Phe 790 795 800 805 ATT GAT TAT TTC AAT GGC ATT TAT GGA TTT GCC ACT GCT ATC AAA GAC 213 He Asp Tyr Phe Asn Gly He Tyr Gly Phe Ala Thr Gly He Lys Asp 810 815 820 ATT ATG AAC ATG ATT TTT AAA ACG GAT ACA GCT GCT GAT CTA ACC CTA 261 He Met Asn Met He Phe Lys Thr Asp Thr Gly Gly Asp Leu Thr Leu 825 830 835 GAC GAA ATT TTA AAG AAT CAG CAG CTA CTA AAT GAT ATT TCT GCT AAA 309 Asp Glu He Leu Lys Asn Gin Gin Leu Leu Asn Asp He Ser Gly Lys 840 845 850 TTG GAT GGG GTG AAT GGA AGC TTA AAT GAT CTT ATC GCA CAG GGA AAC 357 Leu Asp Gly Val Asn Gly Ser Leu Asn Asp Leu He Ala Gin Gly Asn 855 860 865 TTA AAT ACA GAA TTA TCT AAG GAA ATA TTA AAA ATT GCA AAT GAA CAA 405 Leu Asn Thr Glu Leu Ser Lys Glu He Leu Lys He Ala Asn Glu Gin 870 875 880 885 AAT CAA GTT TTA AAT GAT GTT AAT AAC AAA CTC GAT GCG ATA AAT ACG 453 Asn Gin Val Leu Asn Asp Val Asn Asn Lys Leu Asp Ala He Asn Thr 890 895 900 ATG CTT CGG GTA TAT CTA CCT AAA ATT ACC TCT ATG TTG AGT GAT CTA 501 Met Leu Arg Val Tyr Leu Pro Lys He Thr Ser Met Leu Ser Asp Val 905 910 915 ATG AAA CAA AAT TAT GCG CTA AGT CTG CAA ATA GAA TAC TTA AGT AAA 549 Met Lys Gin Asn Tyr Ala Leu Ser Leu Gin He Glu Tyr Leu Ser Lys 920 925 930 CAA TTG CAA GAG ATT TCT GAT AAG TTG GAT ATT ATT AAT GTA AAT CTA 597 Gin Leu Gin Glu He Ser Asp Lys Leu Asp He He Asn Val Asn Val 935 940 945 CTT ATT AAC TCT ACA CTT ACT GAA ATT ACA CCT GCG TAT CAA AGG ATT 645 Leu He Asn Ser Thr Leu Thr Glu He Thr Pro Ala Tyr Gin Arg He 950 955 960 965 AAA TAT GTG AAC GAA AAA TTT GAG GAA TTA ACT TTT GCT ACA GAA ACT 693 Lys Tyr Val Asn Glu Lys Phe Glu Glu Leu Thr Phe Ala Thr Glu Thr 970 975 980 AGT TCA AAA GTA AAA AAG GAT GGC TCT CCT GCA GAT ATT CGT GAT GAG 741 Ser Ser Lys Val Lys Lys Asp Gly Ser Pro Ala Asp He Arg Asp Glu 985 990 995 TTA ACT GAG TTA ACT GAA CTA GCG AAA AGT GTA ACA AAA AAT GAT GTG 789 Leu Thr Glu Leu Thr Glu Leu Ala Lys Ser Val Thr Lys Asn Asp Val 1000 1005 1010 GAT GGT TTT GAA TTT TAC CTT AAT ACA TTC CAC GAT CTA ATG CTA GGA 837 Asp Gly Phe Glu Phe Tyr Leu Asn Thr Phe His Asp Val Met Val Gly 1015 1020 1025 AAT AAT TTA TTC GGG CGT TCA GCT TTA AAA ACT GCA TCG GAA TTA ATT 885 Asn Asn Leu Phe Gly Arg Ser Ala Leu Lys Thr Ala Ser Glu Leu He 1030 1035 1040 1045 ACT AAA GAA AAT GTG AAA ACA AGT GGC ACT GAG GTC GGA AAT GTT TAT 933 Thr Lys Glu Asn Val Lys Thr Ser Gly Ser Glu Val Gly Asn Val Tyr 1050 1055 1060 AAC TTC CTA ATT GTA TTA ACA GCT CTG CAA GCA AAA GCT TTT CTT ACT 981 Asn Phe Leu He Val Leu Thr Ala Leu Gin Ala Lys Ala Phe Leu Thr 1065 1070 1075 TTA ACA CCA TGC CGA AAA TTA TTA GGC TTA GCA GAT ATT GAT TAT ACT 1029 Leu Thr Pro Cys Arg Lys Leu Leu Gly Leu Ala Asp He Asp Tyr Thr 1080 1085 1090 TCT ATT ATG AAT GAA CAT TTA AAT AAG GAA AAA GAG GAA TTT AGA GTA 1077 Ser He Met Asn Glu His Leu Asn Lys Glu Lys Glu Glu Phe Arg Val 1095 1100 1105 AAC ATC CTC CCT ACA CTT TCT AAT ACT TTT TCT AAT CCT AAT TAT GCA 1125 Asn He Leu Pro Thr Leu Ser Asn Thr Phe Ser Asn Pro Asn Tyr Ala 1110 1115 1120 1125 AAA GTT AAA GGA AGT GAT GAA GAT GCA AAG ATG ATT GTG GAA GCT AAA 1173 Lys Val Lys Gly Ser Asp Glu Asp Ala Lys Met He Val Glu Ala Lys 1130 1135 1140 CCA GGA CAT GCA TTG ATT GGG TTT GAA ATT ACT AAT GAT TCA ATT ACA 1221 Pro Gly His Ala Leu He Gly Phe Glu He Ser Asn Asp Ser He Thr 1145 1150 1155 GTA TTA AAA GTA TAT GAG GCT AAG CTA AAA CAA AAT TAT CAA GTC GAT 1269 Val Leu Lys Val Tyr Glu Ala Lys Leu Lys Gin Asn Tyr Gin Val Asp 1160 1165 1170 AAG GAT TCC TTA TCG GAA GTT ATT TAT GGC GAT ATG GAT AAA TTA TTG 1317 Lys Asp Ser Leu Ser Glu Val He Tyr Gly Asp Met Asp Lys Leu Leu 1175 1180 1185 TGC CCA GAT CAA TCT GGA CAA ATC TAT TAT ACA AAT AAC ATA GTA TTT 1365 Cys Pro Asp Gin Ser Gly Gin He Tyr T Thr Asn Asn He Val Phe 1190 1195 1200 1205 CCA AAT GAA TAT GTA ATT ACT AAA ATT GAT TTC ACT AAA AAA ATG AAA 1413 Pro Asn Glu Tyr Val He Thr Lys He Asp Phe Thr Lys Lys Met Lys 1210 1215 1220 ACT TTA AGA TAT GAG GTA ACA GCG AAT TTT TAT GAT TCT TCT ACA GGA 1461 Thr Leu Arg Tyr Glu Val Thr Ala Asn Phe Tyr Asp Ser Ser Thr Gly 1225 1230 1235 GAA ATT GAC TTA AAT AAG AAA AAA GTA GAA TCA AGT GAA GCG GAG TAT 1509 Glu He Asp Leu Asn Lys Lys Lys Val Glu Ser Ser Glu Ala Glu Tyr 1240 1245 1250 AGA ACG TTA ACT GCT AAT GAT GAT GGG GTG TAT ATG CCG TTA GGT GTC 1557 Arg Thr Leu Ser Ala Asn Asp Asp Gly Val Tyr Met Pro Leu Gly Val 1255 1260 1265 ATC AGT GAA ACA TTT TTG ACT CCG ATT AAT GGG TTT GGC CTC CAA GCT 1605 He Ser Glu Thr Phe Leu Thr Pro He Asn Gly Phe Gly Leu Gin Ala 1270 1275 1280 1285 GAT GAA AAT TCA AGA TTA ATT ACT TTA ACA TGT AAA TCA TAT TTA AGA 1653 Asp Glu Asn Ser Arg Leu He Thr Leu Thr Cys Lys Ser Tyr Leu Arg 1290 1295 1300 GAA CTA CTG CTA GCA ACA GAC TTA AGC AAT AAA GAA ACT AAA TTG ATC 1701 Glu Leu Leu Leu Ala Thr Asp Leu Ser Asn Lys Glu Thr Lys Leu He 1305 1310 1315 GTC CCG CCA AGT GGT TTT ATT AGC AAT ATT GTA GAG AAC GGG TCC ATA 1749 Val Pro Pro Ser Gly Phe He Ser Asn He Val Glu Asn Gly Ser He 1320 1325 1330 GAA GAG GAC AAT TTA GAG CCG TGG AAA GCA AAT AAT AAG AAT GCG TAT 1797 Glu Glu Asp Asn Leu Glu Pro Trp Lys Ala Asn Asn Lys Asn Ala Tyr 1335 1340 1345 GTA GAT CAT ACA GGC GGA GTG AAT GGA ACT AAA GCT TTA TAT GTT CAT 1845 Val Asp His Thr Gly Gly Val Asn Gly Thr Lys Ala Leu Tyr Val His 1350 1355 1360 1365 AAG GAC GGA GGA ATT TCA CAA TTT ATT GGA GAT AAG TTA AAA CCG AAA 1893 Lys Asp Gly Gly He Ser Gin Phe He Gly Asp Lys Leu Lys Pro Lys 1370 1375 1380 ACT GAG TAT GTA ATC CAA TAT ACT GTT AAA GGA AAA CCT TCT ATT CAT 1941 Thr Glu Tyr Val He Gin Tyr Thr Val Lys Gly Lys Pro Ser He His 1385 1390 1395 TTA AAA GAT GAA AAT ACT GGA TAT ATT CAT TAT GAA GAT ACA AAT AAT 1989 Leu Lys Asp Glu Asn Thr Gly Tyr He His Tyr Glu Asp Thr Asn Asn 1400 1405 1410 AAT TTA GAA GAT TAT CAA ACT ATT AAT AAA CGT TTT ACT ACA GGA ACT 2037 Asn Leu Glu Asp Tyr Gin Thr He Asn Lys Arg Phe Thr Thr Gly Thr 1415 1420 1425 GAT TTA AAG GGA GTG TAT TTA ATT TTA AAA ACT CAA AAT GGA GAT GAA 2085 Asp Leu Lys Gly Val Tyr Leu He Leu Lys Ser Gin Asn Gly Asp Glu 1430 1435 1440 1445 GCT TGG GGA GAT AAC TTT ATT ATT T G GAA ATT AGT CCT TCT GAA AAG 2133 Ala Trp Gly Asp Asn Phe He He Leu Glu He Ser Pro Ser Glu Lys 1450 1455 1460 TTA TTA ACT CCA GAA TTA ATT AAT ACA AAT AAT TGG ACG ACT ACG GGA 2181 Leu Leu Ser Pro Glu Leu He Asn Thr Asn Asn Trp Thr Ser Thr Gly 1465 1470 1475 TCA ACT AAT ATT AGC GGT AAT ACA CTC ACT CTT TAT CAG GGA GGA CGA 2229 Ser Thr Asn He Ser Gly Asn Thr Leu Thr Leu Tyr Gin Gly Gly Arg 1480 1485 1490 GGG ATT CTA AAA CAA AAC CTT CAA TTA GAT AGT TTT TCA ACT TAT AGA 2277 Gly He Leu Lys Gin Asn Leu Gin Leu Asp Ser Phe Ser Thr Tyr Arg 1495 1500 1505 GTG TAT TTC TCT GTG TCC GGA GAT GCT AAT GTA AGG ATT AGA AAT TCT 2325 Val Tyr Phe Ser Val Ser Gly Asp Ala Asn Val Arg He Arg Asn Ser 1510 1515 1520 1525 AGG GAA GTG TTA TTT GAA AAA AGA TAT ATG AGC GGT GCT AAA GAT GTT 2373 Arg Glu Val Leu Phe Glu Lys Arg Tyr Met Ser Gly Ala Lys Asp Val 1530 1535 1540 TCT GAA ATG TTC ACT ACA AAA TTT GAG AAA GAT AAC TTC TAT ATA GAG 2421 Ser Glu Met Phe Thr Thr Lys Phe Glu Lys Asp Asn Phe Tyr He Glu 1545 1550 1555 CTT TCT CAA GGG AAT AAT TTA TAT GCT GCT CCT ATT GTA CAT TTT TAC 2469 Leu Ser Gin Gly Asn Asn Leu Tyr Gly Gly Pro He Val His Phe Tyr 1560 1565 1570 GAT GTC TCT ATT AAG TAAGATCGGG ATCTAATATT AACAGTTTTT AGAAGCTAAT 2524 Asp Val Ser He Lys 1575 TCTTCTATAA TGTCCTTGAT TATGGAAAAA CACAATTTTG TTTGCTAAGA TGTATATATA 2584 GCTCACTCAT TAAAAGGCAA TCAAGCTT 2612 (2) INFORMATION FOR SEQ ID NO:32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 789 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:32: Met Asn Lys Asn Asn Thr Lys Leu Ser Thr Arg Ala Leu Pro Ser Phe 1 5 10 15 He Asp Tyr Phe Asn Gly He Tyr Gly Phe Ala Thr Gly He Lys Asp 20 25 30 He Met Asn Met He Phe Lys Thr Asp Thr Gly Gly Asp Leu Thr Leu 35 40 45 Asp Glu He Leu Lys Asn Gin Gin Leu Leu Asn Asp He Ser Gly Lys 50 55 60 Leu Asp Gly Val Asn Gly Ser Leu Asn Asp Leu He Ala Gin Gly Asn 65 70 75 80 Leu Asn Thr Glu Leu Ser Lys Glu He Leu Lys He Ala Asn Glu Gin 85 90 95 Asn Gin Val Leu Asn Asp Val Asn Asn Lys Leu Asp Ala He Asn Thr 100 105 110 Met Leu Arg Val Tyr Leu Pro Lys He Thr Ser Met Leu Ser Asp Val 115 120 125 Met Lys Gin Asn Tyr Ala Leu Ser Leu Gin He Glu Tyr Leu Ser Lys 130 135 140 Gin Leu Gin Glu He Ser Asp Lys Leu Asp He He Asn Val Asn Val 145 150 155 160 Leu He Asn Ser Thr Leu Thr Glu He Thr Pro Ala Tyr Gin Arg He 165 170 175 Lys Tyr Val Asn Glu Lys Phe Glu Glu Leu Thr Phe Ala Thr Glu Thr 180 185 190 Ser Ser Lys Val Lys Lys Asp Gly Ser Pro Ala Asp He Arg Asp Glu 195 200 205 Leu Thr Glu Leu Thr Glu Leu Ala Lys Ser Val Thr Lys Asn Asp Val 210 215 220 Asp Gly Phe Glu Phe Tyr Leu Asn Thr Phe His Asp Val Met Val Gly 225 230 235 240 Asn Asn Leu Phe Gly Arg Ser Ala Leu Lys Thr Ala Ser Glu Leu He 245 250 255 Thr Lys Glu Asn Val Lys Thr Ser Gly Ser Glu Val Gly Asn Val Tyr 260 265 270 Asn Phe Leu He Val Leu Thr Ala Leu Gin Ala Lys Ala Phe Leu Thr 275 280 285 Leu Thr Pro Cys Arg Lys Leu Leu Gly Leu Ala Asp He Asp Tyr Thr 290 295 300 Ser He Met Asn Glu His Leu Asn Lys Glu Lys Glu Glu Phe Arg Val 305 310 315 320 Asn He Leu Pro Thr Leu Ser Asn Thr Phe Ser Asn Pro Asn Tyr Ala 325 330 335 Lys Val Lys Gly Ser Asp Glu Asp Ala Lys Met He Val Glu Ala Lys 340 345 350 Pro Gly His Ala Leu He Gly Phe Glu He Ser Asn Asp Ser He Thr 355 360 365 Val Leu Lys Val Tyr Glu Ala Lys Leu Lys Gin Asn Tyr Gin Val Asp 370 375 380 Lys Asp Ser Leu Ser Glu Val He Tyr Gly Asp Met Asp Lys Leu Leu 385 390 395 400 Cys Pro Asp Gin Ser Gly Gin He Tyr Tyr Thr Asn Asn He Val Phe 405 410 415 Pro Asn Glu Tyr Val He Thr Lys He Asp Phe Thr Lys Lys Met Lys 420 425 430 Thr Leu Arg Tyr Glu Val Thr Ala Asn Phe Tyr Asp Ser Ser Thr Gly 435 440 445 Glu He Asp Leu Asn Lys Lys Lys Val Glu Ser Ser Glu Ala Glu Tyr 450 455 460 Arg Thr Leu Ser Ala Asn Asp Asp Gly Val Tyr Met Pro Leu Gly Val 465 470 475 480 He Ser Glu Thr Phe Leu Thr Pro He Asn Gly Phe Gly Leu Gin Ala 485 490 495 Asp Glu Asn Ser Arg Leu He Thr Leu Thr Cys Lys Ser Tyr Leu Arg 500 505 510 Glu Leu Leu Leu Ala Thr Asp Leu Ser Asn Lys Glu Thr Lys Leu He 515 520 525 Val Pro Pro Ser Gly Phe He Ser Asn He Val Glu Asn Gly Ser He 530 535 540 Glu Glu Asp Asn Leu Glu Pro Trp Lys Ala Asn Asn Lys Asn Ala Tyr 545 550 555 560 Val Asp His Thr Gly Gly Val Asn Gly Thr Lys Ala Leu Tyr Veil His 565 570 575 Lys Asp Gly Gly He Ser Gin Phe He Gly Asp Lys Leu Lys Pro Lys 580 585 590 Thr Glu Tyr Val He Gin Tyr Thr Val Lys Gly Lys Pro Ser He His 595 600 605 Leu Lys Asp Glu Asn Thr Gly Tyr He His Tyr Glu Asp Thr Asn Asn 610 615 620 Asn Leu Glu Asp T r Gin Thr He Asn Lys Arg Phe Thr Thr Gly Thr 625 630 635 640 Asp Leu Lys Gly Val Tyr Leu He Leu Lys Ser Gin Asn Gly Asp Glu 645 650 655 Ala Trp Gly Asp Asn Phe He He Leu Glu He Ser Pro Ser Glu Lys 660 665 670 Leu Leu Ser Pro Glu Leu He Asn Thr Asn Asn Trp Thr Ser Thr Gly 675 680 685 Ser Thr Asn He Ser Gly Asn Thr Leu Thr Leu Tyr Gin Gly Gly Arg 690 695 700 Gly He Leu Lys Gin Asn Leu Gin Leu Asp Ser Phe Ser Thr Tyr Arg 705 710 715 720 Val Tyr Phe Ser Val Ser Gly Asp Ala Asn Val Arg He Arg Asn Ser 725 730 735 Arg Glu Val Leu Phe Glu Lys Arg Tyr Met Ser Gly Ala Lys Asp Val 740 745 750 Ser Glu Met Phe Thr Thr Lys Phe Glu Lys Asp Asn Phe Tyr He Glu 755 760 765 Leu Ser Gin Gly Asn Asn Leu Tyr Gly Gly Pro He Val His Phe Tyr 770 775 780 Asp Val Ser He Lys 785 (2) INFORMATION FOR SEQ ID NO:33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 base pairs (B) TYPE: nucleic acid (C) CTRANDEE-NESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "forward primer used to make PCIB5526" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33: GGATCCACCA TCAAGACCAA CCAGATCAGC 30 (2) INFORMATION FOR SIΪQ ID NO:34: (i) SEQUENCE CHARACTERISTICS: (A) LENCTH: 15 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) VDLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "reverse primer used to make PCIB5526" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34: AAGCTTCAGC TCCTT 15 (2) INFORMATION FOR SEQ ID NO:35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2576 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) tOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 9..2564 (D) OTHER INFORMATION: /note= "Maize optimized sequence encoding VTPlA(a) with the Bacillus secretion signal removed as contained in pCIB5526" (xi) SEQUENCE DESCRIPTION: SEQ ID ND:35: GATCCACC ATG AAG ACC AAC CAG ATC AGC ACC ACC CAG AAG AAC CAG CAG 50 Met Lys Thr Asn Gin He Ser Thr Thr Gin Lys Asn Gin Gin 825 830 835 AAG GAG ATG GAC CGC AAG GGC CTG CTG GGC TAC TAC TTC AAG GGC AAG 98 Lys Glu Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys 840 845 850 GAC TTC