TOXIN-ACTIVE PESTICIDE PROTEINS AGAINST LEPIDOPTERA INSECTS

Abstract

The present invention relates to a polynucleotide construct characterized in that it comprises a nucleotide sequence encoding: an insecticidal protein having at least 95% identity with an amino acid sequence comprising amino acids 1 to 607 of SEQ ID NO: 8, wherein said nucleotide sequence is operatively linked to a heterologous promoter sequence.

Description

TOXIN PROTEINS PESTICIDES ACTIVE AGAINST LEPIDOPTERA INSECTS REFERENCE TO RELATED APPLICATION This application claims the benefit of U.S. Provisional Application No. 62 / 445.313, filed on January 12, 2017, which is incorporated herein by reference in its entirety. Incorporation of the Sequence List This document provides a computer-readable version of the sequence list, which is contained in the file named 38-21-51791-0001_BCW_Sequences_ST25.txt, created on December 5, 2017. This file is 166,730 bytes in size, as measured in MS-DOS, and is incorporated herein by reference in its entirety. This sequence list consists of SEQ ID NO; 1- SEQ ID NO: 12. FIELD OF INVENTION The invention relates in general terms to the field of insect-inhibiting proteins, in particular to proteins exhibiting insect-inhibiting activity against agriculturally relevant lepidopteran pests of plants and seeds, particularly lepidopteran pests such as the black cutworm (BCW, black cutworm, Agrotis ipsilon). BACKGROUND OF THE INVENTION Insect-inhibiting proteins produced by Bacillus thuringiensis (Bt) bacterial species are known in the art. Certain Bt proteins can be used to control agricultural pests of crop plants by spraying agriculturally acceptable formulations containing one or more of these proteins onto the plants, coating seeds with a composition formulated to contain an insecticidal amount of these proteins, or by expressing the effective output of one or more proteins in plants / seeds. Only a few Bt proteins have been developed for use as transgenic traits for commercial use by farmers to control insect pests. Farmers rely on these proteins to provide a prescribed spectrum of pest control and may continue to depend on broad-spectrum chemicals applied to foliage and soil to control pests. Certain lepidopteran insects, such as Agrotis and Striacosta species, have proven particularly difficult to control using currently used transgenic insecticidal traits, including CrylAb, CrylAc, CrylFa, Cry2Ab, and Cry2Ae. A / a / ZUZ l / UI 14 IU VIP3Aa, and several other Bt toxins that have been used less frequently. Therefore, there is a need for insect-inhibiting proteins that exhibit activity against a broader spectrum of insect pest species, and for use in toxins to overcome the development of pests resistant to existing pesticides, including toxins currently used in pest management systems. This application describes a novel family of chimeric toxin protein variants and protein constructs, each exhibiting surprisingly effective insecticidal activity against lepidoptera, particularly against pests of Agrotis species, such as the Black Cutworm. BRIEF DESCRIPTION OF THE INVENTION A novel group of insect-inhibiting polypeptides (toxin proteins BCW 001, BCW 002, and BCW 003 and their pesticide fragments) have demonstrated inhibitory activity against several lepidopteran pests of crop plants, particularly black cutworm species (Agrotis). Each protein can be used alone or in combination with others and with other Bt proteins and insect-inhibiting agents in formulations and in-plant applications, thus providing alternatives to Bt proteins and insecticidal chemicals currently used in agricultural systems. The present invention provides polynucleotide constructs containing, in an operable linkage, a heterologous promoter segment linked to a nucleotide sequence encoding an insecticidal protein having CrylA characteristics, having a length that is less than a full length relative to a CrylA class toxin protein, and having the amino acid sequence from approximately position 1 to position 607 as set forth in SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, and SEQ ID NO: 12, or an insecticidal active fragment thereof.The less-than-full length polypeptide exhibiting such insecticidal activity should exhibit at least approximately 100%, 99%, 98%, 97%, 96%, 95%, 94%, 94%, 92%, 91%, or 90% identity with the BCW amino acid sequence 001 as set out in SEQ ID NO: 2 from approximately position 1 to approximately position 606, or from approximately position 5 to approximately position 600.If full-length or considerably larger toxin fragments are to be used, the percent identity should be less stringent and extended to a percent identity of approximately 100, approximately 95, approximately 90, approximately 85, or even 80% identity with respect to the full-length toxin protein sequences as set out in SEQ ID NO: 2, 4, and 6, since these toxin proteins exhibit commercially useful levels of biological activity when tested against black cutworm larvae in biological diet assays, and when tested on maize, cotton, and transgenic soybean plants expressing such proteins. The invention also provides toxic proteins for black cutworm lepidopteran species, including proteins having the amino acid sequence indicated in SEQ ID NO: 2 from position 256 to 606 (a BCW 001 protein), and proteins having the amino acid sequence as set forth in either SEQ ID NO: 4 or SEQ ID NO: 6 from amino acid position 257 to amino acid position 607 (referred to herein as a BCW 002 toxin protein and a BCW 003 toxin protein). It is observed that such insecticidal proteins exhibit activity against selected lepidopteran species from the group consisting of Spodoptera frugiperda, Spodoptera exigua, Spodoptera litura, Mamestra configurata, Striacosta albicosta, Trichoplusia ni, Pseudoplusia includens, Anticarsia gemmatalis, Hypena scabra, Heliothis virescens, Agrotis subterranea, Pseudaletia unipuncta, Agrotis Ípsilon, Agrotis orthogonia, Ostrinia nubilalis, Amyelois transitella, Crambus caliginosellus, Herpetogramma licarsisalis, Homoeosoma electellum, Elasmopalpus lignosellus, Cydia pomonella, Endopiza viteana, Grapholita molesta, Suleima helianthana, Plutella xylostella, Pectinophora gossypiella, Lymantria dispar, / Alabama argillacea, Archips argyrospila, Archips rosana, Chilo suppressalis, Cnaphalocrocis medinalis, Crambus caliginosellus, Crambus teterrellus, Diatraea grandiosella, Diatraea saccharalis, Earias insulana, Egrias vittella, Helicoverpa armígera, Helicoverpa zea, Heliothis virescens,Herpetogramma licarsisalis, Lobesia botrana, Pectinophora gossypiella, Phyllocnistis citrella, Pieris brassicae, Pieris rapae, Plutella xylostella, and Tuta absoluta., The proteins of the present invention may also exhibit biological activity against selected Lepidopteran species from the group consisting of Spodoptera frugiperda, Spodoptera exigua, Spodoptera litura, Mamestra configurata, Striacosta albicosta, Trichoplusia ni, Pseudoplusia includens, Anticarsia gemmatalis, Hypena scabra, Heliothis virescens, Agrotis subterranea, Pseudaletia unipuncta, Agrotis ípsilon, Agrotis orthogonia, Ostrinia nubilalis, Amyelois transitella, Crambus caliginosellus, Herpetogramma licarsisalis, Homoeosoma electellum, Elasmopalpus lignosellus, Cydia pomonella, Endopiza viteana, Grapholita molesta, Suleima helianthana, Plutella xylostella, Pectinophora gossypiella, Lymantria dispar, Alabama argillacea, Archips argyrospila, Archips rosana, Chilo suppressalis, Cnaphalocrocis medinalis, Crambus caliginosellus, Crambus teterrellus, Diatraea grandiosella, Diatraea saccharalis, Earias insulana, Egrias vittella, Helicoverpa armígera, Helicoverpa zea,Heliothis virescens, Herpetogramma licarsisalis, Lobesia botrana, Pectinophora gossypiella, Phyllocnistis citrella, Pieris brassicae, Pieris rapae, Plutella xylostella, and Tuta ABSOLUTA. The proteins of the present invention, and the constructs contemplated in the A / a / zuz ι / ui ιζ iu present, can be included in any vector that includes plasmids, cosmids, bacmids, phage-mediated vectors and the like. Such vectors can be used to introduce the constructs of the present invention into any number of host cells, including bacterial cells, yeast cells, and plant cells. The host cells that are yeast cells can be Saccharomyces cerevisiae or Saccharomyces pombe and similar organisms. The bacterial host cells can be any number of such known host cells, including, but not limited to, E. coli, B. thuringiensis, and other related bacilli.Plant host cells can be obtained from any number of plant species, including, but not limited to, alfalfa, banana, barley, bean, broccoli, cabbage, brassica, carrot, cassava, castor bean, cauliflower, celery, chickpea, bok choy, citrus, coconut, coffee, corn, clover, cotton, cucurbits, cucumber, Douglas fir, eggplant, eucalyptus, flax, garlic, grape, hops, leek, lettuce, Loblolly pine, millet, melon, walnut, oat, olive, onion, ornamental plants, palm, grass, pea, peanut, pepper, pigeon pea, pine, potato, poplar, squash, Radiata pine, radish, rapeseed, rice, roots, rye, safflower, shrub, sorghum, southern pine, soybean, spinach, pumpkin, strawberry, sugar beet, sugarcane, sunflower, sweetcorn, gum chewing gum, sweet potato, switchgrass, tea, tobacco, tomato, triticale, lawn, watermelon, and wheat plants. Transgenic plant events, particularly transgenic plant varieties of maize, cotton, and soybean, can be produced by introducing the constructs hereof containing appropriately modified polynucleotide sequences such as those set forth in SEQ ID NO: 7, SEQ ID NO: 9, and SEQ ID NO: 11, for example, into the genome of said plant cells and recovering a fertile transgenic maize, soybean, or cotton plant comprising in its genome a genetic construct for expressing at least one protein toxin of the present invention, namely a BCW 001, BCW 002, or a BCW 003 protein toxin.Such transgenic plants will have introduced into their plant genome a polynucleotide construct comprising at least one heterologous promoter segment operatively linked to a nucleotide sequence encoding an insecticidal protein BCW 001, BCW 002 or BCW 003 having the amino acid sequence selected from the group consisting of SEQ ID NO: 8, SEQ ID NO: 10, and SEQ ID NO: 12, or an insecticidal protein fragment thereof. The seeds are also considered a feature of the invention, wherein the seeds are produced from such transgenic plants and said seeds contain a detectable amount of the polynucleotide construct introduced into the plant genome. The pollen, seed, progeny plant cells, plant tissue, and commercial products produced from each of such transgenic plants will contain a detectable amount of the polynucleotide construct. Any biological sample containing at least a detectable amount of the polynucleotide construct encoding said protein BCW 001, BCW 002 