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A transgenic plant comprising DNA encoding a Vip3Ab insecticidal protein and DNA encoding a Cry1F insecticidal protein.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"2 . Seed of a plant of claim 1 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"3 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"4 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"5 . A field of plants comprising non-Bt refuge plants and a plurality of plants of claim 1 , wherein said refuge plants comprise less than 40% of all crop plants in said field.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"6 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"7 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"8 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"9 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"10 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"11 . A mixture of seeds comprising refuge seeds from non-Bt refuge plants, and a plurality of seeds of claim 2 , wherein said refuge seeds comprise less than 40% of all the seeds in the mixture.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"12 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"13 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"14 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"15 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"16 . A method of managing development of resistance by an insect to an insecticidal protein derived from a Bacillus thuringiensis , said method comprising planting seeds to produce a field of plants of claim 5 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"17 . The transgenic plant of claim 1 , said plant further comprising DNA encoding a third insecticidal protein, said third protein being selected from the group consisting of Cry1C, Cry1D, Cry1Be, and Cry1E.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"18 . A field of plants comprising non-Bt refuge plants and a plurality of transgenic plants of claim 17 , wherein said refuge plants comprise less than about 20% of all crop plants in said field.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"19 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"20 . A method of managing development of resistance by an insect to an insecticidal protein derived from a Bacillus thuringiensis , said method comprising planting seeds to produce a field of plants of claim 18 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"21 . A composition for controlling lepidopteran pests comprising cells that express effective amounts of both a Cry1F core toxin-containing protein and a Vip3Ab protein.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"22 . The composition of claim 21 comprising a host transformed to express both a Cry1F core toxin-containing protein and a Vip3Ab protein, wherein said host is a microorganism or a plant cell.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"23 . A method of controlling lepidopteran pests comprising presenting to said pests or to the environment of said pests an effective amount of a composition of claim 21 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"24 . The transgenic plant of claim 1 , said plant further comprising DNA encoding a third insecticidal protein, said third protein being selected from the group consisting of Cry1C, Cry1D, and Cry1E.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"25 . The transgenic plant of claim 24 wherein said plant produces a fourth protein and a fifth protein selected from the group consisting of Cry2A, Cry1I, Cry1Ab, and DIG-3.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"26 . The transgenic plant of claim 17 wherein said plant produces a fourth protein selected from the group consisting of Cry2A, Cry1I, Cry1Ab, and DIG-3.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"27 . A method of managing development of resistance to a Cry toxin by an insect, said method comprising planting seeds to produce a field of plants of claim 26 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"28 . A field of plants comprising non-Bt refuge plants and a plurality of plants of claim 26 , wherein said refuge plants comprise less than about 10% of all crop plants in said field.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"29 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"30 . A method of managing development of resistance to a Cry toxin by an insect, said method comprising planting seeds to produce a field of plants of claim 28 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"31 . A mixture of seeds comprising refuge seeds from non-Bt refuge plants, and a plurality of seeds from a plant of claim 26 , wherein said refuge seeds comprise less than 10% of all the seeds in the mixture.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"32 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"33 . The plant of claim 1 , wherein said plant is selected from the group consisting of corn, soybeans, and cotton.