AGC AAC CTG ACC ATG TTC GCC CCC ACG CGT GAC AGC ACC CTG 146 Asp Phe Ser Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Ser Thr Leu 855 860 865 ATC TAC GAC CAG CAG ACC GCC AAC AAG CTG CTG GAC AAG AAG CAG CAG 194 He Tyr Asp Gin Gin Thr Ala Asn Lys Leu Leu Asp Lys Lys Gin Gin 870 875 880 GAG TAC CAG AGC ATC CGC TGG ATC GGC CTG ATC CAG AGC AAG GAG ACC 242 Glu Tyr Gin Ser He Arg Trp He Gly Leu He Gin Ser Lys Glu Thr 885 890 895 GGC GAC TTC ACC TTC AAC CTG AGC GAG GAC GAG CAG GCC ATC ATC GAG 290 Gly Asp Phe Thr Phe Asn Leu Ser Glu Asp Glu Gin Ala He He Glu 900 905 910 915 ATC AAC GGC AAG ATC ATC AGC AAC AAG GGC AAG GAG AAG CAG GTG GTG 338 He Asn Gly Lys He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val 920 925 930 CAC CTG GAG AAG GGC AAG CTG GTG CCC ATC AAG ATC GAG TAC CAG AGC 386 His Leu Glu Lys Gly Lys Leu Val Pro He Lys He Glu Tyr Gin Ser 935 940 945 GAC ACC AAG TTC AAC ATC GAC AGC AAG ACC TTC AAG GAG CTG AAG CTT 434 Asp Thr Lys Phe Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu 950 955 960 TTC AAG ATC GAC AGC CAG AAC CAG CCC CAG CAG GTG CAG CAG GAC GAG 482 Phe Lys He Asp Ser Gin Asn Gin Pro Gin Gin Val Gin Gin Asp Glu 965 970 975 CTG CGC AAC CCC GAG TTC AAC AAG AAG GAG AGC CAG GAG TTC CTG GCC 530 Leu Arg Asn Pro Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala 980 985 990 995 AAG CCC AGC AAG ATC AAC CTG TTC ACC CAG CAG ATG AAG CGC GAG ATC 578 Lys Pro Ser Lys He Asn Leu Phe Thr Gin Gin Met Lys Arg Glu He 1000 1005 1010 GAC GAG GAC ACC GAC ACC GAC GGC GAC AGC ATC CCC GAC CTG TGG GAG 626 Asp Glu Asp Thr Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu 1015 1020 1025 GAG AAC GGC TAC ACC ATC CAG AAC CGC ATC GCC GTG AAG TGG GAC GAC 674 Glu Asn Gly Tyr Thr He Gin Asn Arg He Ala Val Lys Trp Asp Asp 1030 1035 1040 AGC CTG GCT AGC AAG GGC TAC ACC AAG TTC GTG AGC AAC CCC CTG GAG 722 Ser Leu Ala Ser Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Glu 1045 1050 1055 AGC CAC ACC GTG GGC GAC CCC TAC ACC GAC TAC GAG AAG GCC GCC CGC 770 Ser His Thr Val Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg 1060 1065 1070 1075 GAC CTG GAC CTG AGC AAC GCC AAG GAG ACC TTC AAC CCC CTG GTG GCC 818 Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala 1080 1085 1090 GCC TTC CCC AGC GTG AAC GTG AGC ATG GAG AAG GTG ATC CTG AGC CCC 866 Ala Phe Pro Ser Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro 1095 1100 1105 AAC GAG AAC CTG AGC AAC AGC GTG GAG AGC CAC TCG AGC ACC AAC TGG 914 Asn Glu Asn Leu Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp 1110 1115 1120 AGC TAC ACC AAC ACC GAG GGC GCC AGC GTG GAG GCC GGC ATC GGT CCC 962 Ser Tyr Thr Asn Thr Glu Gly Ala Ser Val Glu Ala Gly He Gly Pro 1125 1130 1135 AAG GGC ATC AGC TTC GGC GTG AGC GTG AAC TAC CAG CAC AGC GAG ACC 1010 Lys Gly He Ser Phe Gly Val Ser Val Asn Tyr Gin His Ser Glu Thr 1140 1145 1150 1155 GTG GCC CAG GAG TGG GGC ACC AGC ACC GGC AAC ACC AGC CAG TTC AAC 1058 Val Ala Gin Glu Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn 1160 1165 1170 ACC GCC AGC GCC GGC TAC CTG AAC GCC AAC GTG CGC TAC AAC AAC GTG 1106 Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val 1175 1180 1185 GGC ACC GGC GCC ATC TAC GAC GTG AAG CCC ACC ACC AGC TTC GTG CTG 1154 Gly Thr Gly Ala He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu 1190 1195 1200 AAC AAC GAC ACC ATC GCC ACC ATC ACC GCC AAG TCG AAT TCC ACC GCC 1202 Asn Asn Asp Thr He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala 1205 1210 1215 CTG AAC ATC AGC CCC GGC GAG AGC TAC CCC AAG AAG GGC CAG AAC GGC 1250 Leu Asn He Ser Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gin Asn Gly 1220 1225 1230 1235 ATC GCC ATC ACC AGC ATG GAC GAC TTC AAC AGC CAC CCC ATC ACC CTG 1298 He Ala He Thr Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu 1240 1245 1250 AAC AAG AAG CAG GTG GAC AAC CTG CTG AAC AAC AAG CCC ATG ATG CTG 1346 Asn Lys Lys Gin Veil Asp Asn Leu Leu Asn Asn Lys Pro Met Met Leu 1255 1260 1265 GAG ACC AAC CAG ACC GAC GGC GTC TAC AAG ATC AAG GAC ACC CAC GGC 1394 Glu Thr Asn Gin Thr Asp Gly Veil Tyr Lys He Lys Asp Thr His Gly 1270 1275 1280 AAC ATC GTG ACG GGC GGC GAG TGG AAC GGC GTG ATC CAG CAG ATC AAG 1442 Asn He Val Thr Gly Gly Glu Trp Asn Gly Val He Gin Gin He Lys 1285 1290 1295 GCC AAG ACC GCC AGC ATC ATC GTC GAC GAC GGC GAG CGC GTG GCC GAG 1490 Ala Lys Thr Ala Ser He He Val Asp Asp Gly Glu Arg Val Ala Glu 1300 1305 1310 1315 AAG CGC GTG GCC GCC AAG GAC TAC GAG AAC CCC GAG GAC AAG ACC CCC 1538 Lys Arg Val Ala Ala Lys Asp Tyr Glu Asn Pro Glu Asp Lys Thr Pro 1320 1325 1330 AGC CTG ACC CTG AAG GAC GCC CTG AAG CTG AGC TAC CCC GAC GAG ATC 1586 Ser Leu Thr Leu Lys Asp Ala Leu Lys Leu Ser Tyr Pro Asp Glu He 1335 1340 1345 AAG GAG ATC GAG GGC TTG CTG TAC TAC AAG AAC AAG CCC ATC TAC GAG 1634 Lys Glu He Glu Gly Leu Leu Tyr Tyr Lys Asn Lys Pro He Tyr Glu 1350 1355 1360 AGC AGC GTG ATG ACC TAT CTA GAC GAG AAC ACC GCC AAG GAG GTG ACC 1682 Ser Ser Val Met Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Thr 1365 1370 1375 AAG CAG CTG AAC GAC ACC ACC GGC AAG TTC AAG GAC GTG AGC CAC CTG 1730 Lys Gin Leu Asn Asp Thr Thr Gly Lys Phe Lys Asp Val Ser His leu 1380 1385 1390 1395 TAC GAC GTG AAG CTG ACC CCC AAG ATG AAC GTG ACC ATC AAG CTG AGC 1778 Tyr Asp Val Lys Leu Thr Pro Lys Met Asn Val Thr He Lys Leu Ser 1400 1405 1410 ATC CTG TAC GAC AAC GCC GAG AGC AAC GAC AAC AGC ATC GGC AAG TGG 1826 He Leu Tyr Asp Asn Ala Glu Ser Asn Asp Asn Ser He Gly Lys Trp 1415 1420 1425 ACC AAC ACC AAC ATC GTG AGC GGC GGC AAC AAC GGC AAG AAG CAG TAC 1874 Thr Asn Thr Asn He Val Ser Gly Gly Asn Asn Gly Lys Lys Gin Tyr 1430 1435 1440 AGC AGC AAC AAC CCC GAC GCC AAC CTG ACC CTG AAC ACC GAC GCC CAG 1922 Ser Ser Asn Asn Pro Asp Ala Asn Leu Thr Leu Asn Thr Asp Ala Gin 1445 1450 1455 GAG AAG CTG AAC AAG AAC CGC GAC TAC TAC ATC AGC CTG TAC ATG AAG 1970 Glu Lys Leu Asn Lys Asn Arg Asp Tyr Tyr He Ser Leu Tyr Met Lys 1460 1465 1470 1475 AGC GAG AAG AAC ACC CAG TGC GAG ATC ACC ATC GAC GGC GAG ATA TAC 2018 Ser Glu Lys Asn Thr Gin Cys Glu He Thr He Asp Gly Glu He Tyr 1480 1485 1490 CCC ATC ACC ACC AAG ACC GTG AAC GTG AAC AAG GAC AAC TAC AAG CGC 2066 Pro He Thr Thr Lys Thr Val Asn Val Asn Lys Asp Asn Tyr Lys Arg 1495 1500 1505 CTG GAC ATC ATC GCC CAC AAC ATC AAG AGC AAC CCC ATC AGC AGC CTG 2114 Leu Asp He He Ala His Asn He Lys Ser Asn Pro He Ser Ser Leu 1510 1515 1520 CAC ATC AAG ACC AAC GAC GAG ATC ACC CTG TTC TGG GAC GAC ATA TCG 2162 His He Lys Thr Asn Asp Glu He Thr Leu Phe Trp Asp Asp He Ser 1525 1530 1535 ATT ACC GAC GTC GCC AGC ATC AAG CCC GAG AAC CTG ACC GAC AGC GAG 2210 He Thr Asp Val Ala Ser He Lys Pro Glu Asn Leu Thr Asp Ser Glu 1540 1545 1550 1555 ATC AAG CAG ATA TAC AGT CGC TAC GGC ATC AAG CTG GAG GAC GGC ATC 2258 He Lys Gin He Tyr Ser Arg Tyr Gly He Lys Leu Glu Asp Gly He 1560 1565 1570 CTG ATC GAC AAG AAA GGC GGC ATC CAC TAC GGC GAG TTC ATC AAC GAG 2306 Leu He Asp Lys Lys Gly Gly He His Tyr Gly Glu Phe He Asn Glu 1575 1580 1585 GCC AGC TTC AAC ATC GAG CCC CTG CAG AAC TAC GTG ACC AAG TAC GAG 2354 Ala Ser Phe Asn He Glu Pro Leu Gin Asn Tyr Val Thr Lys Tyr Glu 1590 1595 1600 GTG ACC TAC AGC AGC GAG CTG GGC CCC AAC GTG AGC GAC ACC CTG GAG 2402 Val Thr Tyr Ser Ser Glu Leu Gly Pro Asn Val Ser Asp Thr Leu Glu 1605 1610 1615 AGC GAC AAG ATT TAC AAG GAC GGC ACC ATC AAG TTC GAC TTC ACC AAG 2450 Ser Asp Lys He Tyr Lys Asp Gly Thr He Lys Phe Asp Phe Thr Lys 1620 1625 1630 1635 TAC AGC AAG AAC GAG CAG GGC CTG TTC TAC GAC AGC GGC CTG AAC TGG 2498 Tyr Ser Lys Asn Glu Gin Gly Leu Phe Tyr Asp Ser Gly Leu Asn Trp 1640 1645 1650 GAC TTC AAG ATC AAC GCC ATC ACC TAC GAC GGC AAG GAG ATG AAC GTG 2546 Asp Phe Lys He Asn Ala He Thr Tyr Asp Gly Lys Glu Met Asn Val 1655 1660 1665 TTC CAC CGC TAC AAC AAG TAGATCTGAG CT 2576 Phe His Arg Tyr Asn Lys 1670 (2) INFORMATICesr FOR SEQ ID NO:36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 852 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) VD ECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: Met Lys Thr Asn Gin He Ser Thr Thr Gin Lys Asn Gin Gin Lys Glu 1 5 10 15 Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 20 25 30 Ser Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Ser Thr Leu He Tyr 35 40 45 Asp Gin Gin Thr Ala Asn Lys Leu Leu Asp Lys Lys Gin Gin Glu Tyr 50 55 60 Gin Ser He Arg Trp He Gly Leu He Gin Ser Lys Glu Thr Gly Asp 65 70 75 80 Phe Thr Phe Asn Leu Ser Glu Asp Glu Gin Ala He He Glu He Asn 85 90 95 Gly Lys He He Ser Asn Lys Gly Lys Glu Lys Gin Val Val His Leu 100 105 110 Glu Lys Gly Lys Leu Val Pro He Lys He Glu Tyr Gin Ser Asp Thr 115 120 125 Lys Phe Asn He Asp Ser Lys Thr Phe Lys Glu Leu Lys Leu Phe Lys 130 135 140 He Asp Ser Gin Asn Gin Pro Gin Gin Val Gin Gin Asp Glu Leu Arg 145 150 155 160 Asn Pro Glu Phe Asn Lys Lys Glu Ser Gin Glu Phe Leu Ala Lys Pro 165 170 175 Ser Lys He Asn Leu Phe Thr Gin Gin Met Lys Arg Glu He Asp Glu 180 185 190 Asp Thr Asp Thr Asp Gly Asp Ser He Pro Asp Leu Trp Glu Glu Asn 195 200 205 Gly Tyr Thr He Gin Asn Arg He Ala Val Lys Trp Asp Asp Ser Leu 210 215 220 Ala Ser Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Leu Glu Ser His 225 230 235 240 Thr Val Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu 245 250 255 Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe 260 265 270 Pro Ser Val Asn Val Ser Met Glu Lys Val He Leu Ser Pro Asn Glu 275 280 285 Asn Leu Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr 290 295 300 Thr Asn Thr Glu Gly Ala Ser Val Glu Ala Gly He Gly Pro Lys Gly 305 310 315 320 He Ser Phe Gly Val Ser Val Asn Tyr Gin His Ser Glu Thr Val Ala 325 330 335 Gin Glu Trp Gly Thr Ser Thr Gly Asn Thr Ser Gin Phe Asn Thr Ala 340 345 350 Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr 355 360 365 Gly Ala He Tyr Asp Val Lys Pro Thr Thr Ser Phe Val Leu Asn Asn 370 375 380 Asp Thr He Ala Thr He Thr Ala Lys Ser Asn Ser Thr Ala Leu Asn 385 390 395 400 He Ser Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gin Asn Gly He Ala 405 410 415 He Thr Ser Met Asp Asp Phe Asn Ser His Pro He Thr Leu Asn Lys 420 425 430 Lys Gin Val Asp Asn Leu Leu Asn Asn Lys Pro Met Met Leu Glu Thr 435 440 445 Asn Gin Thr Asp Gly Val Tyr Lys He Lys Asp Thr His Gly Asn He 450 455 460 Val Thr Gly Gly Glu Trp Asn Gly Val He Gin Gin He Lys Ala Lys 465 470 475 480 Thr Ala Ser He He Val Asp Asp Gly Glu Arg Val Ala Glu Lys Arg 485 490 495 Val Ala Ala Lys Asp Tyr Glu Asn Pro Glu Asp Lys Thr Pro Ser Leu 500 505 510 Thr Leu Lys Asp Ala Leu Lys Leu Ser Tyr Pro Asp Glu He Lys Glu 515 520 525 He Glu Gly Leu Leu Tyr Tyr Lys Asn Lys Pro He Tyr Glu Ser Ser 530 535 540 Val Met Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Thr Lys G n 545 550 555 560 Leu Asn Asp Thr Thr Gly Lys Phe Lys Asp Val Ser His Leu Tyr Asp 565 570 575 Val Lys Leu Thr Pro Lys Met Asn Val Thr He Lys leu Ser He Leu 580 585 590 Tyr Asp Asn Ala Glu Ser Asn Asp Asn Ser He Gly Lys Trp Thr Asn 595 600 605 Thr Asn He Val Ser Gly Gly Asn Asn Gly Lys Lys Gin Tyr Ser Ser 610 615 620 Asn Asn Pro Asp Ala Asn Leu Thr Leu Asn Thr Asp Ala Gin Glu Lys 625 630 635 640 Leu Asn Lys Asn Arg Asp Tyr Tyr He Ser Leu Tyr Met Lys Ser Glu 645 650 655 Lys Asn Thr Gin Cys Glu He Thr He Asp Gly Glu He Tyr Pro He 660 665 670 Thr Thr Lys Thr Val Asn Val Asn Lys Asp Asn Tyr Lys Arg Leu Asp 675 680 685 He He Ala His Asn He Lys Ser Asn Pro He Ser Ser Leu His He 690 695 700 Lys Thr Asn Asp Glu He Thr Leu Phe Trp Asp Asp He Ser He Thr 705 710 715 720 Asp Val Ala Ser He Lys Pro Glu Asn Leu Thr Asp Ser Glu He Lys 725 730 735 Gin He Tyr Ser Arg Tyr Gly He Lys Leu Glu Asp Gly He Leu He 740 745 750 Asp Lys Lys Gly Gly He His Tyr Gly Glu Phe He Asn Glu Ala Ser 755 760 765 Phe Asn He Glu Pro Leu Gin Asn Tyr Val Thr Lys Tyr Glu Val Thr 770 775 780 Tyr Ser Ser Glu Leu Gly Pro Asn Val Ser Asp Thr Leu Glu Ser Asp 785 790 795 800 Lys He Tyr Lys Asp Gly Thr He Lys Phe Asp Phe Thr Lys Tyr Ser 805 810 815 Lys Asn Glu Gin Gly Leu Phe Tyr Asp Ser Gly Leu Asn Trp Asp Phe 820 825 830 Lys He Asn Ala He Thr Tyr Asp Gly Lys Glu Met Asn Val Phe His 835 840 845 Arg Tyr Asn Lys 850 (2) INFORMATION FOR SEQ ID NO:37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 base pairs (B) TYPE: nucleic acid (C) STRANL-EENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "forward primer used to make pCIB5527" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37: GGATCCACCA TGCTGCAGAA C-CTGAAGATC AC 32 (2) INFORMATION FOR SEQ ID NO:38: (i) SEQUENCE CHARACTERISTICS: (A) LE-SK-TH: 18 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOI-ECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "reverse