or BCW 003 shall be within the scope of the invention. The compositions provided are insecticidal and contain an effective amount of the BCW protein 001, 002, or 003 of the present invention, and are intended for the control of lepidopteran pest species. Such compositions may also contain a supplementary agent that is different from the BCW toxin protein. This agent will also be toxic to the same lepidopteran species as the BCW toxin protein. The supplementary agent must be selected from the group of agents consisting of proteins or polypeptides having an amino acid sequence different from that of the BCW protein, and may also be an RNA molecule that confers toxic effects on the target insect pest (such as a dsRNA, a miRNA, or a siRNA), or an insecticidal chemical compound such as a pyrethrin, an organophosphate pesticide, or the like.Alternatively, the supplemental agent may be any Cry protein or related toxin such as another CrylA, CrylAb, CrylAc, CrylA.105, CrylAe, (but these are not preferred as they cannot confer adequate resistance control properties), or CrylB, CrylC, CrylD, CrylE, CrylF, CrylG, CrylH, Cryll, CrylJ, CrylK, CrylL, Cry2A, Cry2Ab, Cry2Ae, Cry4B, Cry6, Cry7, Cry8, Cry9, Cryl5, Cry43A, Cry43B, ET35, ET66, TIC400, TIC800, TIC807, TIC834, TIC853, TIC1415, VIP3A, VIP3Ab, Axmi insecticidal proteins, DIG insecticidal proteins, eHIPs, and VIP proteins. any toxic protein known in the art to confer toxic properties against the larvae of the black cutworm species or applicable against other target pests of Lepidoptera species. Such compositions may also include additional pesticidal agents that are not necessarily toxic to the same target pest, such as additional agents selected from the group consisting of a CryC, a Cry3A, a Cry3B, a Cry34, a Cry35, Cry51Aal, ET29, ET33, ET34, ET70, TIC407, TIC417, TIC431, TIC901, TIC1201, TIC3131, 5307, DIG-10, Axm¡184, Axm¡205 and AxmiRl. Methods for producing seeds that utilize the pesticidal properties of the proteins of the present invention are also contemplated. These methods include a polynucleotide construct engineered to express a BCW 001, BCW 002, or BCW 003 protein, or a protein exhibiting at least approximately 90% identity with such protein. The method comprises planting one or more seeds containing a polynucleotide that expresses one or more of the BCW protein toxins of the present invention, growing plants from such seeds, and then harvesting a crop of such plants. The harvested seeds will contain the polynucleotide construct and will produce plants that are also resistant to infestation by the black cutworm pest. A / a / zuz ι / ui iu Such plants may include corn, cotton, soybeans, or any other plant vulnerable to lepidopteran pest species that have been shown to be controlled by the proteins of the present invention. Such plants are considered to be previously produced transgenic plants that would benefit from the toxic properties of the proteins of the present invention. Maize plants that fall into this category include, without limitation, selected transgenic events from the group consisting of DKB89614-9, MON801, MON802, MON809, MON810, MON863, MON88017, MON89034, event 4114-3, event 5307, DAS59122-7, BtlO, Btll, Btl76, CBH-351, DKB-83614-9, MIR162, MIR604, TC1507, TC6275, event 676, event 678, event 680, event 98140, DAS40278-9, DKB89790-5, MON21-9, HCEM485, MON832, MON87427, NK603, T14, T25 and VCO01981-5.Soybean plants that fall into this category of transgenic plants are selected from the group consisting of MON87751, DAS81419-2, MON87701, A2704-12, A270421, A5547-127, A5547-35, CV127, DAS44406-6, DAS68416-4, DP356043, FG72, MON4032, ACSGM003-1, MON87705, MON87708, MON89788, W62, W98 and GFM CrylA. The transgenic cotton plants that fall into this category are selected from the group consisting of DAS24236-5, DAS21023-5, event 31707, event 31803, event 31807, event 31808, event 42317, BNLA-601, COT102, COT67B, event 1, GHB119, GK12, MON15985, MLS9124, MON1076, MON531, MON757, T303-3, T304^í0, SGK321, event 19-51a, GHB614, LLCotton25, MON88701, MON88702, MON1445, MON1698 and MON88913. Transgenic sugarcane plants that fall into this category include the NXI-1T transgenic sugarcane plant event.In the technique, rice plants are known that would benefit from having a construct that encodes such BCW protein toxins, including selected transgenic rice plant events from the group consisting of LLRICE06, LLRICE601, LLRICE62, GM-A17054 and GM-A17054. In addition, processed plant products comprising a detectable amount of the described recombinant polynucleotides are provided. Such processed products include, but are not limited to, plant biomass, oil, meal, animal feed, flour, flakes, bran, fluff, hulls, and processed seeds. Methods for preparing transgenic plants are also provided. Such methods include introducing recombinant polynucleotide into a plant cell and selecting a transgenic plant that expresses an insect-inhibiting amount of the recombinant polypeptide encoded by the recombinant polynucleotide. Other embodiments, features, and advantages of the invention will become apparent from the following detailed description, examples, and claims. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows an alignment of amino acid sequences of BCW 001 (SEQ A / a / zuz ι / ui ιζ iu ID NO: 2, top line) vs. BCW 002 (SEQ ID NO: 4, middle line), vs. BCW 003 (SEQ ID NO: 6, bottom line)); the asterisks below each triplet line represent differences in the applicable amino acid position in at least one of the three different sequences. BRIEF DESCRIPTION OF THE SEQUENCES SEQ ID NO: 1 is a nucleotide sequence EG4384 from the native B. thuringiensis strain that encodes the anti-Lepidoptera toxic protein BCW 0001. SEQ ID NO: 2 is the amino acid sequence deduced from BCW 001 of the open reading frame / as indicated in SEQ ID NO: 1. The SEQ ID NO: 3 is an artificial sequence that encodes a toxic protein against Lepidoptera BCW 002. SEQ ID NO: 4 is the amino acid sequence deduced from BCW 002 of the open reading frame as indicated in SEQ ID NO: 3, wherein such protein BCW 002 consists of domain I of a CrylAc operatively linked to domains II and III of BCW 001 (amino acid position 258 to amino acid position 606 as indicated in SEQ ID NO: 2) and operatively linked to a protoxin domain CrylAc from amino acid position 608 to 1177 as indicated in SEQ ID NO: 4 and SEQ ID NO: 6. SEQ ID NO: 4 (BCW 002) differs from SEQ ID NO: 6 (BCW 003) only at position 259, BCW 002 containing an isoleucine at this position, BCW 003 containing a threonine as in BCW 001. SEQ ID NO: 5 is an artificial sequence encoding a chimeric Lepidopteran toxic protein BCW 300. SEQ ID NO: 6 is the amino acid sequence deduced from BCW 003 of the open reading frame as indicated in SEQ ID NO: 3, wherein such BCW 003 protein consists of domain I of a CrylAc operatively linked to domains II and III of BCW 001 (amino acid position 258 to amino acid position 606 as indicated in SEQ ID NO: 2) and operatively linked to the CrylAc protoxin domain from amino acid position 608 to amino acid position 1177 as indicated in SEQ ID NO: 4 and in SEQ ID NO: 6. SEQ ID NO: 6 (BCW 003) differs from SEQ ID NO: 4 (BCW 002) only at position 259, BCW 002 containing an isoleucine at this position, BCW 003 containing a threonine as in BCW 001. The SEQ ID NO: 7 is an artificial sequence that encodes a BCW 001 protein for expression in plants. SEQ ID NO: 8 is the amino acid sequence deduced from BCW 001 derived from SEQ ID NO: 7. The SEQ ID NO: 9 is an artificial sequence that encodes the BCW 002 protein for its A / a / zuz ι / ui ιζ iu expression in plants. SEQ ID NO: 10 is the amino acid sequence deduced from BCW 002 derived from SEQ ID NO: 9. SEQ ID NO: 11 is an artificial sequence that encodes the BCW 003 protein for expression in plants. SEQ ID NO: 12 is the amino acid sequence deduced from BCW 003 derived from SEQ ID NO: 11. DETAILED DESCRIPTION OF THE INVENTION An alternative to controlling agricultural pests in crops by spraying formulations containing insecticidal proteins onto the plants / seeds involves inserting the polynucleotides that encode these proteins into the plant's genome for expression in the plant or plant parts. Plants transformed with these polynucleotides exhibit insect resistance, which these expressed proteins confer as transgenic traits. To prevent the development of, or to circumvent, insect resistance to currently used proteins, new proteins with different modes of action (MOAs) and broad-spectrum efficacy for Lepidoptera control are needed. One way to address this need is to sequence Bt genomes in the hope of discovering new insecticidal proteins. Another approach is to exchange segments of various Bt proteins to create new chimeric Bt proteins with insect-inhibiting properties. The likelihood of arbitrarily creating a chimeric protein with enhanced properties by rearranging the domain structures of numerous known native insecticidal crystal proteins is remote (see, for example, "A Strategy for Shuffling Numerous Bacíllus thuringiensis Crystal Protein Domains"; Economic Entomology, 97 (6): 1805-1813. 2004). This paper describes nucleotide sequences encoding insecticidal proteins, identified herein as BCW proteins, that address the need for an alternative MOA, provide activity against a broader spectrum of insect pests, and work in a manner that delays or prevents the development of resistance, particularly for use in the control of Black Cutworm (BCW) pests. BCW 001 was discovered as an open reading frame that predicts an amino acid sequence with characteristics of a CrylA-like protein after sequencing the genome of the EG4384 strain of Bacillus thuringiensis. The BCW 001 open reading frame (ORF) encoded a protein of 1180 amino acids, and the protein was predicted to have many of the characteristics of Cryl protein toxins, including an identifiable domain I structure. A / a / zuz ι / ui iu Domains II and III, and a characteristic CrylA-like protoxin domain in the carboxy-terminal half of the predicted protein. The predicted Domain I amino acid sequence (remains 1 to approximately 258 of SEQ ID NO: 2) shows approximately 67% identity with Domain I of the CrylAc protein toxin. The predicted Domain II amino acid sequence (remains approximately 259 to approximately 459 as indicated in SEQ ID NO: 2) exhibits perfect identity (100%) with Domain II of CrylA12. The predicted Domain III amino acid sequence (remains approximately 260 to approximately 606 as indicated in SEQ ID NO: 2) exhibits approximately 63% identity with the corresponding Domain III remains in CrylAh2.The protoxin domain structure of the predicted protein BCW 001 (approximately residues 607 to 1180 as indicated in SEQ ID NO: 2) exhibits approximately 96% identity with the corresponding residues in CrylAa9. Overall, this