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"34 . The plant of claim 1 , wherein said plant is a maize plant.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"35 . The transgenic plant of claim 26 wherein said third protein is a Cry1Be protein.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"36 . A method of managing development of resistance to a Cry toxin by an insect, said method comprising planting seeds to produce a field of plants of claim 35 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"37 . A field of plants comprising non-Bt refuge plants and a plurality of plants of claim 35 , wherein said refuge plants comprise less than about 10% of all crop plants in said field.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"38 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"39 . A method of managing development of resistance to a Cry toxin by an insect, said method comprising planting seeds to produce a field of plants of claim 37 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"40 . A mixture of seeds comprising refuge seeds from non-Bt refuge plants, and a plurality of seeds from a plant of claim 35 , wherein said refuge seeds comprise less than 10% of all the seeds in the mixture.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"41 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"42 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"43 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"44 . A plant cell of a plant of claim 1 , wherein said plant cell comprises said DNA encoding said Cry1F insecticidal protein and said DNA encoding said Vip3Ab insecticidal protein, wherein said Cry1F insecticidal protein is at least 99% identical with SEQ ID NO:1, and said Vip3Ab insecticidal protein is at least 99% identical with SEQ ID NO:2.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"45 . The plant of claim 1 , wherein said Cry1F insecticidal protein comprises SEQ ID NO:1, and said Vip3Ab insecticidal protein comprises SEQ ID NO:2.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"claim_lang":["en"],"has_claim":true,"description":{"en":{"text":"BACKGROUND OF THE INVENTION Humans grow corn for food and energy applications. Humans also grow many other crops, including soybeans and cotton. Insects eat and damage plants and thereby undermine these human efforts. Billions of dollars are spent each year to control insect pests and additional billions are lost to the damage they inflict. Synthetic organic chemical insecticides have been the primary tools used to control insect pests but biological insecticides, such as the insecticidal proteins derived from Bacillus thuringiensis (Bt), have played an important role in some areas. The ability to produce insect-resistant plants through transformation with Bt insecticidal protein genes has revolutionized modern agriculture and heightened the importance and value of insecticidal proteins and their genes. Several Bt proteins have been used to create the insect-resistant transgenic plants that have been successfully registered and commercialized to date. These include Cry1Ab, Cry1Ac, Cry1F and Cry3Bb in corn, Cry1Ac and Cry2Ab in cotton, and Cry3A in potato. The commercial products expressing these proteins express a single protein except in cases where the combined insecticidal spectrum of 2 proteins is desired (e.g., Cry1Ab and Cry3Bb in corn combined to provide resistance to lepidopteran pests and rootworm, respectively) or where the independent action of the proteins makes them useful as a tool for delaying the development of resistance in susceptible insect populations (e.g., Cry1Ac and Cry2Ab in cotton combined to provide resistance management for tobacco budworm). See also US 2009 0313717, which relates to a Cry2 protein plus a Vip3Aa, Cry1F, or Cry1A for control of Helicoverpa zea or armigerain . WO 2009 132850 relates to Cry1F or Cry1A and Vip3Aa for controlling Spodoptera frugiperda . US 2008 0311096 relates in part to Cry1Ab for controlling Cry1F-resistant ECB. That is, some of the qualities of insect-resistant transgenic plants that have led to rapid and widespread adoption of this technology also give rise to the concern that pest populations will develop resistance to the insecticidal proteins produced by these plants. Several strategies have been suggested for preserving the utility of Bt-based insect resistance traits which include deploying proteins at a high dose in combination with a refuge, and alternation with, or co-deployment of, different toxins (McGaughey et al. (1998), “B.t. Resistance Management,” Nature Biotechnol. 