primer used to make PCIB5527" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38: AAGCTTCCAC TCXTTCTC 18 (2) INFORMATION FOR SEQ ID NO:39: (i) SEQUENCE CHARACTERISTICS: (A) LEN3TH: 1241 base pairs (B) TYPE: nucleic acid (C) STRANDEEUESS: single (D) TOPOLOGY: linear (ii) 1 )LECUI_E TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 9..1238 (D) OTHER INFORMATION: /note= "Maize optimized ENA sequence encoding VTP2A(a) with the Bacillus secretion signal removed as contained in pCIB5527" (xi) SEQUENCE DESCRIPTION: SEQ ID NO-.39: GATCCACC ATG CTG CAG AAC CTG AAG ATC ACC GAC AAG GTG GAG GAC TTC 50 Met Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu Asp Phe 855 860 865 AAG GAG GAC AAG GAG AAG GCC AAG GAG TGG GGC AAG GAG AAG GAG AAG 98 Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys Glu Lys 870 875 880 GAG TGG AAG CTT ACC GCC ACC GAG AAG GGC AAG ATG AAC AAC TTC CTG 146 Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn Phe Leu 885 890 895 GAC AAC AAG AAC GAC ATC AAG ACC AAC TAC AAG GAG ATC ACC TTC AGC 194 Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr Phe Ser 900 905 910 ATA GCC GGC AGC TTC GAG GAC GAG ATC AAG GAC CTG AAG GAG ATC GAC 242 He Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu He Asp 915 920 925 930 AAG ATG TTC GAC AAG ACC AAC CTG AGC AAC AGC ATC ATC ACC TAC AAG 290 Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr Tyr Lys 935 940 945 AAC GTG GAG CCC ACC ACC ATC GGC TTC AAC AAG AGC CTG ACC GAG GGC 338 Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr Glu Gly 950 955 960 AAC ACC ATC AAC AGC GAC GCC ATG GCC CAG TTC AAG GAG CAG TTC CTG 386 Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin Phe Leu 965 970 975 GAC CGC GAC ATC AAG TTC GAC AGC TAC CTG GAC ACC CAC CTG ACC GCC 434 Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu Thr Ala 980 985 990 CAG CAG GTG AGC AGC AAG GAG CGC GTG ATC CTG AAG GTG ACC GTC CCC 482 Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr Val Pro 995 1000 1005 1010 AGC GGC AAG GGC AGC ACC ACC CCC ACC AAG GCC GGC GTG ATC CTG AAC 530 Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He Leu Asn 1015 1020 1025 AAC AGC GAG TAC AAG ATG CTG ATC GAC AAC GGC TAC ATG GTG CAC GTG 578 Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val His Val 1030 1035 1040 GAC AAG GTG AGC AAG GTG GTG AAG AAG GGC GTG GAG TGC CTC CAG ATC 626 Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu Gin He 1045 1050 1055 GAG GGC ACC CTG AAG AAG ACT CTA GAC TTC AAG AAC GAC ATC AAC GCC 674 Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He Asn Ala 1060 1065 1070 GAG GCC CAC AGC TGG GGC ATG AAG AAC TAC GAG GAG TGG GCC AAG GAC 722 Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala Lys Asp 1075 1080 1085 1090 CTG ACC GAC AGC CAG CGC GAG GCC CTG GAC GGC TAC GCC CGC CAG GAC 770 Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg Gin Asp 1095 1100 1105 TAC AAG GAG ATC AAC AAC TAC CTG CGC AAC CAG GGC GGC AGC GGC AAC 818 Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser Gly Asn 1110 1115 1120 GAG AAG CTG GAC GCC CAG ATC AAG AAC ATC AGC GAC GCC CTG GGC AAG 866 Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu Gly Lys 1125 1130 1135 AAG CCC ATC CCC GAG AAC ATC ACC GTG TAC CGC TGG TGC GGC ATG CCC 914 Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly Met Pro 1140 1145 1150 GAG TTC GGC TAC CAG ATC AGC GAC CCC CTG CCC AGC CTG AAG GAC TTC 962 Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys Asp Phe 1155 1160 1165 1170 GAG GAG CAG TTC CTG AAC ACC ATC AAG GAG GAC AAG GGC TAC ATG AGC 1010 Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr Met Ser 1175 1180 1185 ACC AGC CTG AGC AGC GAG CGC CTG GCC GCC TTC GGC AGC CGC AAG ATC 1058 Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg Lys He 1190 1195 1200 ATC CTG CGC CTG CAG GTG CCC AAG GGC AGC ACT GGT GCC TAC CTG AGC 1106 He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr Leu Ser 1205 1210 1215 GCC ATC GGC GGC TTC GCC AGC GAG AAG GAG ATC CTG CTG GAT AAG GAC 1154 Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp Lys Asp 1220 1225 1230 AGC AAG TAC CAC ATC GAC AAG GTG ACC GAG GTG ATC ATC AAG GGC GTG 1202 Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He Lys Gly Val 1235 1240 1245 1250 AAG CGC TAC GTG GTG GAC GCC ACC CTG CTG ACC AAC TAG 1241 Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 1255 1260 (2) INFORMATION FOR SEQ ID NO:40: (i) SEQUENCE CHARACTERISTICS: (A) L-2N3TH: 410 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MDLECUE-E TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:40: Met Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu Asp Phe Lys Glu 1 5 10 15 Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys Glu Lys Glu Trp 20 25 30 Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn Phe Leu Asp Asn 35 40 45 Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr Phe Ser He Ala 50 55 60 Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu He Asp Lys Met 65 70 75 80 Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr Tyr Lys Asn Val 85 90 95 Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr Glu Gly Asn Thr 100 105 110 He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin Phe Leu Asp Arg 115 120 125 Asp He Lys Phe Asp Ser Tyr eu Asp Thr His Leu Thr Ala Gin Gin 130 135 140 Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr Val Pro Ser Gly 145 150 155 160 Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He Leu Asn Asn Ser 165 170 175 Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val His Val Asp Lys 180 185 190 Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu Gin He Glu Gly 195 200 205 Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He Asn Ala Glu Ala 210 215 220 His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala Lys Asp Leu Thr 225 230 235 240 Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg Gin Asp Tyr Lys 245 250 255 Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser Gly Asn Glu Lys 260 265 270 Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu Gly Lys Lys Pro 275 280 285 He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly Met Pro Glu Phe 290 295 300 Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys Asp Phe Glu Glu 305 310 315 320 Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr Met Ser Thr Ser 325 330 335 Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg Lys He He Leu 340 345 350 Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr Leu Ser Ala He 355 360 365 Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp Lys Asp Ser Lys 370 375 380 Tyr His He Asp Lys Val Thr Glu Val He He Lys Gly Val Lys Arg 385 390 395 400 Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 405 410 (2) INFORMATION FOR SEQ ID NO:41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 72 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "oligonucleotide encoding eukaryotic secretion signal used to construct pCIB5527" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:41: GGATCCACCA TGGGCTGGAG CTC5GATCTTC CTGTTCCTGC TGAGCGGCGC CGCGGGCGTG 60 CACTCCX-TGC AG 72 (2) INFORMATION FOR SBQ ID NO:42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1241 base pairs (B) TYPE: nucleic acid (C) --TRANE -NESS: single (D) TOPOLOGY: linear (ii) 1 1L--CULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTH.-TICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 9..1238 (D) OTHER INFORMATION: /note= "Maize optimized ENA sequence encoding VIP2A(a) with the Bacillus secretion signal removed and the eukaryotic secretion signal inserted as contained in pCIB5528" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: GATCCACC ATG CTG CAG AAC CTG AAG ATC ACC GAC AAG GTG GAG GAC TTC 50 Met Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu Asp Phe 415 420 AAG GAG GAC AAG GAG AAG GCC AAG GAG TGG GGC AAG GAG AAG GAG AAG 98 Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys Glu Lys 425 430 435 440 GAG TGG AAG CTT ACC GCC ACC GAG AAG GGC AAG ATG AAC AAC TTC CTG 146 Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn Phe Leu 445 450 455 GAC AAC AAG AAC GAC ATC AAG ACC AAC TAC AAG GAG ATC ACC TTC AGC 194 Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr Phe Ser 460 465 470 ATA GCC GGC AGC TTC GAG GAC GAG ATC AAG GAC CTG AAG GAG ATC GAC 242 He Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu He Asp 475 480 485 AAG ATG TTC GAC AAG ACC AAC CTG AGC AAC AGC ATC ATC ACC TAC AAG 290 Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr Tyr Lys 490 495 500 AAC GTG GAG CCC ACC ACC ATC GGC TTC AAC AAG AGC CTG ACC GAG GGC 338 Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr Glu Gly 505 510 515 520 AAC ACC ATC AAC AGC GAC GCC ATG GCC CAG TTC AAG GAG CAG TTC CTG 386 Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin Phe Leu 525 530 535 GAC CGC GAC ATC AAG TTC GAC AGC TAC CTG GAC ACC CAC CTG ACC GCC 434 Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu Thr Ala 540 545 550 CAG CAG GTG AGC AGC AAG GAG CGC GTG ATC CTG AAG GTG ACC GTC CCC 482 Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr Val Pro 555 560 565 AGC GGC AAG GGC AGC ACC ACC CCC ACC AAG GCC GGC GTG ATC CTG AAC 530 Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He Leu Asn 570 575 580 AAC AGC GAG TAC AAG ATG CTG ATC GAC AAC GGC TAC ATG GTG CAC GTG 578 Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val His Val 585 590 595 600 GAC AAG GTG AGC AAG GTG GTG AAG AAG GGC GTG GAG TGC CTC CAG ATC 626 Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu Gin He 605 610 615 GAG GGC ACC CTG AAG AAG AGT CTA GAC TTC AAG AAC GAC ATC AAC GCC 674 Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He Asn Ala 620 625 630 GAG GCC CAC AGC TGG GGC ATG AAG AAC TAC GAG GAG TGG GCC AAG GAC 722 Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala Lys Asp 635 640 645 CTG ACC GAC AGC CAG CGC GAG GCC CTG GAC GGC TAC GCC CGC CAG GAC 770 Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg Gin Asp 650 655 660 TAC AAG GAG ATC AAC AAC TAC CTG CGC AAC CAG GGC GGC AGC GGC AAC 818 Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser Gly Asn 665 670 675 680 GAG AAG CTG GAC GCC CAG ATC AAG AAC ATC AGC GAC GCC CTG GGC AAG 866 Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu Gly Lys 685 690 695 AAG CCC ATC CCC GAG AAC ATC ACC GTG TAC CGC TGG TGC GGC ATG CCC 914 Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly Met Pro 700 705 710 GAG TTC GGC TAC CAG ATC AGC GAC CCC CTG CCC AGC CTG AAG GAC TTC 962 Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Se_r Leu Lys Asp Phe 715 720 725 GAG GAG CAG TTC CTG AAC ACC ATC AAG GAG GAC AAG GGC TAC ATG AGC 1010 Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr Met Ser 730 735 740 ACC AGC CTG AGC AGC GAG CGC CTG GCC GCC TTC GGC AGC CGC AAG ATC 1058 Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg Lys He 745 750 755 760 ATC CTG CGC CTG CAG GTG CCC AAG GGC AGC ACT GGT GCC TAC CTG AGC 1106 He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr Leu Ser 765 770 775 GCC ATC GGC GGC TTC GCC AGC GAG AAG GAG ATC CTG CTG GAT AAG GAC 1154 Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp Lys Asp 780 785 790 AGC AAG TAC CAC ATC GAC AAG GTG ACC GAG GTG ATC ATC AAG GGC GTG 1202 Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He Lys Gly Val 795 800 805 AAG CGC TAC GTG GTG GAC GCC ACC CTG CTG ACC AAC TAG 1241 Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 810 815 820 (2) INFORMATION FOR SEQ ID NO:43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 410 amino acids (D) TOPOLOGY: linear (ii) DI-ECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43: Met Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu Asp Phe Lys Glu 1 5 10 15 Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys Glu Lys Glu Trp 20 25 30 Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn Phe Leu Asp Asn 35 40 45 Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr Phe Ser He Ala 50 55 60 Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu He Asp Lys Met 65 70 75 80 Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr Tyr Lys Asn Val 85 90 95 Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr Glu Gly Asn Thr 100 105 110 He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin Phe Leu Asp Arg 115 120 125 Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu Thr Ala Gin Gin 130 135 140 Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr Val Pro Ser Gly 145 150 155 160 Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He