full-length predicted protein exhibits approximately 83% amino acid sequence identity with CrylAi, and the predicted toxin region from amino acid positions 1 to approximately residue 607 as indicated in SEQ ID NO: 2 exhibits 76% identity with CrylAil. It is difficult to assign this novel toxin protein to a particular class of CrylA, and therefore, this sequence will be provided to the Bacillus thuringiensis Nomenclature Committee, which will determine whether this protein warrants its own separate and innovative class. The BCW 001 protein was produced from a plasmid vector in a crystalliferous strain of Bacillus thuringiensis, and spore crystal preparations were assayed against a variety of Lepidopteran pests. See Table A, column 2 for the data. Evidence indicated that this protein was not characteristic of any of the proteins from which it is derived, namely the CrylAa, CrylAh, or CrylAi toxin proteins known in the prior art. None of the prior art proteins exhibit appreciable activity when assayed against the Black Cutworm; however, this novel BCW 001 protein was toxic in bioassays against the Black Cutworm and, surprisingly, exhibited activity when also assayed against a range of other Lepidopteran pests, as shown in Table A. TABLE A ni zi iη / ι7Π7 / β / υιλι Insect species BCW 001 BCW 002 BCW 003 A. ipsilon + + + S. albicosta + + + H. zea + + + O. nubilalis + + + D. saccharalis ND ND + D. grandiosella + ND + T. ni + ND + P. includens + ND + S. frugiperda - - - It shows a list of Lepidopteran insect pest species that were tested with the protein toxins BCW 001, BCW 002, and BCW 003. + indicates mortality relative to buffer control; indicates that no significant mortality was observed above the buffer control level; ND indicates that it has not been tested using the applicable protein toxin. BCW 001 exhibited mortality against Agrotis upsilon (Black Cutworm), Striacosta albicostsa (Western Chickpea Cutworm), Helicoverpa zea (Corn Earworm), Ostrinia nubilalis (European Corn Borer), Diatraea grandiosella (Southwestern Corn Borer), Trichoplusia ni (Lettuce Surveyor Caterpillar), and Pseudoplusia indudens (Soybean Looper), and showed no mortality or growth retardation when tested against Spodoptera frugiperda (Fall Armyworm). Diatraea saccharalis (Sugarcane Borer) was not tested with BCW 001.BCW 002 showed mortality against Agrotis ipsilon (Black Cutworm), Striacosta albicostsa (Western Chickpea Cutworm), Helicoverpa zea (Corn Earworm), and Ostrinia nubilalis (European Corn Borer), and showed no mortality or delay against Spodoptera frugiperda (Fall Armyworm), Diatraea saccharalis (Sugarcane Borer), Diatraea grandiosella (Southeastern Corn Borer), Trichoplusia ni (Lettuce Surveyor Caterpillar), and Pseudoplusia includens (Soybean Surveyor Caterpillar) were not tested with BCW 002.BCW 003 showed mortality against Agrotis ipsilon (Black Cutworm), Striacosta albicostsa (Western Chickpea Cutworm), Helicoverpa zea (Corn Earworm), Ostrinia nubilalis (European Corn Borer), Diatraea saccharalis (Sugarcane Borer), Diatraea grandiosella (Southeastern Corn Borer), Trichoplusia ni (Lettuce Surveyor Caterpillar), and Pseudoplusia includens (Soybean Surveyor Caterpillar), and showed no mortality or developmental delay when tested against Spodoptera frugiperda (Fall Armyworm). In particular, in bioassays compared to a diet control of untreated insects, the BCW 001 protein showed activity against the western bean cutworm (WBC), corn earworm (CEW, Helicoverpa zea), European corn borer (ECB, Ostrinia nubilalis), southeastern corn borer (SWC, Diatraea grandiosella), soybean surveyor (SL, Pseudoplusia ineludes), lettuce surveyor (CLW, Trichoplusia ni), and the metamorphosis stages 1a and 3a of the black cutworm (BCW, Agrotis upsilon). As described below, chimeric toxin proteins were produced using Domain I of CrylAc and Domains II and III of BCW 001 (i.e., BCW 002 and BCW 003 as indicated in / ID NO: 4 and / NO: 6, respectively), and these chimeric toxin proteins were introduced into maize and sugarcane plants. Both chimeric proteins exhibited activity in maize against BCW, WBC, CEW, and SWC. BCW 003 exhibited activity against SCB in sugarcane. The term BCW protein, as used herein, refers to any novel insect-inhibiting protein comprising, consisting of, being substantially homologous to, or derived from any insect-inhibiting polypeptide sequence of: BCW 001 (SEQ ID NO: 2), BCW 002 (SEQ ID NO: 4), and BCW 003 (SEQ ID NO: 6), and insect-inhibiting segments, or combinations thereof, conferring activity against Lepidoptera, in particular but not limited to, BCW, WBC, and / or SCB. A polynucleotide encoding BCW 001 was derived from strain EG4384.The core toxic amino acid sequence for BCW 001 corresponds to amino acids from approximately position 28 to approximately position 606 and position 618 as indicated in SEQ ID NO: 2, and the core toxic amino acid sequence for BCW 002 and 003 corresponds to amino acids from approximately position 29 to approximately position 607 and approximately position 619 as indicated in SEQ ID NO: 4 and SEQ ID NO: 6, respectively. In one embodiment, the proteins described herein are related by a primary delta-endotoxin structure, by length (approximately 1176-1180 amino acids), by the length of the protein without the protoxin (from approximately 600 to approximately 619 amino acids), by the length of the toxic core (approximately 591 amino acids), or by the presence of at least one BCW-specific segment. Examples of proteins were aligned with each other using the Clustal W algorithm, resulting in an even number of amino acid identities and a percentage of amino acid identity for each pair using these default parameters: weighting matrix: blosum; gap opening penalty: 10.0; gap extension penalty: 0.05; hydrophilic holes: On; hydrophilic residues: GPSNDQERK; residue-specific space penalties: On. The Clustal W algorithm is described in Thompson, ID., Higgins, DG, and Gibson, TJ. (1994) CLUSTAL W: improving the sensitivity of progressive multiple ι / ui iu sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Research, 22:4673-680. Other alignment algorithms are also available in the technique and provide results similar to those obtained using a Clustal W alignment. The term "approximately" is used herein to describe that these segment boundaries can vary by 1, 2, 3, 4, 5, 10, 20, 25, 30, or 35 residues, depending on the sequence of the original proteins and their alignment with each other. To better describe the variability and configuration of the various segments, the segment boundaries of BCW 002 and 003 and other active Black Cutworm chimeras are tabulated in Tables 2 and 3. The term fragment is used herein to describe consecutive sequences of amino acids or nucleic acids that are shorter than the complete sequence of amino acids or nucleic acids that describes a BCW toxic protein. The terms insect inhibitor and insecticide are used interchangeably herein and refer to a protein, protein fragment, protein segment, or polynucleotide that results in any measurable inhibition of insect viability, growth, development, insect reproduction, insect feeding behavior, insect mating behavior, and / or any measurable decrease in adverse effects caused by an insect feeding on this protein, protein fragment, protein segment, or polynucleotide. The terms biological activity, active, activity, effective, efficacious, or variations thereof are used interchangeably herein to describe the effects of the proteins of the present invention on the target insect pests. A crop plant is a voluntary or cultivated plant whose product is harvested at some point during its growth stage. Non-limiting examples of such products include a seed, a capsule, a leaf, a flower, a stem, a root, or any portion thereof. A biological sample obtained from any tissue of a plant, bacteria, virus, or vector comprising a polynucleotide or expressing a protein as exemplified herein, such as, without limitation, a seed, capsule, leaf, flower, stem, root, or any portion thereof, and containing a detectable amount of the polynucleotide, protein, or both. The term detectable quantity is used herein to describe the minimum amount of a protein or polynucleotide described herein that can be detected by standard analytical methods such as, without limitation, polymerase chain reaction (PCR) and ELISA (enzyme-linked immunosorbent assay) techniques, and the like. In one embodiment, the toxin proteins described herein are related by a common function and exhibit insecticidal activity against lepidopteran insect species. The BCW 001 segments confer Black Cutterworm activity to Cryl chimeras containing such segments. Examples of BCW 001 segments that confer Black Cutterworm activity are set out in SEC ID No. 2 from approximately amino acid position 250 to approximately 606, and more particularly from approximately amino acid position 255 to approximately amino acid position 606.Cryl chimeras containing this amino acid segment corresponding to domains II and III of the BCW 001 toxin protein will frequently also confer upon the chimeric protein the toxic properties associated with the control of Black Cutworm, and this has been proven within the CrylA, CrylB, CrylC, CrylD, CrylE, and CrylF scaffolds in which in the applicable toxin construct the domain II and III components have been substituted with this amino acid range of BCW 001 and in many cases, the Black Cutworm activity is surprisingly maintained in the chimeric construct (data not shown). In one aspect of the invention, the pest being controlled by the applicable BCW toxin protein is specifically an insect pest of the order Lepidoptera, which includes adults, pupae, larvae, and neonates. Lepidoptera insects include, but are not limited to, armyworms, cutworms, surveyor caterpillars, and heliotines of the family Noctuidae (e.g., Fall Armyworm (Spodoptera frugiperda), Beet Armyworm (Spodoptera exigua), Bertha Armyworm (Mamestra configurata), Black Cutworm (Agrotis upsilon), Lettuce Surveyor (Trichoplusia ni), Soybean Surveyor (Pseudoplusia includens), Chickpea Velvetbean Caterpillar (Anticarsia gemmatalis), Green Clover Caterpillar (Hypena scabra), Tobacco Budworm (Heliothis virescens), Granular Cutworm (Agrotis subterranea), Western Cutworm (Agrotis orthogonia), Armyworm (Pseudaletia unipuncta)). borers, boxworms, net worms, tapeworms, Lettuce Worms and Skeleton Worms of the Pyralidae family (e.g., the European Corn Borer (Ostrinia nubilalis), Orange Navel Worm (Amyelois transitella),Corn root webworm (Crambus caliginosellus), sod caterpillar (Herpetogramma licarsisalis), sunflower moth (Homoeosoma electellum), lesser corn stalk borer (Elasmopalpus lignosellus), leafrollers, budworms, seedworms, and fruitworms of the family Tortricidae (e.g., codling moth (Cydia pomonella), grapevine moth (Endopiza viteana), oriental fruit moth (Grapholita molesta), sunflower bud moth (Suleima helianthana)); and many other economically important Lepidoptera (e.g., diamondback moth (Plutella xylostella), rose bollworm (Pectinophora gossypiella), gypsy moth (Lymantria dispar). Other insect pests of the order Lepidoptera include, for example, for example, Alabama argillacea (cotton leafworm), Archips argyrospila (fruit tree leafroller),A. rosana (European leafroller) and other Archips species, Chilo suppressalis (Asian rice borer or rice stem borer), Cnaphalocrocis medinalis (rice leafroller), Crambus caliginosellus (corn rootworm), C. teterrellus (blue corn earworm), Diatraea grandiosella (southeastern corn borer), D. saccharalis (sugarcane borer), Earias insulana (spiny bollworm), E. vittella (bollworm), Helicoverpa armigera (American bollworm), H. zea (corn earworm or cotton bollworm), Heliothis virescens (tobacco budworm), Herpetogramma licarsisalis (cobweb beetle), Lobesia botrana (European Grapevine Moth), Pectinophora gossypiella (Pink Bollworm), Phyllocnistis citrella (Citrus Fruit Miner), Pieris brassicae (Large White Butterfly), P. rapae (Imported Cabbage Worm or Small White Butterfly), Plutella xylostella (Diamond Moth),Spodoptera exigua (Beetroot Armyworm), S. litura (Tobacco Cutworm, Grapevine Caterpillar), S. frugiperda (Autumn Armyworm), and Tuta absoluta (Tomato Leafminer). The proteins described herein can also be used to produce antibodies that bind specifically to BCW-specific toxin proteins and can be used to select and find other members of the BCW toxin genus. In one embodiment, examples of polynucleotides encoding insect-inhibiting BCW 001-related proteins are set out in SEQ ID NO: 1, 3, 5, 7, 9, and 11. The nucleotide sequences encoding these proteins can be used as probes and primers to screen for and identify other members of the genus using thermal or isothermal amplification and / or hybridization methods and other identification methods known to those skilled in the art. One aspect of the invention provides methods for discovering related proteins, and such methods include sequencing Bt genomes, assembling sequence data, identifying and cloning Bt genes encoding such pesticidal proteins, and expressing and testing novel Bt proteins to analyze pesticidal activity. Another aspect of the invention employs molecular methods for designing and cloning commercially useful proteins comprising protein chimeras of the pesticidal protein genus; for example, chimeras can be assembled from segments of toxic BCW proteins to derive further embodiments. The described proteins can be aligned with each other and with other Bt pesticidal proteins, and it is possible to identify segments of each of these proteins that are useful for substitution among the aligned proteins, resulting in the construction of A / a / zuzι / uι ιζ iu chimeric proteins. Such chimeric proteins can be subjected to pest bioassay analysis and characterized based on the presence of increased biological activity and / or an expanded target pest spectrum compared to the parental proteins from which each of these segments in the chimera is derived. The pesticidal activity of the polypeptides can be further engineered to be active against a particular pest or against a broader spectrum of pests by exchanging domains or segments with other proteins. In one embodiment, the proteins described herein include functionally equivalent fragments (N- or C-terminal deletions) of the proteins described herein. The present invention provides BCW toxic proteins. In certain embodiments, the BCW-related toxin proteins can be isolated, provided in a composition, in a transgenic microorganism, or in a transgenic plant. In this embodiment, BCW 002 and particularly the BCW 003 proteins confer inhibitory activity against Lepidoptera, specifically inhibitory activity against the Black Cutworm and / or Sugarcane Borer. Reference in this application to an isolated protein, or an equivalent term or phrase, is intended to mean that the protein is present alone or in combination with other compositions, but not within its natural environment. For example, the toxin proteins of the present invention, and similar proteins, that occur naturally within an organism are not considered isolated as long as they are within the organism in which they occur naturally.However, each of these would be isolated within the scope of this description as long as the protein is not found within the organism in which it is naturally found. The term "operationally linked" as used herein refers to the linking of nucleic acid sequences or amino acid sequences in such a way that one sequence can provide a required function or feature compatible or useful to a linked sequence. Peptides, polypeptides, and proteins that are biologically functionally equivalent to BCW 001, BCW 002, and BCW 003 include, without limitation, amino acid sequences containing conservative amino acid substitutions in these BCW toxin protein sequences. In such amino acid sequences, one or more amino acids are substituted with another amino acid, resulting in a silent or conservative amino acid sequence change. Although the insect-inhibiting polypeptides described herein preferably comprise a protein sequence BCW 001, BCW 002 or BCW 003, fragments and variants of this sequence that possess the same or similar activity are also described herein. A / a / zuz ι / ui iz iu insect inhibitory than that of this insect inhibitory protein. For example, contiguous sequences of at least 30, 35, 38, 40, 45, 50, 55, 60, 65, 70, 75, 100, 150, 200, 500, 550 or more amino acids in a BCW-related toxin protein with inhibitory activity on insects. In another embodiment, fragments of a BCW-related toxin protein with insect inhibitory activity may comprise substitutions, deletions, insertions, or additions of amino acids in a BCW toxin protein sequence. In one embodiment, the insect-inhibiting polypeptide comprises an insect-inhibiting segment from approximately the 28th to the 618th residue of a BCW 001 protein sequence as indicated in SEQ ID NO: 2. Non-limiting examples include any of SEQ ID NOs: 2, 4, or 6, or shorter fragments, or variants possessing the same or similar insect-inhibiting activity as this particular BCW 001 protein, either on their own or in an operable linkage in a chimeric protein. In another embodiment, segments having contiguous amino acid sequences of at least approximately 38 amino acids in any of SEQ ID NOs: 2, 4, or 6 with insect-inhibiting activity also provide a functional insecticidal protein.Insect-inhibiting toxic fragments BCW 001 may also comprise segments with at least 30, 35, 38, 40, 45, 50, 100, 150, 200, 500, 550, 555, 560, 565, 570, 572, 574, 580 or 585 amino acid residues from the 591 amino acid region corresponding to approximately residues 28 to approximately 618 of the sequences of any one of the SEQ ID NOs: 2, 4 or 6. In some embodiments, fragments of the mature BCW 001 protein (mature meaning that the protoxin form of the protein is 1180 amino acids, cleaved by proteolysis in the insect pest gut to release a single N-terminal core toxin at residues 607 through about residue 618, releasing an active toxin segment comprising, more or less, residues 1 through residue 606 or any number of residues from about 5 to about 618, as stated in SEQ ID NO:2, provided that the released segment exhibits toxicity properties on Black Cutworm larvae) may be truncated forms in which one or more amino acids have been deleted from the N-terminal end, the C-terminal end, the center of the protein, or combinations thereof, with insect-inhibiting activity.These fragments may be natural or synthetic variants of BCW 001 and retain the insect-inhibiting activity of a BCW toxin protein. In certain embodiments, mature BCW 001, BCW 002, or BCW 003 protein fragments exhibit the pesticidal activity possessed by the parent protein molecules from which they are derived. A fragment or variant described herein may further comprise a domain identified herein that is responsible for the pesticidal activity of the protein. A / a / zuz ι / ui ιζ iu truncated derivative having insect-inhibiting activity is a BCW toxin protein corresponding to residues from approximately 28 to approximately 606 or to approximately 618 of a BCW toxin protein sequence 001 as indicated in SEQ ID NO: 2 or residues from approximately 29 to approximately 607 and through the 619th residue of a BCW toxin protein as indicated in SEQ ID NO: 4 or in SEQ ID NO: 6.And in yet another embodiment, the N-terminal deletion truncated mutations include, without limitation, BCW 001 toxic proteins that lack amino acid residues from the N-terminus and / or the C-terminus of the non-protoxin toxin portion, or the toxic core of the BCW toxin proteins. For example, 1 to 6 N-terminal amino acid residues can be deleted from the toxic core of a BCW 001 protein corresponding to residues 28 to 618 of SEQ ID NOs: 2 or to residues 29 to 619 of SEQ ID NO: 4 or 6. Truncated C-terminal deletion mutations of a BCW toxin protein corresponding to residues 28 to 618 of SEQ ID NO: 2 or residues 29 to 619 of SEQ ID NO: 4 or 6 include, without limitation, BCW toxin proteins lacking 1 to 6 C-terminal amino acid residues.In other embodiments, a BCW toxin protein with corresponding residues 28 to 618 of SEQ ID NO: 2 or with corresponding residues 29 to 619 of SEQ ID NO: 4 or 6 may have either an N-terminal truncation of 1 to 6 amino-terminal residues or a C-terminal truncation of 1 to 6 carboxy-terminal residues. In some embodiments, individual segments 1 to 6 of a CPR24719 protein, or a combination of segments 1 to 6, which confer activity against Black Cutworm to a protein other than CPR24719-1, may also exhibit the same or a similar function. The fragments and variants of a BCW toxin protein described herein may possess approximately 62% or more sequence identity, approximately 65%, 70%, 75%, 80%, 85%, 90%, 92%, 95%, 96%, 97%, 98%, or greater sequence identity, and approximately 99%, 99.5%, 100% amino acid sequence identity, with the corresponding segments of the mature BCW toxin protein having the corresponding amino acid sequences shown in residues 28 to 618 of SEQ ID NO: 2 or residues 29 to 619 of SEQ ID NO: 4 or 6. One embodiment of the invention includes recombinant polynucleotide compositions encoding BCW toxin proteins. For example, BCW toxin proteins can be expressed using recombinant DNA constructs in which an isolated polynucleotide molecule with the open reading frame encoding the protein is operatively linked to elements such as a promoter and any other functional regulatory elements for expression in the system for which the construct is intended. Reference in this application to an isolated DNA molecule, or an equivalent term or phrase, is intended