Leu Asn Asn Ser 165 170 175 Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val His Val Asp Lys 180 185 190 Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu Gin He Glu Gly 195 200 205 Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He Asn Ala Glu Ala 210 215 220 His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala Lys Asp Leu Thr 225 230 235 240 Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg Gin Asp Tyr Lys 245 250 255 Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser Gly Asn Glu Lys 260 265 270 Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu Gly Lys Lys Pro 275 280 285 He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly Met Pro Glu Phe 290 295 300 Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys Asp Phe Glu Glu 305 310 315 320 Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr Met Ser Thr Ser 325 330 335 Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg Lys He He Leu 340 345 350 Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr Leu Ser Ala He 355 360 365 Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp Lys Asp Ser Lys 370 375 380 Tyr His He Asp Lys Val Thr Glu Val He He Lys Gly Val Lys Arg 385 390 395 400 Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 405 410 (2) INFORMATION FOR SEQ ID NO:44: (i) SEQUENCE C-HARACTERISTICS: (A) LENCTH: 86 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "oligonucleotide encoding vacuolar targetting peptide used to construct pCIB5533" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44: CCGCGGGCCT GCACTGCCTC AGCAGCAGCA GCTTCGCCGA CAGCAACCCC ATCCGCGTGA 60 CCGACCGCGC CGCCAGCACC CTGCAG 86 (2) INFORMATION FOR SEQ ID NO:45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1358 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) røl-BCULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 9..1355 (D) OTHER INFORMATION: /note= "Maize optimized VIP2A(a) with the Bacillus secretion signal rerroved and the vacuolar targetting signal inserted as contained in pCIB5533" (xi) SEQUENCE DESCRIPTION: SEQ ID NO.-45: GATCCACC ATG GGC TGG AGC TGG ATC TTC CTG TTC CTG CTG AGC GGC GCC 50 Met Gly Trp Ser Trp He Phe Leu Phe Leu Leu Ser Gly Ala 415 420 GCG GGC GTG CAC TGC CTC AGC AGC AGC AGC TTC GCC GAC AGC AAC CCC 98 Ala Gly Val His Cys Leu Ser Ser Ser Ser Phe Ala Asp Ser Asn Pro 425 430 435 440 ATC CGC GTG ACC GAC CGC GCC GCC AGC ACC CTG CAG AAC CTG AAG ATC 146 He Arg Val Thr Asp Arg Ala Ala Ser Thr Leu Gin Asn Leu Lys He 445 450 455 ACC GAC AAG GTG GAG GAC TTC AAG GAG GAC AAG GAG AAG GCC AAG GAG 194 Thr Asp Lys Val Glu Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu 460 465 470 TGG GGC AAG GAG AAG GAG AAG GAG TGG AAG CTT ACC GCC ACC GAG AAG 242 Trp Gly Lys Glu Lys Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys 475 480 485 GGC AAG ATG AAC AAC TTC CTG GAC AAC AAG AAC GAC ATC AAG ACC AAC 290 Gly Lys Met Asn Asn Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn 490 495 500 TAC AAG GAG ATC ACC TTC AGC ATA GCC GGC AGC TTC GAG GAC GAG ATC 338 Tyr Lys Glu He Thr Hie Ser He Ala Gly Ser Phe Glu Asp Glu He 505 510 515 520 AAG GAC CTG AAG GAG ATC GAC AAG ATG TTC GAC AAG ACC AAC CTG AGC 386 Lys Asp Leu Lys Glu He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser 525 530 535 AAC AGC ATC ATC ACC TAC AAG AAC GTG GAG CCC ACC ACC ATC GGC TTC 434 Asn Ser He He Thr Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe 540 545 550 AAC AAG AGC CTG ACC GAG GGC AAC ACC ATC AAC AGC GAC GCC ATG GCC 482 Asn Lys Ser Leu Thr Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala 555 560 565 CAG TTC AAG GAG CAG TTC CTG GAC CGC GAC ATC AAG TTC GAC AGC TAC 530 Gin Phe Lys Glu Gin Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr 570 575 580 CTG GAC ACC CAC CTG ACC GCC CAG CAG GTG AGC AGC AAG GAG CGC GTG 578 Leu Asp Thr His Leu Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val 585 590 595 600 ATC CTG AAG GTG ACC GTC CCC AGC GGC AAG GGC AGC ACC ACC CCC ACC 626 He Leu Lys Val Thr Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr 605 610 615 AAG GCC GGC GTG ATC CTG AAC AAC AGC GAG TAC AAG ATG CTG ATC GAC 674 Lys Ala Gly Val He Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp 620 625 630 AAC GGC TAC ATG GTG CAC GTG GAC AAG GTG AGC AAG GTG GTG AAG AAG 722 Asn Gly Tyr Met Val His Val Asp Lys Val Ser Lys Val Val Lys Lys 635 640 645 GGC GTG GAG TGC CTC CAG ATC GAG GGC ACC CTG AAG AAG AGT CTA GAC 770 Gly Val Glu Cys Leu Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp 650 655 660 TTC AAG AAC GAC ATC AAC GCC GAG GCC CAC AGC TGG GGC ATG AAG AAC 818 Phe Lys Asn Asp He Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn 665 670 675 680 TAC GAG GAG TGG GCC AAG GAC CTG ACC GAC AGC CAG CGC GAG GCC CTG 866 Tyr Glu Glu Trp Ala Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu 685 690 695 GAC GGC TAC GCC CGC CAG GAC TAC AAG GAG ATC AAC AAC TAC CTG CGC 914 Asp Gly Tyr Ala Arg Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg 700 705 710 AAC CAG GGC GGC AGC GGC AAC GAG AAG CTG GAC GCC CAG ATC AAG AAC 962 Asn Gin Gly Gly Ser Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn 715 720 725 ATC AGC GAC GCC CTG GGC AAG AAG CCC ATC CCC GAG AAC ATC ACC GTG 1010 He Ser Asp Ala Leu Gly Lys Lys Pro He Pro Glu Asn He Thr Val 730 735 740 TAC CGC TGG TGC GGC ATG CCC GAG TTC GGC TAC CAG ATC AGC GAC CCC 1058 Tyr Arg Trp Cys Gly Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro 745 750 755 760 CTG CCC AGC CTG AAG GAC TTC GAG GAG CAG TTC CTG AAC ACC ATC AAG 1106 Leu Pro Ser Leu Lys Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys 765 770 775 GAG GAC AAG GGC TAC ATG AGC ACC AGC CTG AGC AGC GAG CGC CTG GCC 1154 Glu Asp Lys Gly Tyr Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala 780 785 790 GCC TTC GGC AGC CGC AAG ATC ATC CTG CGC CTG CAG GTG CCC AAG GGC 1202 Ala Phe Gly Ser Arg Lys He He Leu Arg Leu Gin Val Pro Lys Gly 795 800 805 AGC ACT GGT GCC TAC CTG AGC GCC ATC GGC GGC TTC GCC AGC GAG AAG 1250 Ser Thr Gly Ala Tyr Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys 810 815 820 GAG ATC CTG CTG GAT AAG GAC AGC AAG TAC CAC ATC GAC AAG GTG ACC 1298 Glu He Leu Leu Asp Lys Asp Ser Lys Tyr His He Asp Lys Val Thr 825 830 835 840 GAG GTG ATC ATC AAG GGC GTG AAG CGC TAC GTG GTG GAC GCC ACC CTG 1346 Glu Val He He Lys Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu 845 850 855 CTG ACC AAC TAG 1358 Leu Thr Asn (2) INFORMATION FOR SEQ ID NO:46: (i) SEQUENCE CHARACTERISTICS: (A) LEM-TH: 449 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:46: Met Gly Trp Ser Trp He Phe Leu Phe Leu Leu Ser Gly Ala Ala Gly 1 5 10 15 Val His Cys Leu Ser Ser Ser Ser Phe Ala Asp Ser Asn Pro He Arg 20 25 30 Val Thr Asp Arg Ala Ala Ser Thr Leu Gin Asn Leu Lys He Thr Asp 35 40 45 Lys Val Glu Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly 50 55 60 Lys Glu Lys Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys 65 70 75 80 Met Asn Asn Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys 85 90 95 Glu He Thr Phe Ser He Ala Gly Ser Phe Glu Asp Glu He Lys Asp 100 105 110 Leu Lys Glu He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser 115 120 125 He He Thr Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys 130 135 140 Ser Leu Thr Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe 145 150 155 160 Lys Glu Gin Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp 165 170 175 Thr His Leu Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu 180 185 190 Lys Val Thr Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala 195 200 205 Gly Val He Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly 210 215 220 Tyr Met Val His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val 225 230 235 240 Glu Cys Leu Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys 245 250 255 Asn Asp He Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu 260 265 270 Glu Trp Ala Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly 275 280 285 Tyr Ala Arg Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin 290 295 300 Gly Gly Ser Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser 305 310 315 320 Asp Ala Leu Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg 325 330 335 Trp Cys Gly Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro 340 345 350 Ser Leu Lys Asp Phe Glu Glu Gin Hie Leu Asn Thr He Lys Glu Asp 355 360 365 Lys Gly Tyr Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe 370 375 380 Gly Ser Arg Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr 385 390 395 400 Gly Ala Tyr Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He 405 410 415 Leu Leu Asp Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val 420 425 430 He He Lys Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr 435 440 445 Asn (2) INFORMATION FOR SEQ ID NO:47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MDLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: Peptide (B) LOCATION: 1..16 (D) OTHER INFORMATION: /note= "linker peptide for fusion of VIPlA(a) and VIP2A(a) used to construct pCIB5533" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:47: Pro Ser Thr Pro Pro Thr Pro Ser Pro Ser Thr Pro Pro Thr Pro Ser 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:48: (i) SEQUENCE CHARACTERISTICS: (A) LEN3TH: 66 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MDLECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "ENA encoding linker peptide used to construct pCIB5533" (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48: CCX-GGGCCTT CTACTCCCCC AACTCCCTCT CCTAGCACGC CTCCGACACC TAGCGATATC 60 GGATCC 66 (2) INFORMATION FOR SEQ ID NO:49: (i) SEQUENCE CHARACTERISTICS: (A) LE-SGTH: 4031 base pairs (B) TYPE: nucleic acid (C) -_TRA_røEENESS: single (D) TOPOLOGY: linear (ii) MDI-ECULE TYPE: other nucleic acid (A) DESCRIPTION: /desc = "Synthetic ENA" (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 6..4019 (D) OTHER INFORMATION: /note= "Maize optimized NA sequence encoding a VIP2A(a) - VIPlA(a) fusion protein as contained in pCIB5531" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49: GATCC ATG AAG CGC ATG GAG GGC AAG CTG TTC ATG GTG AGC AAG AAG 47 Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys 450 455 460 CTC CAG GTG GTG ACC AAG ACC GTG CTG CTG AGC ACC GTG TTC AGC ATC 95 Leu Gin Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser He 465 470 475 AGC CTG CTG AAC AAC GAG GTG ATC AAG GCC GAG CAG CTG AAC ATC AAC 143 Ser Leu Leu Asn Asn Glu Val He Lys Ala Glu Gin Leu Asn He Asn 480 485 490 495 AGC CAG AGC AAG TAC ACC AAC CTC CAG AAC CTG AAG ATC ACC GAC AAG 191 Ser Gin Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Thr Asp Lys 500 505 510 GTG GAG GAC TTC AAG GAG GAC AAG GAG AAG GCC AAG GAG TGG GGC AAG 239 Val Glu Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys 515 520 525 GAG AAG GAG AAG GAG TGG AAG CTT ACC GCC ACC GAG AAG GGC AAG ATG 287 Glu Lys Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met 530 535 540 AAC AAC TTC CTG GAC AAC AAG AAC GAC ATC AAG ACC AAC TAC AAG GAG 335 Asn Asn Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu 545 550 555 ATC ACC TTC AGC ATA GCC GGC AGC TTC GAG GAC GAG ATC AAG GAC CTG 383 He Thr Phe Ser He Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu 560 565 570 575 AAG GAG ATC GAC AAG ATG TTC GAC AAG ACC AAC CTG AGC AAC AGC ATC 431 Lys Glu He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He 580 585 590 ATC ACC TAC AAG AAC GTG GAG CCC ACC ACC ATC GGC TTC AAC AAG AGC 479 He Thr Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser 595 600 605 CTG ACC GAG GGC AAC ACC ATC AAC AGC GAC GCC ATG GCC CAG TTC AAG 527 Leu Thr Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys 610 615 620 GAG CAG TTC CTG GAC CGC GAC ATC AAG TTC GAC AGC TAC CTG GAC ACC 575 Glu Gin Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr 625 630 635 CAC CTG ACC GCC CAG CAG GTG AGC AGC AAG GAG CGC GTG ATC CTG AAG 623 His Leu Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys 640 645 650 655 GTG ACC GTC CCC AGC GGC AAG GGC AGC ACC ACC CCC ACC AAG GCC GGC 671 Val Thr Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly 660 665 670 GTG ATC CTG AAC AAC AGC GAG TAC AAG ATG CTG ATC GAC AAC GGC TAC 719 Val He Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr 675 680 685 ATG GTG CAC GTG GAC AAG GTG AGC AAG GTG GTG AAG AAG GGC GTG GAG 767 Met Val His Val Asp Lys Veil Ser Lys Val Val Lys Lys Gly Val Glu 690 695 700 TGC CTC CAG ATC GAG GGC ACC CTG AAG AAG ACT CTA GAC TTC AAG AAC 815 Cys Leu Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn 705 710 715 GAC ATC AAC GCC GAG GCC CAC AGC TGG GGC ATG AAG AAC TAC GAG GAG 863 Asp He Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu 720 725 730 735 TGG GCC AAG GAC CTG ACC GAC AGC CAG CGC GAG GCC CTG GAC GGC TAC 911 Trp Ala Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr 740 745 750 GCC CGC CAG GAC TAC AAG GAG ATC AAC AAC TAC CTG CGC AAC CAG GGC 959 Ala Arg Gin Asp Tyr Lys Glu He Asn Asn yr Leu Arg Asn Gin Gly 755 760 765 GGC AGC GGC AAC GAG AAG CTG GAC GCC CAG ATC AAG AAC ATC AGC GAC 1007 Gly Ser Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp 770 775 780 GCC CTG GGC AAG AAG CCC ATC CCC GAG AAC ATC ACC GTG TAC CGC TGG 1055 Ala Leu Gly Lys Lys Pro He Pro Glu Asn He Thr Veil Tyr Arg Trp 785 790 795 TGC GGC ATG CCC GAG TTC GGC TAC CAG ATC AGC GAC CCC CTG CCC AGC 1103 Cys Gly Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro .Ser 800 805 810 815 CTG AAG GAC TTC GAG GAG CAG TTC CTG AAC ACC ATC AAG GAG GAC AAG 1151 Leu Lys Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys 820 825 830 GGC TAC ATG AGC ACC AGC CTG AGC AGC GAG CGC CTG GCC GCC TTC GGC 1199 Gly Tyr Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly 835 840 845 AGC CGC AAG ATC ATC CTG CGC CTG CAG GTG CCC AAG GGC AGC ACT GCT 1247 Ser Arg Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly 850 855 860 GCC TAC CTG AGC GCC ATC GGC GGC TTC GCC AGC GAG AAG GAG ATC CTG 1295 Ala Tyr Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu 865 870 875 CIG GAT AAG GAC AGC AAG TAC CAC ATC GAC AAG GTG ACC GAG GTG ATC 1343 Leu Asp Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val He 880 885 890 895 ATC AAG GGC GTG AAG CGC TAC GTG GTG GAC GCC ACC CTG CTG ACC AAC 1391 He Lys Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 900 905 910 TCC CGG GGG CCT TCT ACT CCC CCA ACT CCC TCT CCT AGC ACG CCT CCG 1439 Ser Arg Gly Pro Ser Thr Pro Pro Thr Pro Ser Pro Ser Thr Pro Pro 915 920 925 ACA CCT AGC GAT ATC GGA TCC ACC ATG AAG ACC AAC CAG ATC AGC ACC 1487 Thr Pro Ser Asp He Gly Ser Thr Met Lys Thr Asn Gin He Ser Thr 930 935 940 ACC CAG AAG AAC CAG CAG AAG GAG ATG GAC CGC AAG GGC CTG CTG GGC 1535 Thr Gin Lys Asn Gin Gin Lys Glu Met Asp Arg Lys Gly Leu Leu Gly 945 950 955 TAC TAC TTC AAG GGC AAG GAC TTC AGC AAC CTG ACC ATG TTC GCC CCC 1583 Tyr Tyr Phe Lys Gly Lys Asp Phe Ser Asn Leu Thr Met Phe Ala Pro 960 965 970 975 ACG CGT GAC AGC ACC CTG ATC TAC GAC CAG CAG ACC GCC AAC AAG CTG 1631 Thr Arg Asp Ser Thr Leu He Tyr Asp Gin Gin Thr Ala Asn Lys Leu 980 985 990 CTG GAC AAG AAG CAG CAG GAG TAC CAG AGC ATC CGC TGG ATC GGC CTG 1679 Leu Asp Lys Lys Gin Gin Glu Tyr Gin Ser He Arg Trp He Gly Leu 995 1000 1005 ATC CAG AGC AAG GAG ACC GGC GAC TTC ACC TTC AAC CTG AGC GAG GAC 1727 He Gin Ser Lys Glu Thr Gly Asp Phe Thr Phe Asn Leu Ser Glu Asp 1010 1015 1020 GAG CAG GCC ATC ATC GAG ATC AAC GGC AAG ATC ATC AGC AAC AAG GGC 1775 Glu Gin Ala He He Glu He Asn Gly Lys He He Ser Asn Lys Gly 1025 1030 1035 AAG GAG AAG CAG GTG GTG CAC CTG GAG AAG GGC AAG CTG GTG CCC ATC 1823 Lys Glu Lys Gin Val Val His Leu Glu Lys Gly Lys Leu Val Pro He 1040 1045 1050 1055 AAG ATC GAG TAC CAG AGC GAC ACC AAG TTC AAC ATC GAC AGC AAG ACC 1871 Lys He Glu Tyr Gin Ser Asp Thr Lys Hie Asn He Asp Ser Lys Thr 1060 1065 1070 TTC AAG GAG CTG AAG CTT TTC AAG ATC GAC AGC CAG AAC CAG CCC CAG 1919 Phe Lys Glu Leu Lys Leu Phe Lys He Asp Ser Gin Asn Gin Pro Gin 1075 1080 1085 CAG GTG CAG CAG GAC GAG CTG CGC AAC CCC GAG TTC AAC AAG AAG GAG 1967 Gin Val Gin Gin Asp Glu Leu Arg Asn Pro Glu Phe Asn Lys Lys Glu 1090 1095 1100 AGC CAG GAG TTC CTG GCC AAG CCC AGC AAG ATC AAC CTG TTC ACC CAG 2015 Ser Gin Glu Phe Leu Ala Lys Pro Ser Lys He Asn Leu Phe Thr Gin 1105 1110 1115 CAG ATG AAG CGC GAG ATC GAC GAG GAC ACC GAC ACC GAC GGC GAC AGC 2063 Gin Met Lys Arg Glu He Asp Glu Asp Thr Asp Thr Asp Gly Asp Ser 1120 1125 1130 1135 ATC CCC GAC CTG TGG GAG GAG AAC GGC TAC ACC ATC CAG AAC CGC ATC 2111 He Pro Asp Leu Trp Glu Glu Asn Gly Tyr Thr He Gin Asn Arg He 1140 1145 1150 GCC GTG AAG TGG GAC GAC AGC CTG GCT AGC AAG GGC TAC ACC AAG TEC 2159 Ala Val Lys Trp Asp Asp Ser Leu Ala Ser Lys Gly Tyr Thr Lys Phe 1155 1160 1165 GTG AGC AAC CCC CTG GAG AGC CAC ACC GTG GGC GAC CCC TAC ACC GAC 2207 Val Ser Asn Pro Leu Glu Ser His Thr Val Gly Asp Pro Tyr Thr Asp 1170 1175 1180 TAC GAG AAG GCC GCC CGC GAC CTG GAC CTG AGC AAC GCC AAG GAG ACC 2255 Tyr Glu Lys Ala Ala Arg Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr 1185 1190 1195 TTC AAC CCC CTG GTG GCC GCC TTC CCC AGC GTG AAC GTG AGC ATG GAG 2303 Phe Asn Pro Leu Val Ala Ala Phe Pro Ser Val Asn Val Ser Met Glu 1200 1205 1210 1215 AAG GTG ATC CTG AGC CCC AAC GAG AAC CTG AGC AAC AGC GTG GAG AGC 2351 Lys Val He Leu Ser Pro Asn Glu Asn Leu Ser Asn Ser Val Glu Ser 1220 1225 1230 CAC TCG AGC ACC AAC TGG AGC TAC ACC AAC ACC GAG GGC GCC AGC GTG 2399 His Ser Ser Thr Asn Trp Ser Tyr Thr Asn Thr Glu Gly Ala Ser Val 1235 1240 1245 GAG GCC GGC ATC GGT CCC AAG GGC ATC AGC TTC GGC GTG AGC GTG AAC 2447 Glu Ala Gly He Gly Pro Lys Gly He Ser Phe Gly Val Ser Val Asn 1250 1255 1260 TAC CAG CAC AGC GAG ACC GTG GCC CAG GAG TGG GGC ACC AGC ACC GGC 2495 Tyr Gin His Ser Glu Thr Val Ala Gin Glu Trp Gly Thr Ser Thr Gly 1265 1270 1275 AAC ACC AGC CAG T C AAC ACC GCC AGC GCC GGC TAC CTG AAC GCC AAC 2543 Asn Thr Ser Gin Phe Asn Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn 1280 1285 1290 1295 GTG CGC TAC AAC AAC GTG GGC ACC GGC GCC ATC TAC GAC GTG AAG CCC 2591 Val Arg Tyr Asn Asn Val Gly Thr Gly Ala He Tyr Asp Val Lys Pro 1300 1305 1310 ACC ACC AGC TTC GTG CTG AAC AAC GAC ACC ATC GCC ACC ATC ACC GCC 2639 Thr Thr Ser Phe Val Leu Asn Asn Asp Thr He Ala Thr He Thr Ala 1315 1320 1325 AAG TCG AAT TCC ACC GCC CTG AAC ATC AGC CCC GGC GAG AGC TAC CCC 2687 Lys Ser Asn Ser Thr Ala Leu Asn He Ser Pro Gly Glu Ser Tyr Pro 1330 1335 1340 AAG AAG GGC CAG AAC GGC ATC GCC ATC ACC AGC ATG GAC GAC TTC AAC 2735 Lys Lys Gly Gin Asn Gly He Ala He Thr Ser Met Asp Asp Phe Asn 1345 1350 1355 AGC CAC CCC ATC ACC CTG AAC AAG AAG CAG GTG GAC AAC CTG CTG AAC 2783 Ser His Pro He Thr Leu Asn Lys Lys Gin Val Asp Asn Leu Leu Asn 1360 1365 1370 1375 AAC AAG CCC ATG ATG CTG GAG ACC AAC CAG ACC GAC GGC GTC TAC AAG 2831 Asn Lys Pro Met Met Leu Glu Thr Asn Gin Thr Asp Gly Val Tyr Lys 1380 1385 1390 ATC AAG GAC ACC CAC GGC AAC ATC GTG ACG GGC GGC GAG TGG AAC GGC 2879 He Lys Asp Thr His Gly Asn He Val Thr Gly Gly Glu Trp Asn Gly 1395 1400 1405 GTG ATC CAG CAG ATC AAG GCC AAG ACC GCC AGC ATC ATC GTC GAC GAC 2927 Val He Gin Gin He Lys Ala Lys Thr Ala Ser He He Val Asp Asp 1410 1415 1420 GGC GAG CGC GTG GCC GAG AAG CGC GTG GCC GCC AAG GAC TAC GAG AAC 2975 Gly Glu Arg Val Ala Glu Lys Arg Val Ala Ala Lys Asp Tyr Glu Asn 1425 1430 1435 CCC GAG GAC AAG ACC CCC AGC CTG ACC CTG AAG GAC GCC CTG AAG CTG 3023 Pro Glu Asp Lys Thr Pro Ser Leu Thr Leu Lys Asp Ala Leu Lys Leu 1440 1445 1450 1455 AGC TAC CCC GAC GAG ATC AAG GAG ATC GAG GGC TTG CTG TAC TAC AAG 3071 Ser Tyr Pro Asp Glu He Lys Glu He Glu Gly Leu Leu Tyr T r Lys 1460 1465 1470 AAC AAG CCC ATC TAC GAG AGC AGC GTG ATG ACC TAT CTA GAC GAG AAC 3119 Asn Lys Pro He Tyr Glu Ser Ser Val Met Thr Tyr Leu Asp Glu Asn 1475 1480 1485 ACC GCC AAG GAG GTG ACC AAG CAG CTG AAC GAC ACC ACC GGC AAG TTC 3167 Thr Ala Lys Glu Val Thr Lys Gin Leu Asn Asp Thr Thr Gly Lys Phe 1490 1495 1500 AAG GAC GTG AGC CAC CTG TAC GAC GTG AAG CTG ACC CCC AAG ATG AAC 3215 Lys Asp Val Ser His Leu Asp Val Lys Leu Thr Pro Lys Met Asn 1505 1510 1515 GTG ACC ATC AAG CTG AGC ATC CTG TAC GAC AAC GCC GAG AGC AAC GAC 3263 Val Thr He Lys Leu Ser He Leu Tyr Asp Asn Ala Glu Ser Asn Asp 1520 1525 1530 1535 AAC AGC ATC GGC AAG TGG ACC AAC ACC AAC ATC GTG AGC GGC GGC AAC 3311 Asn Ser He Gly Lys Trp Thr Asn Thr Asn He Val Ser Gly Gly Asn 1540 1545 1550 AAC GGC AAG AAG CAG TAC AGC AGC AAC AAC CCC GAC GCC AAC CTG ACC 3359 Asn Gly Lys Lys Gin Tyr Ser Ser Asn Asn Pro Asp Ala Asn Leu Thr 1555 1560 1565 CTG AAC ACC GAC GCC CAG GAG AAG CTG AAC AAG AAC CGC GAC TAC TAC 3407 Leu Asn Thr Asp Ala Gin Glu Lys Leu Asn Lys Asn Arg Asp Tyr Tyr 1570 1575 1580 ATC AGC CTG TAC ATG AAG AGC GAG AAG AAC ACC CAG TGC GAG ATC ACC 3455 He Ser Leu Tyr Met Lys Ser Glu Lys Asn Thr Gin Cys Glu He Thr 1585 1590 1595 ATC GAC GGC GAG ATA TAC CCC ATC ACC ACC AAG ACC GTG AAC GTG AAC 3503 He Asp Gly Glu He Tyr Pro He Thr Thr Lys Thr Val Asn Val Asn 1600 1605 1610 1615 AAG GAC AAC TAC AAG CGC CTG GAC ATC ATC GCC CAC AAC ATC AAG AGC 3551 Lys Asp Asn Tyr Lys Arg Leu Asp He He Ala His Asn He Lys Ser 1620 1625 1630 AAC CCC ATC AGC AGC CTG CAC ATC AAG ACC AAC GAC GAG ATC ACC CTG 3599 Asn Pro He Ser Ser Leu His He Lys Thr Asn Asp Glu He Thr Leu 1635 1640 1645 TTC TGG GAC GAC ATA TCG ATT ACC GAC GTC GCC AGC ATC AAG CCC GAG 3647 Phe Trp Asp Asp He Ser He Thr Asp Val Ala Ser He Lys Pro Glu 1650 1655 1660 AAC CTG ACC GAC AGC GAG ATC AAG CAG ATA TAC AGT CGC TAC GGC ATC 3695 Asn Leu Thr Asp Ser Glu He Lys Gin He Tyr Ser Arg Tyr Gly He 1665 1670 1675 AAG CTG GAG GAC GGC ATC CTG ATC GAC AAG AAA GGC GGC ATC CAC TAC 3743 Lys leu Glu Asp Gly He Leu He Asp Lys Lys Gly Gly He His Tyr 1680 1685 1690 1695 GGC GAG TTC ATC AAC GAG GCC AGC TTC AAC ATC GAG CCC CTG CAG AAC 3791 Gly Glu Phe He Asn Glu Ala Ser Phe Asn He Glu Pro Leu Gin Asn 1700 1705 1710 TAC GTG ACC AAG TAC GAG GTG ACC TAC AGC AGC GAG CTG GGC CCC AAC 3839 Tyr Val Thr Lys Tyr Glu Val Thr Tyr Ser Ser Glu Leu Gly Pro Asn 1715 1720 1725 GTG AGC GAC ACC CTG GAG AGC GAC AAG ATT TAC AAG GAC GGC ACC ATC 3887 Val Ser Asp Thr Leu Glu Ser Asp Lys He Tyr Lys Asp Gly Thr He 1730 1735 1740 AAG TTC GAC TTC ACC AAG TAC AGC AAG AAC GAG CAG GGC CTG TTC TAC 3935 Lys Phe Asp Phe Thr Lys Tyr Ser Lys Asn Glu Gin Gly Leu Phe Tyr 1745 1750 1755 GAC AGC GGC CTG AAC TOG GAC TTC AAG ATC AAC GCC ATC ACC TAC GAC 3983 Asp Ser Gly Leu Asn Trp Asp Phe Lys He Asn Ala He Thr Tyr Asp 1760 1765 1770 1775 GGC AAG GAG ATG AAC GTG TTC CAC CGC TAC AAC AAG TAGATCTGAG 4029 Gly Lys Glu Met Asn Val Phe His Arg Tyr Asn Lys 1780 1785 CT 4031 (2) INFORMATION FOR SEQ ID NO:50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1338 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:50: Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu Gin 1 5 10 15 Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser He Ser Leu 20 25 30 Leu Asn Asn Glu Val He Lys Ala Glu Gin Leu Asn He Asn Ser Gin 35 40 45 Ser Lys Tyr Thr Asn Leu Gin Asn Leu Lys He Thr Asp Lys Val Glu 50 55 60 Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys 65 70 75 80 Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn 85 90 95 Phe Leu Asp Asn Lys Asn Asp He Lys Thr Asn Tyr Lys Glu He Thr 100 105 110 Phe Ser He Ala Gly Ser Phe Glu Asp Glu He Lys Asp Leu Lys Glu 115 120 125 He Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser He He Thr 130 135 140 Tyr Lys Asn Val Glu Pro Thr Thr He Gly Phe Asn Lys Ser Leu Thr 145 150 155 160 Glu Gly Asn Thr He Asn Ser Asp Ala Met Ala Gin Phe Lys Glu Gin 165 170 175 Phe Leu Asp Arg Asp He Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 180 185 190 Thr Ala Gin Gin Val Ser Ser Lys Glu Arg Val He Leu Lys Val Thr 195 200 205 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val He 210 215 220 Leu Asn Asn Ser Glu Tyr Lys Met Leu He Asp Asn Gly Tyr Met Val 225 230 235 240 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu 245 250 255 Gin He Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp He 260 265 270 Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala 275 280 285 Lys Asp Leu Thr Asp Ser Gin Arg Glu Ala Leu Asp Gly Tyr Ala Arg 290 295 300 Gin Asp Tyr Lys Glu He Asn Asn Tyr Leu Arg Asn Gin Gly Gly Ser 305 310 315 320 Gly Asn Glu Lys Leu Asp Ala Gin He Lys Asn He Ser Asp Ala Leu 325 330 335 Gly Lys Lys Pro He Pro Glu Asn He Thr Val Tyr Arg Trp Cys Gly 340 345 350 Met Pro Glu Phe Gly Tyr Gin He Ser Asp Pro Leu Pro Ser Leu Lys 355 360 365 Asp Phe Glu Glu Gin Phe Leu Asn Thr He Lys Glu Asp Lys Gly Tyr 370 375 380 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg 385 390 395 400 Lys He He Leu Arg Leu Gin Val Pro Lys Gly Ser Thr Gly Ala Tyr 405 410 415 Leu Ser Ala He Gly Gly Phe Ala Ser Glu Lys Glu He Leu Leu Asp 420 425 430 Lys Asp Ser Lys Tyr His He Asp Lys Val Thr Glu Val He He Lys 435 440 445 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn Ser Arg 450 455 460 Gly Pro Ser Thr Pro Pro Thr Pro Ser Pro Ser Thr Pro Pro Thr Pro 465 470 475 480 Ser Asp He Gly Ser Thr Met Lys Thr Asn Gin He Ser Thr Thr Gin 485 490 495 Lys Asn Gin Gin Lys Glu Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr 500 505 