to mean that the DNA molecule is one that is present alone or in combination with other compositions, but not within its A / a / zuz ι / ui ιζ iu natural environment. For example, nucleic acid elements such as a coding sequence, intron sequence, untranslated leader sequence, promoter sequence, transcriptional termination sequence, and the like, which are naturally found in the DNA of an organism's genome are not considered isolated as long as the element is within the organism's genome and at the location within the genome where it is naturally found. However, each of these elements, and subparts of these elements, would be isolated within the scope of this description as long as the element is not within the organism's genome and at the location within the genome where it is naturally found.Similarly, a nucleotide sequence encoding an insecticidal protein or any naturally occurring insecticidal variant of that protein would be an isolated nucleotide sequence as long as the nucleotide sequence is not within the DNA of the bacterium from which the protein-coding sequence is naturally found. A synthetic nucleotide sequence encoding the amino acid sequence of the naturally occurring insecticidal protein would be considered isolated for the purposes of this description.For the purposes of this description, any transgenic nucleotide sequence—that is, the nucleotide sequence of DNA inserted into the genome of a plant or bacterial cell, or present in an extrachromosomal vector—would be considered an isolated nucleotide sequence whether present within the plasmid or a similar structure used to transform the cells, within the genome of the plant or bacterium, or present in detectable quantities in tissues, progeny, biological samples, or commodity products derived from the plant or bacterium. Non-limiting examples include plant functional promoters operatively linked to the BCW toxin protein that encode sequences for protein expression in plants, or Bt functional promoters operatively linked to the BCW toxin protein that encode sequences for protein expression in Bt.Other elements that can be operationally linked to the BCW toxin protein encoding sequences include, but are not limited to, enhancers, introns, leaders, encoded protein immobilization tags (HIStags), encoded subcellular translocation peptides (e.g., plastid transit peptides, signal peptides), polypeptide sites encoded for post-translational modifying enzymes, ribosome binding sites, and RNAi target sites. As used herein, a recombinant DNA molecule is a DNA molecule comprising a combination of DNA molecules that would not occur naturally together without human intervention. For example, a recombinant DNA molecule may be a DNA molecule composed of at least two heterologous DNA molecules, a DNA molecule comprising a DNA sequence that deviates from naturally occurring DNA sequences, or a DNA molecule that has been incorporated into the DNA of a host cell through genetic transformation or gene editing. Similarly, a protein molecule A recombinant protein is a protein molecule comprising a combination of amino acids that would not occur naturally together without human intervention. For example, a recombinant protein molecule may be a protein molecule composed of at least two heterologous amino acid molecules, a protein molecule comprising an amino acid sequence that deviates from naturally occurring amino acid sequences, or a protein molecule expressed in a host cell as a result of genetic transformation of the host cell or through genetic modification of the host cell's genome. The recombinant polynucleotide molecules provided as examples herein include, but are not limited to, SEQ ID NO: 7, SEQ ID NO: 9, and SEQ ID NO: 11, as well as each of the nucleotide segments listed in SEQ ID NO: 3 and SEQ ID NO: 5, which encode the respective polypeptides or proteins having the amino acid sequences as indicated in SEQ ID NO: 2 (BCW 001), SEQ ID NO: 4 (BCW 002), SEQ ID NO: 6 (BCW 003), and SEQ ID NO: 8, SEQ ID NO: 10, and SEQ ID NO: 12. The codons of a recombinant polynucleotide molecule encoding proteins described herein may be substituted with synonymous codons (also referred to as silent substitution). Recombinant polynucleotides encoding any of the variant proteins of the BCW toxin described herein are also provided. A recombinant DNA construct comprising BCW toxin protein-coding sequences may also further comprise a DNA region encoding one or more insect-inhibiting agents that can be configured to express or co-express concomitantly with a DNA sequence encoding a BCW toxin protein, a protein other than a BCW toxin protein, an insect-inhibiting dsRNA molecule, or an insecticidal chemical compound. Non-limiting examples of insecticidal chemical compounds include organochlorines, organophosphates and carbamates, pyrethroids, neon iodines, and ryanoids. A recombinant DNA construct can be assembled such that all proteins or dsRNA molecules are expressed from a single promoter, or each protein or dsRNA molecule is under the control of a separate promoter, or some combination thereof. The proteins described herein can be expressed from a multigene expression system in which one or more of the proteins described herein are expressed from a common nucleotide segment that also contains other open reading frames and / or promoters, depending on the type of expression system selected. For example, a bacterial multigene expression system may use a single promoter to drive the expression of tandem / multilinked open reading frames from within a single operon.In another example, a plant multigene expression system may utilize 1 / IU to 14 IU multiplexed expression cassettes, each expressing a different protein or other agent such as one or more dsRNA molecules. In yet another example, a plant multigene expression system may utilize multiplexed unbound expression cassettes, each expressing a different protein or other agent such as one or more dsRNA molecules. A promoter for use in a recombinant nucleic acid described herein may comprise a complete promoter sequence or any variant or fragment thereof having gene-promoting or gene-regulating activity. A recombinant polynucleotide or recombinant DNA construct comprising a sequence encoding a BCW toxin protein may be delivered to host cells by vectors, such as a plasmid, baculovirus, artificial chromosome, virion, cosmid, phagemid, phage, or viral vector. Such vectors may be used to achieve stable or transient expression of a sequence encoding the BCW toxin protein in a host cell, or subsequent expression of the polypeptide. An exogenous recombinant polynucleotide or recombinant DNA construct comprising a sequence encoding a toxin protein that is introduced into a host cell is referred to herein as a transgene. Also provided herein are transgenic bacteria, transgenic plant cells, transgenic plants, fungi and yeasts, and transgenic plant parts containing any recombinant polynucleotide expressing any one or more of the BCW toxin protein-coding sequences provided herein. The bacterial cell expressions may include, without limitation, an Agrobacterium, a Bacillus, an Escherichia, a Salmonella, a Pseudomonas, or a Rhizobium cell.The expressions plant cell or plant may include, without limitation, alfalfa, banana, barley, bean, broccoli, cabbage, brassica, carrot, cassava, castor bean, cauliflower, celery, chickpea, Chinese cabbage, citrus, coconut, coffee, corn, clover, cotton, a cucurbit, cucumber, Douglas fir, eggplant, eucalyptus, flax, garlic, grape, hops, leek, lettuce, Loblolly pine, millet, melon, walnut, oats, olive, onion, ornamental plants, palm, grass, pea, peanut, pepper, pigeon pea, pine, potato, poplar, squash, radiata pine, radish, rapeseed, rice, roots, rye, safflower, shrub, sorghum, southern pine, soybean, spinach, pumpkin, strawberry, sugar beet, sugarcane, sunflower, sweetcorn, sweet gum, sweet potato, switchgrass, tea, tobacco, tomato, Triticale, grass, watermelon, and a wheat cell or plant. In certain embodiments, transgenic plants and transgenic plant parts regenerated from a transgenic plant cell are provided.In certain embodiments, transgenic plants can be obtained from a transgenic seed by propagation, cutting, slicing, milling, or otherwise separating the plant part. In certain embodiments, the plant part can be a seed, capsule, leaf, flower, stem, root, or any portion thereof, or a non-regenerable part of a transgenic plant part. A / a / zuz ι / ui ιζ iu As used in this context, the expression "non-regenerable portion of a transgenic plant part" means a portion that cannot be induced to form a complete plant or that cannot be induced to form a complete plant capable of producing sexual effects and / or asexual reproduction. In certain embodiments, a non-regenerable portion of a plant part is a portion of a transgenic seed, capsule, leaf, flower, stem, or root. This document also provides methods for preparing transgenic plants comprising insect- or lepidopteran-inhibiting quantities of a BCW toxin protein. Such plants can be prepared by introducing a recombinant polynucleotide encoding any of the BCW toxin proteins provided herein into a plant cell, and by selecting a plant derived from that plant cell that expresses an insect- or lepidopteran-inhibiting quantity of the BCW toxin proteins. The plants can be derived from plant cells by regeneration, seed, pollen, or meristem transformation techniques. Methods for transforming plants are known in the art. For example, Agrobacterium-mediated transformation is described in U.S. Patent Application Publications 2009 / 0138985A1 (soybean), 2008 / 0280361A1 (soybean), 2009 / 0142837A1 (corn), 2008 / 0282432 (cotton), 2008 / 0256667 (cotton), 2003 / 0110531 (wheat), 2001 / 0042257A1 (sugar beet), U.S. Patents 5,750,871 (candle), 7,026,528 (wheat), and 6,365,757 (rice), and in Arencibia et al. (1998) Transgenic Res. 7: 213-222 (sugarcane). This document also provides for the use of a transgenic plant expressing an insect- or lepidopteran-inhibiting quantity of the BCW toxin protein to control an insect or lepidopteran infestation. Any of the transgenic plants mentioned above may be used in the methods provided herein for protecting a plant from insect or lepidopteran infestation. Methods for obtaining transgenic plants that express active proteins for lepidoptera such as CrylA (U.S. Patent No. 5,880,275), CrylB (U.S. Patent Application No. 10 / 525318), CrylC (U.S. Patent No. 6,033,874), CrylF, CrylA / F chimeras (U.S. Patents Nos. 7,070,982, 6,962,705, and 6,713,063), and Cry2Ab (U.S. Patent No. 7,064,249) proteins are well characterized. The present invention also provides for the use of any of the above-mentioned transgenic host cells to produce a BCW toxin protein. Additional aspects of the invention include antibodies and methods for detecting polynucleotides encoding BCW toxin proteins or for distinguishing between fragments and segments thereof, methods for identifying additional insect inhibitory members of the protein genus, formulations and methods for controlling insect growth and / or infestation, and A / a / zuz ι / ui ιζ iu methods to provide such control to plants and other receiving hosts. In certain embodiments, a plant product may comprise commodity products or trade products derived from a transgenic plant or a part of a transgenic plant, where the trade product or other products can be traced through commerce by detecting nucleotide segments, or expressed RNA or proteins encoding or comprising distinctive portions of a BCW toxin protein. Such commodity products or other products include, without limitation, plant parts, biomass, oil, meal, sugar, animal feed, flour, flakes, bran, fluff, processed seeds, and seeds. Also provided herein are processed plant products wherein said processed product comprises a detectable amount of a recombinant polynucleotide encoding a BCW toxin protein, a segment thereof, an insect-inhibiting fragment thereof, or any distinctive portion thereof. In certain embodiments, the processed product is selected from the group consisting of: plant biomass, oil, meal, animal feed, flour, flakes, bran, fluff, hulls, and processed seeds. In certain embodiments, the processed product is not regenerable. Methods for controlling insects are also provided herein. In certain embodiments, lepidopteran infestations in cultivated plants are controlled. Such methods may comprise cultivating a plant comprising an insect- or lepidopteran-inhibiting quantity of a BCW toxin protein. In certain embodiments, such methods may further comprise any one or more of: (i) applying any composition comprising or encoding a BCW toxin protein to the plant or to a seed giving rise to the plant; and / or (ii) transforming the plant or a plant cell giving rise to the plant with a polynucleotide encoding a BCW toxin protein. In certain embodiments, the plant is a transiently or stably transformed transgenic plant comprising a transgene expressing a lepidopteran-inhibiting quantity of a BCW toxin protein.In certain embodiments, the plant is a non-transgenic plant to which a composition comprising a BCW toxin protein has been applied. In certain embodiments of such methods, the plant is a maize or sugarcane plant. In certain embodiments, the Lepidoptera species is Agrotis ipsilon. In certain embodiments, the Lepidoptera species is Diatraea saccharalis. In certain embodiments, the Lepidoptera species is found in a cultivated field. The enrichment of the proteins described herein, whether in plants or by a process, may include the cultivation of recombinant Bt cells under conditions to express / produce recombinant polypeptides / proteins. Such a process may include the preparation by drying, lyophilization, homogenization, extraction, filtration, centrifugation, sedimentation, or concentration of a culture of recombinant Bt cells that express / produce said recombinant polypeptide. Such a process may result in a Bt cell extract, a cell suspension, a cell homogenate, a cell lysate, a cell supernatant, a cell filtrate, or a Bt cell pellet.By obtaining the recombinant polypeptides / proteins thus produced, a composition including the recombinant polypeptides / proteins may include bacterial cells, bacterial spores and parasporal inclusion bodies and may be formulated for various uses, including agricultural insect-inhibiting spray products or as insect-inhibiting formulations in dietary dioassays. In one embodiment, the insect-inhibiting composition / formulation comprising the disclosed recombination polypeptide / protein may further comprise at least one additional polypeptide that exhibits insect-inhibiting activity against the same Lepidopteran insect species, but is different from the recombination polypeptide, so as to provide a decreased incidence of resistance of Lepidopteran insects to the BCW toxin protein or another Lepidopteran insect-inhibiting composition. Such a polypeptide is selected from the group consisting of: an insect-inhibiting protein, an insect-inhibiting dsRNA molecule, and a chemical compound. An example for the use of such ribonucleotide sequences for controlling insect pests is described in U.S. Patent Application Publication No. 2006 / 0021087. Examples of such other compositions include, without limitation, CrylA (U.S. Patent No.5,880,275), CrylAb, CrylAc, CrylAe, CrylB (US Patent Application No. 10 / 525,318), CrylC (US Patent No. 6,033,874), CrylE, CrylF, and CrylA / F chimeras (US Patent Nos. 7,070,982; 6,962,705 ; Cry43B, ET35, ΕΓ66, TIC400, TIC800, TIC807, TIC834, TIC853 and TIC1415. Other non-limiting examples are proteins active against Lepidoptera: VIP, Axmi and DIG such as, without limitation, Vip3A, VIP3Ab, AXMI-184, AXMI-196, DIG-3, DIG^1, DIG-5, and DIG-11, which can be combined with the proteins described herein. In other embodiments, said composition may further comprise at least one additional polypeptide exhibiting inhibitory activity against an insect not inhibited by an otherwise insect-inhibiting BCW toxin protein to expand the resulting insect inhibition spectrum. For example, for the control of beetle pests, combinations of insect-inhibiting BCW toxin proteins can be used with proteins active against Coleoptera such as, but not limited to, variants of CrylC, variants of Cry3A, Cry3Bb (U.S. Patent No. 6,501,009), Cry34 / 35, 5307, Axm184, Axm205, Axm1, TIC407, TIC417, TIC431, TIC901, TIC1201, TIC3131, DIG-10 and eHIPs (U.S. Patent Application Publication No. 2010 / 0017914). A / a / zuz ι / ui iu The possibility of insects developing resistance to certain insecticides has been documented in the art. One strategy for managing insect resistance involves using transgenic crops that express two different insect-inhibiting agents that operate through different modes of action. Therefore, any insect resistant to one of the insect-inhibiting agents can be controlled by the other insect-inhibiting agent. Another strategy for managing insect resistance involves using plants that are not protected against lepidopteran pest species to create a refuge. A particular example is described in U.S. Patent No. 6,551,962. Other embodiments described herein comprise topically applied pesticide chemical compounds designed to control pests also controlled by the proteins described herein, for use with proteins in seed treatments, spraying, dripping, or wiping formulations that can be applied directly to the soil (a soil soak), applied to growing plants expressing the proteins described herein, or formulated for application to seed containing one or more transgenes encoding one or more of the proteins described. Such seed treatment formulations can be applied with various adhesives and tackifying agents known in the art.Such formulations may contain pesticides that are synergistic in MOA with the described proteins, so that the pesticides in the formulation act through a different MOA to control the same or similar pests that can be controlled by the described proteins, or such pesticides act to control pests with a wider host range, such as species of lepidoptera or hemiptera or other plant pest species such as species of coleoptera that are not effectively controlled. The above-mentioned composition / formulation may further comprise an agriculturally acceptable carrier, such as a bait, powder, granule, spray, emulsion, colloidal suspension, aqueous solution, Bacillus spore / crystal preparation, seed treatment, recombinant plant cell / plant tissue / seed / plant transformed to express one or more of the proteins, or bacteria transformed to express one or more of the proteins. Depending on the inhibitory level on insects or the inherent insecticidal inhibition of the recombinant polypeptide and the formulation level to be applied to a plant or diet trial, the composition / formulation may include various weight percentages of the recombinant polypeptide, for example, from 0.0001% to 0.001% to 0.01% to 1% to 99% by weight of the recombinant polypeptide. The proteins described herein can be combined in formulations for topical application to plant surfaces, to soil, in seed treatment formulations, and A / a / zuz ι / υ i iz iu in formulations with other toxic agents for the target pests of the lepidopteran species. Such agents include without limitation: the proteins CrylA, CrylB, CrylC, CrylF, CrylA / F chimeras, and a Cry2Ab protein. EXAMPLES The following embodiments described are merely representative of the invention, which may be incorporated in various forms. Therefore, the specific structural and functional details described herein should not be interpreted as limiting. It should be understood that the full description of each reference mentioned herein is incorporated herein by reference. EXAMPLE 1 This example teaches the description and analysis of the BCW 001 toxin protein and the construction of chimeric toxins BCW 002 and BCW 003. The Bt strain EG4384 was identified as conferring activity against lepidopteran pests in diet bioassays using spore crystal preparations. The genome sequence of this strain was generated, raw sequence reads were processed, contigs of processed reads were assembled, open reading frames showing homology with Cryl proteins were identified, and the analyzed amino acid sequences were deduced. A particular open reading frame was identified, as indicated in SEQ ID NO: 1, which encoded an amino acid sequence deduced from a protein (BCW 001, SEQ ID NO: 2) that presents a novel amino acid sequence compared to most Cryl proteins known to the art.The protein deduced from the open reading frame has all the characteristics of a novel Cryl-like protein, as it is 1180 amino acids long, and alignment with known Cryl proteins indicates that this protein has a characteristic three-domain structure within the approximately 600–630 amino-terminal amino acids, and a protoxin amino acid sequence characteristic of the CrylA type. The polynucleotide sequence encoding this predicted amino acid sequence contains an open reading frame that is also characteristic of Cryl, namely, an Nhel restriction site within the DNA segment encoding the C-terminal region of the predicted toxin domain I, and a Kpnl restriction site within the DNA segment encoding the N-terminal portion of the predicted protoxin domain. A comparison of the amino acid sequence of BCW 001 toxin with CrylAc reveals that the amino acid segment corresponding to Domain I (amino acids from approximately position 1 to approximately position 258) exhibits only 67% identity with that same segment within CrylAc, the corresponding amino acid segment A / a / zuz ι / ui ιζ iu to domain II (amino acids from approximately position 