510 Phe Lys Gly Lys Asp Phe Ser Asn leu Thr Met Phe Ala Pro Thr Arg 515 520 525 Asp Ser Thr Leu He Tyr Asp Gin Gin Thr Ala Asn Lys Leu Leu Asp 530 535 540 Lys Lys Gin Gin Glu Tyr Gin Ser He Arg Trp He Gly Leu He Gin 545 550 555 560 Ser Lys Glu Thr Gly Asp Phe Thr Phe Asn Leu Ser Glu Asp Glu Gin 565 570 575 Ala He He Glu He Asn Gly Lys He He Ser Asn Lys Gly Lys Glu 580 585 590 Lys Gin Val Val His Leu Glu Lys Gly Lys Leu Val Pro He Lys He 595 600 605 Glu Tyr Gin Ser Asp Thr Lys Phe Asn He Asp Ser Lys Thr Phe Lys 610 615 620 Glu Leu Lys Leu Phe Lys He Asp Ser Gin Asn Gin Pro Gin Gin Val 625 630 635 640 Gin Gin Asp Glu Leu Arg Asn Pro Glu Phe Asn Lys Lys Glu Ser Gin 645 650 655 Glu Phe Leu Ala Lys Pro Ser Lys He Asn Leu Phe Thr Gin Gin Met 660 665 670 Lys Arg Glu He Asp Glu Asp Thr Asp Thr Asp Gly Asp Ser He Pro 675 680 685 Asp Leu Trp Glu Glu Asn Gly Tyr Thr He Gin Asn Arg He Ala Val 690 695 700 Lys Trp Asp Asp Ser Leu Ala Ser Lys Gly Tyr Thr Lys Phe Val Ser 705 710 715 720 Asn Pro Leu Glu Ser His Thr Val Gly Asp Pro Tyr Thr Asp Tyr Glu 725 730 735 Lys Ala Ala Arg Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn 740 745 750 Pro Leu Val Ala Ala Phe Pro Ser Val Asn Val Ser Met Glu Lys Val 755 760 765 He Leu Ser Pro Asn Glu Asn Leu Ser Asn Ser Veil Glu Ser His Ser 770 775 780 Ser Thr Asn Trp Ser Tyr Thr Asn Thr Glu Gly Ala Ser Val Glu Ala 785 790 795 800 Gly He Gly Pro Lys Gly He Ser Phe Gly Val Ser Val Asn Tyr Gin 805 810 815 His Ser Glu Thr Val Ala Gin Glu Trp Gly Thr Ser Thr Gly Asn Thr 820 825 830 Ser Gin Phe Asn Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg 835 840 845 Tyr Asn Asn Val Gly Thr Gly Ala He Tyr Asp Val Lys Pro Thr Thr 850 855 860 Ser Phe Val Leu Asn Asn Asp Thr He Ala Thr He Thr Ala Lys Ser 865 870 875 880 Asn Ser Thr Ala Leu Asn He Ser Pro Gly Glu Ser Tyr Pro Lys Lys 885 890 895 Gly Gin Asn Gly He Ala He Thr Ser Met Asp Asp Phe Asn Ser His 900 905 910 Pro He Thr Leu Asn Lys Lys Gin Val Asp Asn Leu Leu Asn Asn Lys 915 920 925 Pro Met Met Leu Glu Thr Asn Gin Thr Asp Gly Val Tyr Lys He Lys 930 935 940 Asp Thr His Gly Asn He Val Thr Gly Gly Glu Trp Asn Gly Val He 945 950 955 960 Gin Gin He Lys Ala Lys Thr Ala Ser He He Val Asp Asp Gly Glu 965 970 975 Arg Val Ala Glu Lys Arg Val Ala Ala Lys Asp Tyr Glu Asn Pro Glu 980 985 990 Asp Lys Thr Pro Ser Leu Thr Leu Lys Asp Ala Leu Lys Leu Ser Tyr 995 1000 1005 Pro Asp Glu He Lys Glu He Glu Gly Leu Leu Tyr Tyr Lys Asn Lys 1010 1015 1020 Pro He Tyr Glu Ser Ser Val Met Thr Tyr Leu Asp Glu Asn Thr Ala 1025 1030 1035 1040 Lys Glu Val Thr Lys Gin Leu Asn Asp Thr Thr Gly Lys Phe Lys Asp 1045 1050 1055 Val Ser His Leu Tyr Asp Veil Lys Leu Thr Pro Lys Met Asn Val Thr 1060 1065 1070 He Lys Leu Ser He Leu Tyr Asp Asn Ala Glu Ser Asn Asp Asn Ser 1075 1080 1085 He Gly Lys Trp Thr Asn Thr Asn He Val Ser Gly Gly Asn Asn Gly 1090 1095 1100 Lys Lys Gin Tyr Ser Ser Asn Asn Pro Asp Ala Asn Leu Thr Leu Asn 1105 1110 1115 1120 Thr Asp Ala Gin Glu Lys Leu Asn Lys Asn Arg Asp Tyr Tyr He Ser 1125 1130 1135 Leu Tyr Met Lys Ser Glu Lys Asn Thr Gin Cys Glu He Thr He Asp 1140 1145 1150 Gly Glu He Tyr Pro He Thr Thr Lys Thr Val Asn Val Asn Lys Asp 1155 1160 1165 Asn Tyr Lys Arg Leu Asp He He Ala His Asn He Lys Ser Asn Pro 1170 1175 1180 He Ser Ser Leu His He Lys Thr Asn Asp Glu He Thr Leu Phe Trp 1185 1190 1195 1200 Asp Asp He Ser He Thr Asp Val Ala Ser He Lys Pro Glu Asn Leu 1205 1210 1215 Thr Asp Ser Glu He Lys Gin He Tyr Ser Arg Tyr Gly He Lys Leu 1220 1225 1230 Glu Asp Gly He Leu He Asp Lys Lys Gly Gly He His Tyr Gly Glu 1235 1240 1245 Phe He Asn Glu Ala Ser Phe Asn He Glu Pro Leu Gin Asn Tyr Val 1250 1255 1260 Thr Lys Tyr Glu Val Thr Tyr Ser Ser Glu Leu Gly Pro Asn Val Ser 1265 1270 1275 1280 Asp Thr Leu Glu Ser Asp Lys He Tyr Lys Asp Gly Thr He Lys Phe 1285 1290 1295 Asp Phe Thr Lys Tyr Ser Lys Asn Glu Gin Gly Leu Phe Tyr Asp Ser 1300 1305 1310 Gly Leu Asn Trp Asp Phe Lys He Asn Ala He Thr Tyr Asp Gly Lys 1315 1320 1325 Glu Met Asn Val Phe His Arg Tyr Asn Lys 1330 1335 (2) INFORMATION FOR SEQ ID NO:51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2444 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MD-_ECULE TYPE: ENA (genαmic) (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 17..2444 (D) OTHER INFORMATION: /product= "3A(a) synthetic:native fusion" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:51: GGATCCACCA ATGAAC ATG AAC AAG AAC AAC ACC AAG CTG AGC ACC CGC 49 Met Asn Lys Asn Asn Thr Lys Leu Ser Thr Arg 1 5 10 GCC CTG CCG AGC TTC ATC GAC TAC TTC AAC GGC ATC TAC GGC TTC GCC 97 Ala Leu Pro Ser Phe He Asp Tyr Phe Asn Gly He Tyr Gly Phe Ala 15 20 25 ACC GGC ATC AAG GAC ATC ATG AAC ATG ATC TTC AAG ACC GAC ACC GGC 145 Thr Gly He Lys Asp He Met Asn Met He Phe Lys Thr Asp Thr Gly 30 35 40 GGC GAC CTG ACC CTG GAC GAG ATC CTG AAG AAC CAG CAG CTG CTG AAC 193 Gly Asp Leu Thr Leu Asp Glu He Leu Lys Asn Gin Gin Leu Leu Asn 45 50 55 GAC ATC AGC GGC AAG CTG GAC GGC GTG AAC GGC AGC CTG AAC GAC CTG 241 Asp He Ser Gly Lys Leu Asp Gly Val Asn Gly Ser Leu Asn Asp Leu 60 65 70 75 ATC GCC CAG GGC AAC CTG AAC ACC GAG CTG AGC AAG GAG ATC CTT AAG 289 He Ala Gin Gly Asn Leu Asn Thr Glu Leu Ser Lys Glu He Leu Lys 80 85 90 ATC GCC AAC GAG CAG AAC CAG GTG CTG AAC GAC GTG AAC AAC AAG CTG 337 He Ala Asn Glu Gin Asn Gin Val Leu Asn Asp Val Asn Asn Lys Leu 95 100 105 GAC GCC ATC AAC ACC ATG CTG CGC GTG TAC CTG CCG AAG ATC ACC AGC 385 Asp Ala He Asn Thr Met Leu Arg Val Tyr Leu Pro Lys He Thr Ser 110 115 120 ATG CTG AGC GAC GTG ATG AAG CAG AAC TAC GCC CTG AGC CTG CAG ATC 433 Met Leu Ser Asp Val Met Lys Gin Asn Tyr Ala Leu Ser Leu Gin He 125 130 135 GAG TAC CTG AGC AAG CAG CTG CAG GAG ATC AGC GAC AAG CTG GAC ATC 481 Glu Tyr Leu Ser Lys Gin Leu Gin Glu He Ser Asp Lys Leu Asp He 140 145 150 155 ATC AAC GTG AAC GTC CTG ATC AAC AGC ACC CTG ACC GAG ATC ACC CCG 529 He Asn Val Asn Val Leu He Asn Ser Thr leu Thr Glu He Thr Pro 160 165 170 GCC TAC CAG CGC ATC AAG TAC GTG AAC GAG AAG TTC GAA GAG CTG ACC 577 Ala Tyr Gin Arg He Lys Tyr Val Asn Glu Lys Phe Glu Glu Leu Thr 175 180 185 TTC GCC ACC GAG ACC AGC AGC AAG GTG AAG AAG GAC GGC AGC CCG GCC 625 Phe Ala Thr Glu Thr Ser Ser Lys Val Lys Lys Asp Gly Ser Pro Ala 190 195 200 GAC ATC CTG GAC GAG CTG ACC GAG CTG ACC GAG CTG GCC AAG AGC GTG 673 Asp He Leu Asp Glu Leu Thr Glu Leu Thr Glu Leu Ala Lys Ser Val 205 210 215 ACC AAG AAC GAC GTG GAC GGC TTC GAG TTC TAC CTG AAC ACC TTC CAC 721 Thr Lys Asn Asp Val Asp Gly Phe Glu Phe Tyr Leu Asn Thr Phe His 220 225 230 235 GAC GTG ATG GTG GGC AAC AAC CTG TTC GGC CGC AGC GCC CTG AAG ACC 769 Asp Val Met Val Gly Asn Asn Leu Phe Gly Arg Ser Ala Leu Lys Thr 240 245 250 GCC AGC GAG CTG ATC ACC AAG GAG AAC GTG AAG ACC AGC GGC AGC GAG 817 Ala Ser Glu Leu He Thr Lys Glu Asn Val Lys Thr Ser Gly Ser Glu 255 260 265 GTG GGC AAC GTG TAC AAC TTC CTG ATC GTG CTG ACC GCC CTG CAG GCC 865 Val Gly Asn Val Tyr Asn Phe eu He Val Leu Thr Ala Leu Gin Ala 270 275 280 CAG GCC TTC CTG ACC CTG ACC ACC TGT CGC AAG CTG CTG GGC CTG GCC 913 Gin Ala Phe Leu Thr Leu Thr Thr Cys Arg Lys Leu Leu Gly Leu Ala 285 290 295 GAC ATC GAC TAC ACC AGC ATC ATG AAC GAG CAC TTG AAC AAG GAG AAG 961 Asp He Asp Tyr Thr Ser He Met Asn Glu His Leu Asn Lys Glu Lys 300 305 310 315 GAG GAG TTC CGC GTG AAC ATC CTG CCG ACC CTG AGC AAC ACC TTC AGC 1009 Glu Glu Phe Arg Val Asn He Leu Pro Thr Leu Ser Asn Thr Phe Ser 320 325 330 AAC CCG AAC TAC GCC AAG GTG AAG GGC AGC GAC GAG GAC GCC AAG ATG 1057 Asn Pro Asn Tyr Ala Lys Val Lys Gly Ser Asp Glu Asp Ala Lys Met 335 340 345 ATC GTG GAG GCT AAG CCG GGC CAC GCG T G ATC GGC TTC GAG ATC AGC 1105 He Val Glu Ala Lys Pro Gly His Ala Leu He Gly Phe Glu He Ser 350 355 360 AAC GAC AGC ATC ACC GTG CTG AAG GTG TAC GAG GCC AAG CTG AAG CAG 1153 Asn Asp Ser He Thr Val Leu Lys Val Tyr Glu Ala Lys Leu Lys Gin 365 370 375 AAC TAC CAG GTG GAC AAG GAC AGC TTG AGC GAG GTG ATC TAC GGC GAC 1201 Asn Tyr Gin Val Asp Lys Asp Ser Leu Ser Glu Val He Tyr Gly Asp 380 385 390 395 ATG GAC AAG CTG CTG TGT CCG GAC CAG AGC GAG CAA ATC TAC TAC ACC 1249 Met Asp Lys Leu Leu Cys Pro Asp Gin Ser Glu Gin He Tyr Tyr Thr 400 405 410 AAC AAC ATC GTG TTC CCG AAC GAG TAC GTG ATC ACC AAG ATC GAC TTC 1297 Asn Asn He Val Phe Pro Asn Glu Tyr Val He Thr Lys He Asp Phe 415 420 425 ACC AAG AAG ATG AAG ACC CTG CGC TAC GAG GTG ACC GCC AAC TTC TAC 1345 Thr Lys Lys Met Lys Thr Leu Arg Tyr Glu Val Thr Ala Asn Phe Tyr 430 435 440 GAC AGC AGC ACC GGC GAG ATC GAC CTG AAC AAG AAG AAG GTG GAG AGC 1393 Asp Ser Ser Thr Gly Glu He Asp Leu Asn Lys Lys Lys Val Glu Ser 445 450 455 AGC GAG GCC GAG TAC CGC ACC CTG AGC GCG AAC GAC GAC GGC GTC TAC 1441 Ser Glu Ala Glu Tyr Arg Thr Leu Ser Ala Asn Asp Asp Gly Val Tyr 460 465 470 475 ATG CCA CTG GGC GTG ATC AGC GAG ACC TTC CTG ACC CCG ATC AAC GGC 1489 Met Pro Leu Gly Val He Ser Glu Thr Phe Leu Thr Pro He Asn Gly 480 485 490 TTT GGC CTG CAG GCC GAC GAG AAC AGC CGC CTG ATC ACC CTG ACC TGT 1537 Phe Gly Leu Gin Ala Asp Glu Asn Ser Arg Leu He Thr Leu Thr Cys 495 500 505 AAG AGC TAC CTG CGC GAG CTG CTG CTA GCC ACC GAC CTG AGC AAC AAG 1585 Lys Ser Tyr Leu Arg Glu Leu Leu Leu Ala Thr Asp Leu Ser Asn Lys 510 515 520 GAG ACC AAG CTG ATC GTG CCA CCG AGC GGC TTC ATC AGC AAC ATC GTG 1633 Glu Thr Lys Leu He Val Pro Pro Ser Gly Phe He Ser Asn He Val 525 530 535 GAG AAC GGC AGC ATC GAG GAG GAC AAC CTG GAG CCG TGG AAG GCC AAC 1681 Glu Asn Gly Ser He Glu Glu Asp Asn Leu Glu Pro Trp Lys Ala Asn 540 545 550 555 AAC AAG AAC GCC TAC GTG GAC CAC ACC GGC GGC GTG AAC GGC ACC AAG 1729 Asn Lys Asn Ala Tyr Val Asp His Thr Gly Gly Val Asn Gly Thr Lys 560 565 570 GCC CTG TAC GTG CAC AAG GAC GGC GGC ATC AGC CAG TTC ATC GGC GAC 1777 Ala Leu Tyr Val His Lys Asp Gly Gly He Ser Gin Phe He Gly Asp 575 580 585 AAG CTG AAG CCG AAG ACC GAG TAC GTG ATC CAG TAC ACC GTG AAG GGC 1825 Lys Leu Lys Pro Lys Thr Glu Tyr Val He Gin Tyr Thr Val Lys Gly 590 595 600 AAG CCA TCG ATT CAC CTG AAG GAC GAG AAC ACC GGC TAC ATC CAC TAC 1873 Lys Pro Ser He His Leu Lys Asp Glu Asn Thr Gly Tyr He His Tyr 605 610 615 GAG GAC ACC AAC AAC AAC CTG GAG GAC TAC CAG ACC ATC AAC AAG CGC 1921 Glu Asp Thr Asn Asn Asn Leu Glu Asp Tyr Gin Thr He Asn Lys Arg 620 625 630 635 TTC ACC ACC GGC ACC GAC CTG AAG GGC GTG TAC CTG ATC CTG AAG AGC 1969 Phe Thr Thr Gly Thr Asp Leu Lys Gly Val Tyr Leu He Leu Lys Ser 640 645 650 CAG AAC GGC GAC GAG GCC TGG GGC GAC AAC TTC ATC ATC CTG GAG ATC 2017 Gin Asn Gly Asp Glu Ala Trp Gly Asp Asn Phe He He Leu Glu He 655 660 665 AGC CCG AGC GAG AAG CTG CTG AGC CCG GAG CTG ATC AAC ACC AAC AAC 2065 Ser Pro Ser Glu Lys Leu Leu Ser Pro Glu Leu He Asn Thr Asn Asn 670 675 680 TGG ACC AGC ACC GGC AGC ACC AAC ATC AGC GGC AAC ACC CTG ACC CTG 2113 Trp Thr Ser Thr Gly Ser Thr Asn He Ser Gly Asn Thr Leu Thr Leu 685 690 695 TAC CAG GGC GGC CGG GGG ATT CTA AAA CAA AAC CTT CAA TTA GAT ACT 2161 Tyr Gin Gly Gly Arg Gly He Leu Lys Gin Asn eu Gin Leu Asp Ser 700 705 710 715 TTT TCA ACT TAT AGA GTG TAT TTT TCT GTG TCC GGA GAT GCT AAT GTA 2209 Phe Ser Thr Tyr Arg Val Tyr Phe Ser Val Ser Gly Asp Ala Asn Veil 720 725 730 AGG ATT AGA AAT TCT AGG GAA GTG TTA TTT GAA AAA AGA TAT ATG AGC 2257 Arg He Arg Asn Ser Arg Glu Val Leu Phe Glu Lys Arg Tyr Met Ser 735 740 745 GCT GCT AAA GAT GTT TCT GAA ATG TTC ACT ACA AAA TTT GAG AAA GAT 2305 Gly Ala Lys Asp Val Ser Glu Met Phe Thr Thr Lys Phe Glu Lys Asp 750 755 760 AAC TTT TAT ATA GAG CTT TCT CAA GGG AAT AAT TTA TAT GCT GCT CCT 2353 Asn Phe Tyr He Glu Leu Ser Gin Gly Asn Asn Leu Tyr Gly Gly Pro 765 770 775 ATT GTA CAT TTT TAC GAT GTC TCT ATT AAG NAA GAT CGG GAT CTA ATA 2401 He Veil His Phe Tyr Asp Val Ser He Lys Xe_a Asp Arg Asp Leu He 780 785 790 795 TTA ACA GTT TTT AAA AGC NAA TTC TTG TAT AAT GTC CTT GAT T 2444 Leu Thr Val Phe Lys Ser Xaa Phe Leu Tyr Asn Val Leu Asp 800 805 (2) INFORMATION FOR SEQ ID NO:52: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 809 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:52: Met Asn Lys Asn Asn Thr Lys Leu Ser Thr Arg Ala Leu Pro Ser Phe 1 5 10 15 Ile Asp Tyr Phe Asn Gly He Tyr Gly Phe Ala Thr Gly He Lys Asp 20 25 30 He Met Asn Met He Phe Lys Thr Asp Thr Gly Gly Asp Leu Thr Leu 35 40 45 Asp Glu He Leu Lys Asn Gin Gin Leu Leu Asn Asp He Ser Gly Lys 50 55 60 Leu Asp Gly Val Asn Gly Ser Leu Asn Asp Leu He Ala Gin Gly Asn 65 70 75 80 Leu Asn Thr Glu Leu Ser Lys Glu He Leu Lys He Ala Asn Glu Gin 85 90 95 Asn Gin Val Leu Asn Asp Val Asn Asn Lys Leu Asp Ala He Asn Thr 100 105 110 Met Leu Arg Val Tyr Leu Pro Lys He Thr Ser Met Leu Ser Asp Val 115 120 125 Met Lys Gin Asn Tyr Ala Leu Ser Leu Gin He Glu