58 to approximately position 460) has a very low percentage of identity with respect to said segment within CrylAc, and the amino acid segment corresponding to domain III (amino acids from approximately position 460 to approximately position 607) has approximately 63% identity with respect to a segment of Domain III of CrylAh2. The DNA segment encoding substantially the predicted domains II and III, from restriction sites Nhel to Kpnl, was excised and the corresponding segment of a CrylAc-coding sequence was replaced in an expression vector containing a CrylAc-encoding DNA segment, resulting in an open reading frame consisting of, and linking in frame order from five primes to three primes, a first segment encoding Domain I of a CrylAc, a second segment encoding Domains II and III of BCW 001, and a third segment encoding the protoxin domain of the CrylAc toxin protein. This chimeric construct (SEQ ID NO: 3) encodes a chimeric toxin protein referred to herein as BCW 002 (SEQ ID NO: 4).Changing the breakpoint between Domain I and Domain II results in a slightly open reading frame (SEQ ID NO: 5) that encodes a chimeric toxin protein referred to herein as BCW 003 (SEQ ID NO: 6), which has an amino acid sequence different from BCW002 only at the acidic position 259. BCW 003, like BCW 001, contains a threonine (T) at position 259, whereas BCW 002 contains an isoleucine (I) at that position. BCW 001 differs from BCW 002 and BCW 003 primarily within Domain I of the toxin, i.e., amino acids 1-202, and BCW 002 and BCW 003 are, as stated above, virtually identical except for the I / T difference at position 259. EXAMPLE 2 This example demonstrates the biological control activity against the Lepidoptera pest of the BCW proteins 001, 002 and 003. Transformation constructs expressing the BCW 001, 002, and 003 toxin proteins in E. coli, applicable Bacillus thuringiensis, or other Bacilli allowed for the assay of the expressed proteins in the bioassay and their comparison with proteins known in the art to be toxic to the Black Cutworm, such as CrylFa and CrylAc. The resulting recombinant strains were found to express a recombinant protein with activity against lepidopteran pests. The bioassay activity was particularly strong when tested against Black Cutworm and Corn Earworm larvae. As specified earlier in the detailed description, background, and abstract of the invention, very few toxic proteins have been found to exhibit an appreciable level of biological activity. A / a / zuz ι / υ i iz iu against the Black Cutworm, so there is a need in the technique for the identification of such proteins for use in plants to protect such plants against Black Cutworm infestation, and to ensure that there is a sufficient supply of supplemental active proteins available against the Black Cutworm to overcome any development of resistance to any active protein against the Black Cutworm currently in use, such as the CrylFa toxin proteins. EXAMPLE 3 This example shows that domains II and III of BCW 001 are sufficient to carry biological activity against the Black Cutworm to other Cryl toxin proteins when such domains are substituted for the corresponding domains in such other Cryl toxins. Many BCW toxin chimeras with activity against lepidoptera have been identified; two chimeras in particular showed strong activity against BCW, WBC, and SCB. Constructs containing nucleotide sequences encoding CrylAb, CrylAc, and CrylCa were used to construct chimeras containing the Domain II and Domain III segments of BCW 001 substituted with the applicable domains of CrylAb, CrylAc, and CrylCa. The resulting native and chimeric proteins were analyzed in spore crystal bioassays. Activities against BCW, FAW, and CEW were tabulated in these diet bioassays. Under the tested experimental conditions, CrylAc exhibited activity against FAW, BCW, and CEW; CrylAb exhibited activity against FAW and CEW but not against BCW; and CrylCa showed no activity against FAW, BCW, or CEW. BCW 001 exhibited activity against BCW and CEW but not against FAW. Compared to BCW 003, the activity against BCW for CrylAc was approximately ten times lower. CrylAb and CrylAc, chimeras containing domains II and III of BCW 001, exhibited toxic properties when tested in bioassays against FAW, BCW, and CEW.CrylAc was not toxic against CEW and CrylAb was not toxic against BCW. CrylCa / BCW 001 chimeras were constructed in which domain III of CrylCa was replaced by the corresponding domain of BCW 001, and the resulting chimeric toxin exhibited toxic properties against FAW, BCW, and CEW, while the CrylCa toxin was ineffective when tested against any of these pests. EXAMPLE 4 This example illustrates the toxic properties of BCW 001, 002, and 003 when tested in bioassay against a variety of lepidopteran pests. Protocols for insect bioassays and markers for mortality and growth retardation are known in the art, examples of which are described in PCT Patent Application Publication No. WO 2012 / 139004 and in United States Patent No. 7,927,598. Table A correlates the various BCW proteins / toxins 001, 002, and 003 with pesticidal activity against insect species in diet bioassays. Each of these protein toxins demonstrated activity against lepidopteran insects. EXAMPLE 5 This example teaches the construction of artificial sequences encoding the proteins of the present invention for use in plants, the preparation of plant vectors and constructs for use in plants, and the production of plants expressing the proteins of the present invention. The nucleotide sequences encoding protein BCW 001 (SEQ ID NO: 1), protein BCW 002 (SEQ ID NO: 3), and protein BCW 003 (SEQ ID NO: 5) were designed and synthesized according to the methods described in US Patent No. 5,500,365. These coding regions designed for plant expression are provided herein as SEQ ID NO: 7 encoding BCW 001, SEQ ID NO: 9 encoding BCW 002, and SEQ ID NO: 11 encoding BCW 003. A variety of plant expression cassettes were constructed with the sequences as indicated in SEQ ID Nos: 7, 9, and 11. Such expression cassettes are useful for transient expression in plant protoplasts or plant cell transformation. Typical expression cassettes were designed with respect to the final placement of the protein within the cell. One set of expression cassettes was designed to allow the protein to be translated and remain in the cytosol. Another set of expression cassettes was designed to have a transit peptide contiguous to the toxin protein to allow targeting to a cell organelle, such as the chloroplast or plastid. All expression cassettes were designed to begin at the 5' end with a promoter, which may be composed of multiple contiguously linked promoter and enhancer elements to enhance transgene expression.The promoter sequence was usually followed contiguously by one or more 3' leader sequences. A 3' intron sequence was provided to the leader sequence to enhance transgene expression. A coding sequence for the toxin, or the transit peptide and toxin coding sequences, was located 3' upstream of the promoter, in a leader-intron configuration. A 3' upstream sequence was provided to facilitate transcription termination and to supply important sequences for polyadenylation of the resulting transcript. All the elements described above were arranged contiguously, often with an additional sequence provided for expression cassette construction, such as restriction endonuclease sites or ligation-independent cloning sites. ni 7i iη / ι7Π7 / β / υιλι For maize plants, an expression cassette set was designed for cytosolic expression of BCW 001 comprising a Mexicana ubiquitin 1 promoter, BCW 002 comprising an Orysza sativa actin 15 promoter or a 355 promoter, and BCW 003 comprising a 35S promoter. Another set of expression cassettes was designed for targeted expression in maize plants of the insect toxin proteins BCW 002 and BCW 003 in which a chloroplast peptide sequence encoding (e.g., CTP2) was fused into the frame at the 5' end of the DNA segment encoding the BCW toxin proteins, comprising an Orysza sativa actin 15 promoter or a 35S promoter, a sequence comprising a 35S promoter Sugarcane plant expression cassettes were constructed comprising a CaMV 35S promoter or a PCISV.FLt promoter operatively linked to a 35S promoter in plant transformation vectors. In some cases, a cassette expressing a chloroplast-directed Cry2Ab was included. Plants expressing the proteins of the present invention were tested against third-stage metamorphosis larvae of BCW, WBC, CEW, SWC, and SCB. The cytosolic expression cassette for BCW 001 and the cytosolic and plastid-directed expression cassettes for BCW 002 and BCW 003 were cloned and used to produce transgenic maize events expressing these proteins. The transformed cells were induced to form plants using methods known in the art. Bioassays using plant leaf discs were performed similarly to that described in U.S. Patent 8,344,207. The leaf damage rating (LDR) was assigned a rating score based on the percentage of the leaf disc eaten by the insect on a scale from 0 (0% eaten) to 11 (more than 50% eaten). Rating score stages increase incrementally by 5%.An isogenic maize line was used to obtain tissue as a negative control, and the results were evaluated. Both plastid-directed and cytosolic expression of the insect toxin proteins BCW 002 and BCW 003 reduced feeding damage relative to the non-transformed control. The results of leaf disc assays against these insects were consistent with the bioassay data from the examples presented earlier. A construct comprising a BCW 003 cassette for cytosolic expression resulted in 34 transformation events, 25 of which showed complete control of BCW newborns. Maize plants expressing BCW 001 and BCW 003 in the cytosol were also tested against CEW, SWC, and FAW. Plants expressing BCW 003 showed 100% control of CEW and SWC values, with LDRs ranging from 1 to 2.Three transformation events expressing BCW 001 resulted in plants that showed efficacy against CEW and SWC and LDR values ​​between 1 and 3. This is consistent with diet bioassay data. A / a / zuz ι / ui ιζ iu presented in the previous examples. Transgenic sugarcane plants expressing BCW 003 were generated and tested against the sugarcane borer (SCB) in bioassays. Each bioassay included wild-type sugarcane leaf discs as a negative control and a positive control expressing elevated levels of Cry2Ab. Insect mortality and leaf damage were measured four (4) days post-infestation. Leaf discs from various transgenic sugarcane events expressing BCW 003 were found to control the sugarcane borer in planta, exhibiting a damage index below 2, similar to the positive control, and an average insect mortality rate of 90–100%. Transgenic events expressing BCW 003 and Cry2Ab showed better SCB control compared to events that only expressed BCW 003.