Tyr Leu Ser Lys 130 135 140 Gin Leu Gin Glu He Ser Asp Lys Leu Asp He He Asn Val Asn Val 145 150 155 160 Leu He Asn Ser Thr Leu Thr Glu He Thr Pro Ala Tyr Gin Arg He 165 170 175 Lys Tyr Val Asn Glu Lys Phe Glu Glu Leu Thr Phe Ala Thr Glu Thr 180 185 190 Ser Ser Lys Val Lys Lys Asp Gly Ser Pro Ala Asp He Leu Asp Glu 195 200 205 Leu Thr Glu Leu Thr Glu Leu Ala Lys Ser Val Thr Lys Asn Asp Val 210 215 220 Asp Gly Phe Glu Phe Tyr Leu Asn Thr Phe His Asp Val Met Val Gly 225 230 235 240 Asn Asn Leu Phe Gly Arg Ser Ala Leu Lys Thr Ala Ser Glu Leu He 245 250 255 Thr Lys Glu Asn Val Lys Thr Ser Gly Ser Glu Val Gly Asn Val Tyr 260 265 270 Asn Phe Leu He Val Leu Thr Ala Leu Gin Ala Gin Ala Phe Leu Thr 275 280 285 Leu Thr Thr Cys Arg Lys Leu Leu Gly Leu Ala Asp He Asp Tyr Thr 290 295 300 Ser He Met Asn Glu His Leu Asn Lys Glu Lys Glu Glu Phe Arg Val 305 310 315 320 Asn He Leu Pro Thr Leu Ser Asn Thr Phe Ser Asn Pro Asn Tyr Ala 325 330 335 Lys Val Lys Gly Ser Asp Glu Asp Ala Lys Met He Val Glu Ala Lys 340 345 350 Pro Gly His Ala Leu He Gly Phe Glu He Ser Asn Asp Ser He Thr 355 360 365 Val Leu Lys Val Tyr Glu Ala Lys Leu Lys Gin Asn Tyr Gin Val Asp 370 375 380 Lys Asp Ser Leu Ser Glu Val He Tyr Gly Asp Met Asp Lys Leu Leu 385 390 395 400 Cys Pro Asp Gin Ser Glu Gin He Tyr Tyr Thr Asn Asn He Val Phe 405 410 415 Pro Asn Glu Tyr Val He Thr Lys He Asp Phe Thr Lys Lys Met Lys 420 425 430 Thr Leu Arg Tyr Glu Val Thr Ala Asn Phe Tyr Asp Ser Ser Thr Gly 435 440 445 Glu He Asp Leu Asn Lys Lys Lys Val Glu Ser Ser Glu Ala Glu Tyr 450 455 460 Arg Thr Leu Ser Ala Asn Asp Asp Gly Val Tyr Met Pro Leu Gly Val 465 470 475 480 He Ser Glu Thr Phe Leu Thr Pro He Asn Gly Phe Gly Leu Gin Ala 485 490 495 Asp Glu Asn Ser Arg Leu He Thr Leu Thr Cys Lys Ser Tyr Leu Arg 500 505 510 Glu Leu Leu Leu Ala Thr Asp Leu Ser Asn Lys Glu Thr Lys Leu He 515 520 525 Val Pro Pro Ser Gly Phe He Ser Asn He Val Glu Asn Gly Ser He 530 535 540 Glu Glu Asp Asn Leu Glu Pro Trp Lys Ala Asn Asn Lys Asn Ala Tyr 545 550 555 560 Val Asp His Thr Gly Gly Val Asn Gly Thr Lys Ala Leu Tyr Val His 565 570 575 Lys Asp Gly Gly He Ser Gin Phe He Gly Asp Lys Leu Lys Pro Lys 580 585 590 Thr Glu Tyr Val He Gin Tyr Thr Val Lys Gly Lys Pro Ser He His 595 600 605 Leu Lys Asp Glu Asn Thr Gly Tyr He His Tyr Glu Asp Thr Asn Asn 610 615 620 Asn Leu Glu Asp Tyr Gin Thr He Asn Lys Arg Phe Thr Thr Gly Thr 625 630 635 640 Asp Leu Lys Gly Val Tyr Leu He Leu Lys Ser Gin Asn Gly Asp Glu 645 650 655 Ala Trp Gly Asp Asn Phe He He Leu Glu He Ser Pro Ser Glu Lys 660 665 670 Leu Leu Ser Pro Glu Leu He Asn Thr Asn Asn Trp Thr Ser Thr Gly 675 680 685 Ser Thr Asn He Ser Gly Asn Thr Leu Thr Leu Tyr Gin Gly Gly Arg 690 695 700 Gly He Leu Lys Gin Asn Leu Gin Leu Asp Ser Phe Ser Thr Tyr Arg 705 710 715 720 Val Tyr Phe Ser Val Ser Gly Asp Ala Asn Val Arg He Arg Asn Ser 725 730 735 Arg Glu Val Leu Phe Glu Lys Arg Tyr Met Ser Gly Ala Lys Asp Val 740 745 750 Ser Glu Met Phe Thr Thr Lys Phe Glu Lys Asp Asn Hie Tyr He Glu 755 760 765 Leu Ser Gin Gly Asn Asn Leu Tyr Gly Gly Pro He Val His Phe Tyr 770 775 780 Asp Val Ser He Lys Xaa Asp Arg Asp Leu He Leu Thr Val Phe Lys 785 790 795 800 Ser Xaa Phe Leu Tyr Asn Val Leu Asp 805 (2) INFORMATION FOR SEQ ID NO: 53: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3474 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (iii) HYPOTHETICAL: YES (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Pure maize optimized synthetic BT CryΙA(b) gene (xi) SEQUENCE DESCRIPTION: SEQ ID NO:53: ATGGACAACA ACCCCAACAT CAACGAGTGC ATCCCCTACA ACTGCCTGAG CAACCCCGAG 60 GTGGAGGTGC TGGGCGGCGA GCGCATCGAG ACCGGCTACA CCCCCATCGA CATCAGCCTG 120 AGCCTGACCC AGTTCCTGCT GAGCGAGTTC GTGCCCGGCG CCGGCTTCGT GCTGGGCCTG 180 GTGGACATCA TCTGGGGCAT CTTCGGCCCC AGCCAGTGGG ACGCCTTCCT GGTGCAGATC 240 GAGCAGCTGA TCAACCAGCG CATCGAGGAG TTCGCCCGCA ACCAGGCCAT CAGCCGCCTG 300 GAGGGCCTGA GCAACCTGTA CCAGATCTAC GCCGAGAGCT TCCGCGAGTG GGAGGCCGAC 360 CCCACCAACC CCGCCCTGCG CGAGGAGATG CGCATCCAGT TCAACGACAT GAACAGCGCC 420 CTGACCACCG CCATCCCCCT GTTCGCCGTG CAGAACTACC AGGTGCCCCT GCTGAGCGTG 480 TACGTGCAGG CCGCCAACCT GCACCTGAGC GTGCTGCGCG ACGTGAGCGT GTTCGGCCAG 540 CGCTGGGGCT TCGACGCCGC CACCATCAAC AGCCGCTACA ACGACCTGAC CCGCCTGATC 600 GGCAACTACA CCGACCACGC CGTGCGCTGG TACAACACCG GCCTGGAGCG CGTGTGGGGC 660 CCCGACAGCC GCGACTGGAT CCGCTACAAC CAGTTCCGCC GCGAGCTGAC CCTGACCGTG 720 CTGGACATCG TGAGCCTGTT CCCCAACTAC GACAGCCGCA CCTACCCCAT CCGCACCGTG 780 AGCCAGCTGA CCCGCGAGAT CTACACCAAC CCCGTGCTGG AGAACTTCGA CGGCAGCTTC 840 CGCGGCAGCG CCCAGGGCAT CGAGGGCAGC ATCCGCAGCC CCCACCTGAT GGACATCCTG 900 AACAGCATCA CCATCTACAC CGACGCCCAC CGCGGCGAGT ACTACTGGAG CGGCCACCAG 960 ATCATGGCCA GCCCCGTGGG CTTCAGCGGC CCCGAGTTCA CCTTCCCCCT GTACGGCACC 1020 ATGGGCAACG CCGCCCCCCA GCAGCGCATC GTGGCCCAGC TGGGCCAGGG CGTGTACCGC 1080 ACCCTGAGCA GCACCCTGTA CCGCCGCCCC TTCAACATCG GCATCAACAA CCAGCAGCTG 1140 AGCGTGCTGG ACGGCACCGA GTTCGCCTAC GGCACCAGCA GCAACCTGCC CAGCGCCGTG 1200 TACCGCAAGA GCGGCACCGT GGACAGCCTG GACGAGATCC CCCCCCAGAA CAACAACGTG 1260 CCCCCCCGCC AGGGCTTCAG CCACCGCCTG AGCCACGTGA GCATGTTCCG CAGCGGCTTC 1320 AGCAACAGCA GCGTGAGCAT CATCCGCGCC CCCATGTTCA GCTGGATCCA CCGCAGCGCC 1380 GAGTTCAACA ACATCATCCC CAGCAGCCAG ATCACCCAGA TCCCCCTGAC CAAGAGCACC 1440 AACCTGGGCA GCGGCACCAG CGTGGTGAAG GGCCCCGGCT TCACCGGCGG CGACATCCTG 1500 CGCCGCACCA GCCCCGGCCA GATCAGCACC CTGCGCGTGA ACATCACCGC CCCCCTGAGC 1560 CAGCGCTACC GCGTGCGCAT CCGCTACGCC AGCACCACCA ACCTGCAGTT CCACACCAGC 1620 ATCGACGGCC GCCCCATCAA CCAGGGCAAC TTCAGCGCCA CCATGAGCAG CGGCAGCAAC 1680 CTGCAGAGCG GCAGCTTCCG CACCGTGGGC TTCACCACCC CCTTCAACTT CAGCAACGGC 1740 AGCAGCGTGT TCACCCTGAG CGCCCACGTG TTCAACAGCG GCAACGAGGT GTACATCGAC 1800 CGCATCGAGT TCGTGCCCGC CGAGGTGACC TTCGAGGCCG AGTACGACCT GGAGCGCGCC 1860 CAGAAGGCCG TGAACGAGCT GTTCACCAGC AGCAACCAGA TCGGCCTGAA GACCGACGTG 1920 ACCGACTACC ACATCGACCA GGTGAGCAAC CTGGTGGAGT GCCTGAGCGA CGAGTTCTGC 1980 CTGGACGAGA AGAAGGAGCT GAGCGAGAAG GTGAAGCACG CCAAGCGCCT GAGCGACGAG 2040 CGCAACCTGC TGCAGGACCC CAACTTCCGC GGCATCAACC GCCAGCTGGA CCGCGGCTGG 2100 CGCGGCAGCA CCGACATCAC CATCCAGGGC GGCGACGACG TGTTCAAGGA GAACTACGTG 2160 ACCCTGCTGG GCACCTTCGA CGAGTGCTAC CCCACCTACC TGTACCAGAA GATCGACGAG 2220 AGCAAGCTGA AGGCCTACAC CCGCTACCAG CTGCGCGGCT ACATCGAGGA CAGCCAGGAC 2280 CTGGAGATCT ACCTGATCCG CTACAACGCC AAGCACGAGA CCGTGAACGT GCCCGGCACC 2340 GGCAGCCTGT GGCCCCTGAG CGCCCCCAGC CCCATCGGCA AGTGCGCCCA CCACAGCCAC 2400 CACTTCAGCC TGGACATCGA CGTGGGCTGC ACCGACCTGA ACGAGGACCT GGGCGTGTGG 2460 GTGATCTTCA AGATCAAGAC CCAGGACGGC CACGCCCGCC TGGGCAACCT GGAGTTCCTG 2520 GAGGAGAAGC CCCTGGTGGG CGAGGCCCTG GCCCGCGTGA AGCGCGCCGA GAAGAAGTGG 2580 CGCGACAAGC GCGAGAAGCT GGAGTGGGAG ACCAACATCG TGTACAAGGA GGCCAAGGAG 2640 AGCGTGGACG CCCTGTTCGT GAACAGCCAG TACGACCGCC TGCAGGCCGA CACCAACATC 2700 GCCATGATCC ACGCCGCCGA CAAGCGCGTG CACAGCATCC GCGAGGCCTA CCTGCCCGAG 2760 CTGAGCGTGA TCCCCGGCGT GAACGCCGCC ATCTTCGAGG AGCTGGAGGG CCGCATCTTC 2820 ACCGCCTTCA GCCTGTACGA CGCCCGCAAC GTGATCAAGA ACGGCGACTT CAACAACGGC 2880 CTGAGCTGCT GGAACGTGAA GGGCCACGTG GACGTGGAGG AGCAGAACAA CCACCGCAGC 2940 GTGCTGGTGG TGCCCGAGTG GGAGGCCGAG GTGAGCCAGG AGGTGCGCGT GTGCCCCGGC 3000 CGCGGCTACA TCCTGCGCGT GACCGCCTAC AAGGAGGGCT ACGGCGAGGG CTGCGTGACC 3060 ATCCACGAGA TCGAGAACAA CACCGACGAG CTGAAGTTCA GCAACTGCGT GGAGGAGGAG 3120 GTGTACCCCA ACAACACCGT GACCTGCAAC GACTACACCG CCACCCAGGA GGAGTACGAG 3180 GGCACCTACA CCAGCCGCAA CCGCGGCTAC GACGGCGCCT ACGAGAGCAA CAGCAGCGTG 3240 CCCGCCGACT ACGCCAGCGC CTACGAGGAG AAGGCCTACA CCGACGGCCG CCGCGACAAC 3300 CCCTGCGAGA GCAACCGCGG CTACGGCGAC TACACCCCCC TGCCCGCCGG CTACGTGACC 3360 AAGGAGCTGG AGTACTTCCC CGAGACCGAC AAGGTGTGGA TCGAGATCGG CGAGACCGAG 3420 GGCACCTTCA TCGTGGACAG CGTGGAGCTG CTGCTGATGG AGGAGTAGTA CATG 3474 (2) INFORMATION FOR SEQ ID NO:54: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3508 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Full length synthetic maize optimized BT CryΙA(b) gene (xi) SEQUENCE DESCRIPTION: SEQ ID NO:54: GATCCAACAA TGGACAACAA CCCCAACATC AACGAGTGCA TCCCCTACAA CTGCCTGAGC 60 AACCCCGAGG TGGAGGTGCT GGGCGGCGAG CGCATCGAGA CCGGCTACAC CCCCATCGAC 120 ATCAGCCTGA GCCTGACCCA GTTCCTGCTG AGCGAGTTCG TGCCCGGCGC CGGCTTCGTG 180 CTGGGCCTGG TGGACATCAT CTGGGGCATC TTCGGCCCCA GCCAGTGGGA CGCCTTCCTG 240 GTGCAGATCG AGCAGCTGAT CAACCAGCGC ATCGAGGAGT TCGCCCGCAA CCAGGCCATC 300 AGCCGCCTGG AGGGCCTGAG CAACCTGTAC CAAATCTACG CCGAGAGCTT CCGCGAGTGG 360 GAGGCCGACC CCACCAACCC CGCCCTGCGC GAGGAGATGC GCATCCAGTT CAACGACATG 420 AACAGCGCCC TGACCACCGC CATCCCCCTG TTCGCCGTGC AGAACTACCA GGTGCCCCTG 480 CTGAGCGTGT ACGTGCAGGC CGCCAACCTG CACCTGAGCG TGCTGCGCGA CGTCAGCGTG 540 TTCGGCCAGC GCTGGGGCTT CGACGCCGCC ACCATCAACA GCCGCTACAA CGACCTGACC 600 CGCCTGATCG GCAACTACAC CGACCACGCC GTGCGCTGGT ACAACACCGG CCTGGAGCGC 660 GTGTGGGGTC CCGACAGCCG CGACTGGATC AGGTACAACC AGTTCCGCCG CGAGCTGACC 720 CTGACCGTGC TGGACATCGT GAGCCTGTTC CCCAACTACG ACAGCCGCAC CTACCCCATC 780 CGCACCGTGA GCCAGCTGAC CCGCGAGATT TACACCAACC CCGTGCTGGA GAACTTCGAC 840 GGCAGCTTCC GCGGCAGCGC CCAGGGCATC GAGGGCAGCA TCCGCAGCCC CCACCTGATG 900 GACATCCTGA ACAGCATCAC CATCTACACC GACGCCCACC GCGGCGAGTA CTACTGGAGC 960 GGCCACCAGA TCATGGCCAG CCCCGTCGGC TTCAGCGGCC CCGAGTTCAC CTTCCCCCTG 1020 TACGGCACCA TGGGCAACGC TGCACCTCAG CAGCGCATCG TGGCACAGCT GGGCCAGGGA 1080 GTGTACCGCA CCCTGAGCAG CACCCTGTAC CGTCGACCTT TCAACATCGG CATCAACAAC 1140 CAGCAGCTGA GCGTGCTGGA CGGCACCGAG TTCGCCTACG GCACCAGCAG CAACCTGCCC 1200 AGCGCCGTGT ACCGCAAGAG CGGCACCGTG GACAGCCTGG ACGAGATCCC CCCTCAGAAC 1260 AACAACGTGC CACCTCGACA GGGCTTCAGC CACCGTCTGA GCCACGTGAG CATGTTCCGC 1320 AGTGGCTTCA GCAACAGCAG CGTGAGCATC ATCCGTGCAC CTATGTTCAG CTGGATTCAC 1380 CGCAGTGCCG AGTTCAACAA CATCATCCCC AGCAGCCAGA TCACCCAGAT CCCCCTGACC 1440 AAGAGCACCA ACCTGGGCAG CGGCACCAGC GTGGTGAAGG GCCCCGGCTT CACCGGCGGC 1500 GACATCCTGC GCCGCACCAG CCCCGGCCAG ATCAGCACCC TGCGCGTGAA CATCACCGCC 1560 CCCCTGAGCC AGCGCTACCG CGTCCGCATC CGCTACGCCA GCACCACCAA CCTGCAGTTC 1620 CACACCAGCA TCGACGGCCG CCCCATCAAC CAGGGCAACT TCAGCGCCAC CATGAGCAGC 1680 GGCAGCAACC TGCAGAGCGG CAGCTTCCGC ACCGTGGGCT TCACCACCCC CTTCAACTTC 1740 AGCAACGGCA GCAGCGTGTT CACCCTGAGC GCCCACGTGT TCAACAGCGG CAACGAGGTG 1800 TACATCGACC GCATCGAGTT CGTGCCCGCC GAGGTGACCT TCGAGGCCGA GTACGACCTG 1860 GAGAGGGCTC AGAAGGCCGT GAACGAGCTG TTCACCAGCA GCAACCAGAT CGGCCTGAAG 1920 ACCGACGTGA CCGACTACCA CATCGATCAG GTGAGCAACC TGGTGGAGTG CCTGAGCGAC 1980 GAGTTCTGCC TGGACGAGAA GAAGGAGCTG AGCGAGAAGG TGAAGCACGC CAAGCGCCTG 2040 AGCGACGAGC GCAACCTGCT GCAGGACCCC AACTTCCGCG GCATCAACCG CCAGCTGGAC 2100 CGCGGCTGGC GCGGCAGCAC CGACATCACC ATCCAGGGCG GCGACGACGT GTTCAAGGAG 2160 AACTACGTGA CCCTGCTGGG CACCTTCGAC GAGTGCTACC CCACCTACCT GTACCAGAAG 2220 ATCGACGAGA GCAAGCTGAA GGCCTACACC CGCTACCAGC TGCGCGGCTA CATCGAGGAC 2280 AGCCAGGACC TGGAGATCTA CCTGATCCGC TACAACGCCA AGCACGAGAC CGTGAACGTG 2340 CCCGGCACCG GCAGCCTGTG GCCCCTGAGC GCCCCCAGCC CCATCGGCAA GTGCGCCCAC 2400 CACAGCCACC ACTTCAGCCT GGACATCGAC GTGGGCTGCA CCGACCTGAA CGAGGACCTG 2460 GGCGTGTGGG TGATCTTCAA GATCAAGACC CAGGACGGCC ACGCCCGCCT GGGCAACCTG 2520 GAGTTCCTGG AGGAGAAGCC CCTGGTGGGC GAGGCCCTGG CCCGCGTGAA GCGCGCCGAG 2580 AAGAAGTGGC GCGACAAGCG CGAGAAGCTG GAGTGGGAGA CCAACATCGT GTACAAGGAG 2640 GCCAAGGAGA GCGTGGACGC CCTGTTCGTG AACAGCCAGT ACGACCGCCT GCAGGCCGAC 2700 ACCAACATCG CCATGATCCA CGCCGCCGAC AAGCGCGTGC ACAGCATTCG CGAGGCCTAC 2760 CTGCCCGAGC TGAGCGTGAT CCCCGGCGTG AACGCCGCCA TCTTCGAGGA GCTGGAGGGC 2820 CGCATCTTCA CCGCCTTCAG CCTGTACGAC GCCCGCAACG TGATCAAGAA CGGCGACTTC 2880 AACAACGGCC TGAGCTGCTG GAACGTGAAG GGCCACGTGG ACGTGGAGGA GCAGAACAAC 2940 CACCGCAGCG TGCTGGTGGT GCCCGAGTGG GAGGCCGAGG TGAGCCAGGA GGTGCGCGTG 3000 TGCCCCGGCC GCGGCTACAT CCTGCGCGTG ACCGCCTACA AGGAGGGCTA CGGCGAGGGC 3060 TGCGTGACCA TCCACGAGAT CGAGAACAAC ACCGACGAGC TCAAGTTCAG CAACTGCGTG 3120 GAGGAGGAGG TGTACCCCAA CAACACCGTG ACCTGCAACG ACTACACCGC CACCCAGGAG 3180 GAGTACGAGG GCACCTACAC CAGCCGCAAC CGCGGCTACG ACGGCGCCTA CGAGAGCAAC 3240 AGCAGCGTGC CCGCCGACTA CGCCAGCGCC TACGAGGAGA AGGCCTACAC CGACGGCCGC 3300 CGCGACAACC CCTGCGAGAG CAACCGCGGC TACGGCGACT ACACCCCCCT GCCCGCCGGC 3360 TACGTGACCA AGGAGCTGGA GTACTTCCCC GAGACCGACA AGGTGTGGAT CGAGATCGGC 3420 GAGACCGAGG GCACCTTCAT CGTGGACAGC GTGGAGCTGC TGCTGATGGA GGAGTAGTAC 3480 ATGTGATAGT ACGTAAGCTC GAGGATCT 3508 (2) INFORMATION FOR SEQ ID NO:55: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1961 base pairs (B) TYPE: nucleic acid (C) STRANDEENESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: ENA (iii) HYPOTHETICAL: NO ( iv) ANTI-SENSE: NO (vi ) ORIGINAL SOURCE: (A) ORGANISM: Truncated synthetic maize optimized BT CryΙA (b) gene (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 55 : GATCCAACAA TGGACAACAA CCCCAACATC AACGAGTGCA TCCCCTACAA CTGCCTGAGC 