Claims

1. A polynucleotide construct comprising a nucleotide sequence encoding: (a) an insecticidal protein having the amino acid sequence comprising amino acids 1 to 607 of a sequence selected from the group consisting of SEQ ID NO: 2 and SEQ ID NO: 8, or one of the insecticidal fragments thereof; (b) a polypeptide fragment having at least 95% identity with the amino acid sequence of (a); (c) a polypeptide fragment having at least 84% identity with the amino acid sequence of (a); (d) a polypeptide fragment having at least 64% identity with the amino acid sequence of (a); or (e) an insecticidal protein having the amino acid sequence from position 7 to 607 as indicated in either SEQ ID NO: 2 or 8 wherein said nucleotide sequence is operatively linked to a heterologous promoter sequence.

2. A protein toxic to the lepidopteran species Black Cutworm comprising the amino acid sequence as indicated in SEQ ID NO: 2 from position 256 to 606.

3. The polynucleotide construct of claim 1, wherein said insecticidal protein has activity against selected Lepidoptera species of the group consisting of Spodoptera frugiperda, Spodoptera exigua, Spodoptera iitura, Mamegúr, St. Trichopiusia ni, Pseudopiusia inciudens, Anticarsia gemmataiis, Hypena scabra, Heiiothis virescens, Agrotis subterranea, Pseudaietia unipuncta, Agrotis ípsilon, Agrotis orthogonia, Ostrínia nubilalis, Amyeiois transiteiligiia, Crambus calum, Hersiscarma, Hersis, Homoeosoma electellum, Elasmopalpus lignosellus, Cydia pomoneiia, Endopiza viteana, Graphoiita molesta, Suleima helianthana, Plutella xylostella, Pectinophora gossypiella, Lyman tria dispar, / Aiabama argüiacea, Archips argyrospiia, Archips suppressa, Archips suppressa, Cnaphalocrocis medinaiis, Crambus caliginosellus, Crambus teterrellus, Diatraea grandiosella, Diatraea saccharaüs, Earías insulana, Egrías vittella,Helicoverpa armigera, Helicoverpa zea, Heiiothis virescens, Herpetogramma licarsisalis, Lobesia botrana, Pectinophora gossypiella, Phyllocnistis citrella, Pieris brassicae, Pieris rapae, Plutella xylostella, and Tuta absoluta.

4. The protein in accordance with claim 2 which further comprises a biological activity against selected lepidopterous species of the group consisting of Spodoptera A / a / zuz ι / ui ιζ iu frugiperda, Spodoptera exigua, Spodoptera Htura, Mamestra configurata, Striacosta albicosta, Tríchop / usia ni, Pseudop / usia indudens, Anticarsia gemmatalis, Hy scabpenara, Heliothis virescens, Agrotis subterranea, Pseuda / etia unipuncta, Agrotis ípsilon, Agrotis orthogonia, Ostrinia nubi / a / is, Amyelois transitella, Crambus calíginosellus, Herpetogramma Hcarsisa / is, Homoeosoma electellum, E / asmopa / pus lignosellus, Cydia pomonella, Endopiza viteana, Grapho / ita molesta, Suleima helianthana, Plutella xylostella, Pectinophora gossypiella, Lymantria dispar, ¡A / abama argillacea, Archips argyrospi / a, Archips rosana, Chito suppressaüs, Cnaphalocrocis medinalis, Crambus calíginosellus, Crambus teterrellus, Diatraea grandiosella, Diatraea saccharaüs, Earias insulana, Egrias vittella, Helico / erpa armígera,Heíicoverpa zea, Heíiothis virescens, Herpetogramma Hcarsisaíis, Lobesia botrana, Pectinophora gossypiella, Phyllocnistis citrella, Pieris brassicae, Pieris rapae, Plutella xylostella, and Tuta ABSOLUTA.

5. A vector comprising the polynucleotide construct according to claim 1.

6. A host cell comprising the polynucleotide construct according to claim 1, wherein the host cell is selected from the group consisting of a bacterial cell, a yeast cell, and a plant cell.

7. A host cell according to claim 6, wherein said host cell is selected from the group consisting of alfalfa, banana, barley, bean, broccoli, cabbage, brassica, carrot, cassava, castor bean, cauliflower, celery, chickpea, Chinese cabbage, citrus, coconut, coffee, corn, clover, cotton, cucurbits, cucumber, Douglas fir, eggplant, eucalyptus, flax, garlic, grape, hops, leek, lettuce, Loblolly pine, millet, melon, walnut, oat, olive, onion, ornamental plants, palm, grass, pea, peanut, pepper, pigeon pea, pine, potato, poplar, pumpkin, Radiata pine, radish, rapeseed, rice, roots, rye, safflower, shrub, sorghum, southern pine, soybean, spinach, squash, strawberry, sugar beet, sugar cane, sunflower, sweetcorn, gum chewing gum, sweet potato, switchgrass, tea, tobacco, tomato, triticale, lawn, watermelon, and wheat plants.

8. A plant comprising the polynucleotide construct according to claim 1 9. A seed produced from a plant according to claim 8, comprising a detectable amount of said polynucleotide construct.

10. The plant according to claim 8, wherein the seed, pollen, progeny, plant cells, plant tissue and consumer products produced from said plant comprise a detectable amount of said polynucleotide construct.

11. A biological sample comprising a detectable amount of the polynucleotide construct according to claim 1.

12. A composition providing an effective insecticidal amount of the ι / ui iu protein according to claim 2 for controlling a species of lepidopteran pest, and: (a) an agent different from said protein and also toxic to the same species of lepidopteran, wherein said agent is selected from the group consisting of a polypeptide having an amino acid sequence different from said protein, an RNA molecule, and a chemical compound; or (b) an agent selected from the group consisting of: insecticidal proteins CrylA, CrylAb, CrylAc, CrylA.105, CrylAe, CrylB, CrylC, CrylD, CrylE, CrylF, CrylG, CrylH, Cryll, CrylJ, CrylK, CrylL, Cry2A, Cry2Ab, insecticidal proteins Cry2Ae, Cry4B, Cry6, Cry7, Cry8, Cry9, Cryl5, Cry43A, Cry43B, ET35, ET66, TIC400, TIC800, TIC807, TIC853, TIC853, TIC1415, VIP3A, VIP3Ab, AXMI, insecticidal proteins DIG, eHIP, and VIP proteins.

13. The composition according to claim 12, further comprising an additional pesticide agent, wherein said additional agent is selected from the group consisting of CrylC, Cry3A, Cry3B, Cry34, Cry35, Cry51Aal, ET29, ET33, EG34, ET70, TIC407, TIC417, TIC431, TIC901, TIC1201, TIC3131, 5307, DIG-10, Axmil84, Axmi205 and AxmIRl.

14. A plant according to claim 8, further comprising: (a) a transgenic maize plant event selected from the group consisting of DKB89614-9, MON801, MON802, MON809, MON810, MON863, MON88017, MON89034, event 4114-3, event 5307, DAS59122-7, BtlO, Btll, Btl76, CBH-351, DKB-83614-9, MIR162, MIR604, TC1507, TC6275, event 676, event 678, event 680, event 98140, DAS40278-9, DKB89790-5, MON21-9, HCEM485, MON832, MON87427, NK603, T14, T25 and VCO01981-5; (b) a transgenic event in soybean plants selected from the group consisting of MON87751, DAS81419-2, MON87701, A2704-12, A2704-21, A5547-127, A5547-35, CV127, DAS44406-6, DAS68416-4, DP356043, FG72, MON4032, ACS-GM003-1, MON87705, MON87708, MON89788, W62, W98 and GFM CrylA;(c) a transgenic event in cotton plants selected from the group consisting of DAS24236-5, DAS21023-5, event 31707, event 31803, event 31807, event 31808, event 42317, BNLA-601, COT102, COT67B, event 1, GHB119, GK12, MON15985, MLS9124, MON1076, MON531, MON757, T303-3, T304-40, SGK321, event 19-51a, GHB614, LLCotton25, MON88701, MON88702, MON1445, MON1698 and MON88913; (d) an NXI-1T transgenic event in sugarcane plants and (e) a transgenic event in rice plants selected from the group consisting of LLRICE06, LLRICE601, LLRIC2E62, GM-A17054 and GM-A17054.; 15. A lepidopteran toxic protein comprising in one operable linkage: (a) a first peptide segment comprising an amino acid sequence of domain I CrylA; (b) a second peptide segment comprising an amino acid sequence BCW 001 Domain II - Domain Illen wherein said lepidopteran toxic protein exhibits toxic biological activity when assayed against a lepidopteran pest selected from the group consisting of a Black Cutworm (4. ipsilon), a Corn Earworm (H. zea), a Western Bean Cutworm (S. a / bicostá), a European Corn Borer {O. nubilalis}, a Southeastern Corn Borer (D. grandioseiia), a Lettuce Survey Caterpillar (T ni), a Soybean Survey Caterpillar (P. inciudens), an Autumn Armyworm (5. frugiperda), and a Sugarcane Borer (D. saccharaiis).