60 AADCCCGAGG TGGAGGTGCT GGGCGGCGAG CGCATCGAGA CXX-GCTACAC CCCCATCGAC 120 ATCAGCCTGA GCCTGACCCA GTTCCTGCTG AGCGAGTTOG TGCCCGGCGC CGGCTTCGTG 180 CTQGGCCTGG TGGACATCAT CTGGGGCATC TTCGGCCCCA GCCAGTGGGA CGCX-TTCCTG 240 σiGCAGATCG AGCAGCTGAT CAACCAGCGC ATCGAGGAGT TCGCCCGCAA CCAGGCCATC 300 AGCCGCCTGG AGGGCCTGAG CAACCTGTAC CAAATCTACG <_>D3AGAGCTT C.CGCGAGTGG 360 GAGGCCGACC CCACCAACCC CGCCCTGCGC GAGGAGATGC GCATCCAGTT CAACGACATG 420 AAl-AGCGCCC TGACCACCGC CATCCCCCTG TICGCCGTGC AGAACTACCA QGTGCCCCTG 480 CTGAGCGTCT ACGTGCAQGC C>3CCAACCTG CACCTGAQOG TGCTGCGCGA CGTC.AGCGTG 540 TTCGGCCAGC GCTGGGGCTT CGACGCCGCC ACCATCAACA GCCGCTACAA CGACCTGACC 600 CGCCTGATCG GCAACTACAC CGACCACGCC GTGCGCTGCT ACAACACCGG CCTGGAGCGC 660 GTGTGGGGTC CCGACAGCCG CGACTGGATC AGCTACAACC AGTTCCGCCG OGAGCTGACC 720 CTGACCGTGC TGGACATCGT GAGCCTGTTC CCCAACTACG ACACCCGCAC CTACCCCATC 780 CGCACCGTGA GCCAGCTGAC CCGCGAGATT TACACCAACC CCGTGCTGGA GAACTTCGAC 840 GGCAGCTTCC GCGGCAGCGC CCAGGGCATC GAGGGCAGCA TCCGCAGCCC CCACCTGATG 900 GACATCCTGA ACAGCATCAC CATCTACACC CΑCGCCCACC GCGGCGAGTA CTACTGGAGC 960 GGCCACCAGA TCATGGCCAG CCCCGTCGGC TTCAGCGGCC CCGAGTTCAC CTTCCCCCTG 1020 TACGGCACCA TGGGCAACGC TGCACCTCAG CAGCGCATCG TGGCACAGCT GGGCCAGGGA 1080 GTGTACCGCA CCCTGAGCAG CACCCTGTAC CGTCGACCTT TCAACATCGG CATCAACAAC 1140 CAGCAGCTGA GCGTGCTGGA CGGCACCGAG TTCGCCTACG GCACCAGCAG CAACCTGCCC 1200 AGCGCCGTGT ACCGCAAGAG CGGCACCGTG GACAGCCTGG ACGAGATCCC CCCTCAGAAC 1260 AACAACGTGC CACCTCGACA GGGCTTCAGC CACCGTCTGA GCCACGTGAG CATGTTCCGC 1320 AGTGGCTTCA GCAACAGCAG CGTGAGCATC ATCCGTGCAC CTATGTTCAG CTGGATTCAC 1380 CGCAGTGCCG AGTTCAACAA CATCATCCCC AGCAGCCAGA TCACCCAGAT CCX_CCTGACC 1440 AAGAGCACCA ACCTGGGCAG CGGCACCAGC GIGGTGAAGG CXX-CCGGCTT CACCGGCGGC 1500 GACATCCTGC GCCGCACCAG CXXCGGCCAG ATCAGCACCC TGCGCGTGAA CATCACCGCC 1560 CCCCTGAGCC AGCGCTACCG CGTCCGCATC ∞CTACGCCA GCACCACCAA <_X_TGCAGTTC 1620 CACACCAGCA TCGACGGCCG CCCCATCAAC CAGGGCAACT TCAGCGCCAC CATGAGCAGC 1680 GGCAGCAACC TGCAGAGCGG CAGCTTCCGC ACCGTGGGCT TCACCACCCC CTTCAACTTC 1740 AGCAACGGCA GCAGCGTGTT ( .ACCCTGAGC GCCCACGTGT TCAACAGCGG CAACGAGGTG 1800 TACATCGACC GCATCGAGTT CGTGCCCGCC GAGGTGACCT TCGAGGCCGA GTACGACCTG 1860 GAGAGGGCTC AGAAGGCCGT GAACGAGCTG TTCACCAGCA GCAACCAGAT CGGCCTGAAG 1920 ACCGACGTGA CCGACTACCA CATCGATCAG GTGTAGGAGC T 1961 INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13t)ts) A. The indications made below relate to the microorganism referred to in the description on page ^0 > ij ne 23-26 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet [ | Name of depositary institution Agricultural Research Service Culture Collection (NRRL) Address of depositary institution (including postal code and country) 1815 North University Street Peoria, XL 61604 USA Date of deposit Accession Number 21 September 1992 (21.09.92) NRRL B-18998 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet | | We request the Expert Solution where available D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature ofthe indications eg., "Accession Number of Deposit") For receiving Office use only For International Bureau use only I j This sheet was received with the international application I j This sheet was received by the International Bureau on: Authorized officer Authorized officer Form PCT/RO/134 (July 1992) ■

Claims: Claims: 1. Method for protecting plants including the progeny thereof against damage caused by Sesamia species comprising directly or indirectly applying to the plant or the plant seed or to the growing area of the plant a toxin protein of a Bacillus species as the active ingredient. 2. A method according to claim 1 , wherein the toxin protein is a toxin protein of Bacillus thuringiensis. 3. A method according to claim 1 , wherein the toxin protein is a toxin protein of Bacillus cereus. 4. A method according to claim 1 , wherein the toxin protein is a Cry-type protein, preferably a Cryl-type protein, more preferably a CrylA-type protein, and most preferably a CrylA(b) protein. 5. A method according to anyone of claim's 4 or 5, wherein the toxin protein is a Cryl- type protein according to SEQ ID Nos. 53 to 55. 6. A method according to claim 1 , wherein the toxin protein is a VIP-type protein, preferably a VIP1-type protein, such as a VIP1A(a) protein or a VIP1A(b) protein, or a VIP2- type protein, such as a VIP2A(a) protein or a VIP2A(b) protein or a combination of a VIP1- type protein and a VIP2-type protein. 7. A method according to claim 1 , wherein the toxin protein is a VIP3-type protein, such as a VIP3A(a) protein or a VIP3A(b) protein. 8. A method according to anyone of claims 7-10, wherein the toxin protein is a VIP-type protein according to SEQ ID Nos. 1 , 2, 4-7, 17-24, 26-32, 35, 36, 39, 40, 42, 43, 45, 46, 49, 50, 51 or 52. 9. A method according to claim 1 , wherein the toxin protein is applied to the plant in form of an entomocidal composition. 10. A method according to claim 9, wherein the entomocidal composition comprises at least one Cryl-type toxin protein and/or a VIP-type protein or a microorganism, but especially a Bacillus thuringiensis and/or a Bacillus cereus strain, containing at least one toxin gene encoding the said toxin protein together with a suitable carrier. 11. A method according to claim 9, wherein the microorganism is a naturally-occurring organism containing at least one cry-type toxin gene, preferably a cryl-type toxin gene, more preferably a crylA-type toxin gene, and most preferably a crylA(b) toxin gene. 12. A method according to claim 9, wherein the microorganism is a recombinant organism containing at least one cry-type toxin gene, preferably a cryl-type toxin gene, more preferably a crylA-type toxin gene, and most preferably a crylA(b) toxin gene. 13. A method according to claim 9, wherein the microorganism is a naturally-occurring organism containing at least one VIP-type protein gene encoding the said toxin protein, preferably a VIP1 A(a) protein or a VIP1 A(b) protein gene or a VIP2-type protein gene such as as a VIP2A(a) protein or a VIP2A(b) protein gene. 14. A method according to claim 9, wherein the microorganism is a naturally-occurring organism containing at least one VIP3-type protein gene such as as a VIP3A(a) protein or a VIP3A(b) protein gene encoding the said toxin protein. 15. A method according to anyone of claims 13-14, wherein the toxin protein is a VIP-type protein according to SEQ ID Nos.1 , 2, 4-7, 17-24, 26-32, 35, 36, 39, 40, 42, 43, 45, 46, 49, 50, 51 or 52. 16. A method according to anyone of claims 10-12, wherein the toxin protein is a Cry-type protein according to SEQ ID Nos. 53 to 55. 17. Anyone of claims 13 to 16, wherein the microorganism is a recombinant organism. 18. A method according to any one of claims 1 to 17, wherein the toxin protein is indirectly applied to the plant, by expressing within the said plant and the progeny therof a toxin gene encoding a toxin protein of Bacillus species to produce the said toxin protein in an amount sufficient to provide control against Sesamia species upon planting the so transformed plant within an area where the said insect pest may occur. 19. A method according to claim 18, wherein the toxin gene encodes a toxin protein of Bacillus thuringiensis or Bacillus cereus. 20. A method according to claim 18, wherein the toxin gene encodes a Cry-type toxin protein, preferably a Cryl-type protein, more preferably a CrylA-type protein, and most preferably a CrylA(b) protein such as those provided in SEQ ID Nos. 53 to 55. 21. A method according to claim 18, wherein the toxin gene encodes a VIP-type toxin protein, preferably a VIP1-type protein, such as a VIP1 A(a) protein or a VIP1A(b) protein or a VIP2-type protein, such as a VIP2A(a) protein or a VIP2A(b) protein. 22. A method according to claim 18, wherein the toxin gene encodes a VIP3-type protein, such as as a VIP3A(a) protein or a VIP3A(b) protein. 23. A method according to anyone of claims 18-22, wherein the toxin gene is a synthetic gene the codon usage of which is optimized by using the codons which are most preferred in plants. 24. A method according to any one of claims 21 to 23, wherein the toxin gene encodes a VIP-type protein according to SEQ ID Nos.1 , 2, 4-7, 17-24, 26-32, 35, 36, 39, 40, 42, 43, 45, 46, 49, 50, 51 or 52. 25. A method according to any one of claims 1 to 24, wherein the plant to be protected is a cereal plant. 26. A method according to claim 25, wherein the plant to be protected is a maize plant. 27. A method accroding to any one of claims 18 to 26, wherein at least a Cry-tpye toxin protein is expressed in the plant to be protected in combination with a VIP-type toxin protein in an amount sufficient to provide control against Sesamia pests. 28. A composition comprising as an active ingredient at least a Cry-type toxin protein and a VIP-type protein in a insecticidally effective amount together with a agronomically acceptable carrier. 29. Use of an active ingredient as defined in the previous claims for controlling Sesamia pests in crop plants. 30. Use of a composition according to claim 28 for controlling Sesamia pests in crop plants. 31. Use of a transgenic plant as defined in claim 18 for controlling Sesamia pests in crop plants. 32 Use of recombinant microorganisms or transgenic plants according to anyone of claims 18 to 24 comprising a DNA molecule which hybridizes to a cry-type or a VIP-type gene encoding the respective toxin protein under moderate stringent conditions for controlling Sesamia pests in crop plants. 33. A commercial bag comprising seed of a transgenic plant or a microorganism, but especially a Bacillus thuringiensis and/or a Bacillus cereus strain, comprising at least a toxin gene encoding a toxin protein as defined previously in claims 1 to 24 and 32, and expressing the said toxin protein in an amount sufficient to provide control against Sesamia species, together with lable instructions for the use thereof for control of Sesamia pests in crop plants. 34. A commercial bag comprising seed of a transgenic plant comprising at least a Cryl-type toxin protein and/or a VIP-type protein as defined herein before or a microorganism, but especially a Bacillus thuringiensis and/or a Bacillus cereus strain, containing at least a Cryl- type toxin protein and/or a VIP-type protein as defined herein before together with a suitable carrier in an amount sufficient to provide control against Sesamia species, together with lable instructions for the use thereof for control of Sesamia pests in crop plants. 35. A commercial bag comprising an insecticidal composition according to claim 28 together with lable instructions for the use thereof for control of Sesamia pests in crop plants. 36. An agricultural method, wherein a transgenic plant or the progeny thereof is used comprising a toxin gene encoding a toxin protein of a Bacillus species and expressing the said toxin protein in an amount sufficient to provide control against Sesamia species or transgenic seed thereof, as defined in anyone of claims 18 to 27. 37. The invention is thus further directed to an agricultural method for protecting plants against damage caused by Sesamia species comprising a combination of steps (2) and (3) with any one of steps (1 ) or (4): (1) control of diapause population by mechanical grinding of the plant residues after harvest (2) control of the first generation of Sesamia species by one of the methods according to anyone of claims 1-27, or 36. (3) control of the second generation of Sesamia species by one of the methods according to anyone of claims 1-27 or 36. (4) control of the diapause population, the first and/or the second generation by treating them with a commonly applied insecticide. 38. An agricultural method according to claim 37 wherein a composition according to claim 28 is used in Step (2) or (3). 39. A transgenic plant expressing at least a Cryl-type toxin protein in combination with at least a VIP-type protein as defined herein before in an amount sufficient to provide control against Sesamia pests. 40. A transgenic plant according to claim 39,wherein the Cry-type protein is a CrylA(b) toxin protein. 41. A transgenic plant according to claims 39 and 40 which is a maize plant.

Inventors: GAY PHILIPPE BERNARD, GAY, PHILIPPE, BERNARD
Applicants: CIBA GEIGY AG, GAY PHILIPPE BERNARD, GAY, PHILIPPE, BERNARD, NOVARTIS AG
Application year: 1996
Main classification: C12N15
IPC codes: A01N63, C07K14, C12N15