16:144-146). The proteins selected for use in an IRM stack need to exert their insecticidal effect independently so that resistance developed to one protein does not confer resistance to the second protein (i.e., there is not cross resistance to the proteins). If, for example, a pest population selected for resistance to “Protein A” is sensitive to “Protein B”, one would conclude that there is not cross resistance and that a combination of Protein A and Protein B would be effective in delaying resistance to Protein A alone. In the absence of resistant insect populations, assessments can be made based on other characteristics presumed to be related to mechanism of action and cross-resistance potential. The utility of receptor-mediated binding in identifying insecticidal proteins likely to not exhibit cross resistance has been suggested (van Mellaert et al. 1999). The key predictor of lack of cross resistance inherent in this approach is that the insecticidal proteins do not compete for receptors in a sensitive insect species. In the event that two Bt toxins compete for the same receptor, then if that receptor mutates in that insect so that one of the toxins no longer binds to that receptor and thus is no longer insecticidal against the insect, it might be the case that the insect will also be resistant to the second toxin (which competitively bound to the same receptor). That is, the insect is said to be cross-resistant to both Bt toxins. However, if two toxins bind to two different receptors, this could be an indication that the insect would not be simultaneously resistant to those two toxins. Cry1Fa is useful in controlling many lepidopteran pests species including the European corn borer (ECB; Ostrinia nubilalis (Hubner)) and the fall armyworm (FAW; Spodoptera frugiperda ), and is active against the sugarcane borer (SCB; Diatraea saccharalis ). The Cry1Fa protein, as produced in corn plants containing event TC1507, is responsible for an industry-leading insect resistance trait for FAW control. Cry1Fa is further deployed in the Herculex®, SmartStax™, and WideStrike™ products. The ability to conduct (competitive or homologous) receptor binding studies using Cry1Fa protein is limited because the most common technique available for labeling proteins for detection in receptor binding assays inactivates the insecticidal activity of the Cry1Fa protein. Additional Cry toxins are listed at the website of the official B. t. nomenclature committee (Crickmore et al.; lifesci.sussex.ac.uk/home/Neil_Crickmore/Bt/). There are currently nearly 60 main groups of “Cry” toxins (Cry1-Cry59), with additional Cyt toxins and VIP toxins and the like. Many of each numeric group have capital-letter subgroups, and the capital letter subgroups have lower-cased letter sub-subgroups. (Cry1 has A-L, and Cry1A has a-i, for example). BRIEF SUMMARY OF THE INVENTION The subject invention relates in part to the surprising discovery that a fall armyworm ( Spodoptera frugiperda ; FAW) population resistant to the insecticidal activity of the Cry1Fa protein is not resistant to the insecticidal activity of the Vip3Ab protein. The subject pair of toxins provides non-cross-resistant action against FAW. As one skilled in the art will recognize with the benefit of this disclosure, plants expressing Vip3Ab and Cry1Fa, or insecticidal portions thereof, will be useful in delaying or preventing the development of resistance to either of these insecticidal proteins alone. The subject invention is also supported by the discovery that Vip3Ab and Cry1Fa do not compete with each other for binding sites in the gut of FAW. Thus, the subject invention relates in part to the use of a Vip3Ab protein in combination with a Cry1Fa protein. Plants (and acreage planted with such plants) that produce Vip3Ab plus Cry1Fa are included within the scope of the subject invention. The subject invention also relates in part to triple stacks or “pyramids” of three toxins, or more, with Vip3Ab and Cry1Fa being the base pair. In some preferred pyramid embodiments, the selected toxin(s) have non-cross-resistant action against FAW. Some preferred proteins for these triple-stack pyramid combinations are Cry1Fa plus Vip3Ab plus Cry1C, Cry1D, Cry1Be, or Cry1E. These particular triple stacks would, according to the subject invention, advantageously and surprisingly provide non-cross-resistant action against FAW. This can help to reduce or eliminate the requirement for refuge acreage. With Cry1Fa being active against both FAW and European cornborer (ECB), and in light of the data presented herein, a quad (four-way) stack could also be selected to provide four proteins, wherein three of the four have non-cross-resistant activity against ECB, and three of the four have non-cross-resistant activity against FAW. This could be obtained by using Cry1Be (active against both ECB and FAW) together with the subject pair of proteins, plus one additional protein that is active against ECB. Such quad stacks, according to the subject invention, are: Cry1F plus Cry1Be plus Vip3Ab (active against FAW) plus Cry1Ab, Cry2A, Cry1I, or DIG-3 (active against ECB). BRIEF DESCRIPTION OF THE FIGURES FIG. 1 . Growth inhibition (bars) and mortality (♦) dose responses for full length Vip3Ab1 against wild type Spodoptera frugiperda (J. E. Smith), (FAW) and Cry1Fa resistant type Spodoptera frugiperda (J. E. Smith), (rFAW). Percent growth inhibition is based upon comparison of average weight of 8 larvae treated with buffer only to the weight of larvae exposed to the toxin for 5 days. FIG. 2 . Phosphor-image of 125 I Cry1Fa bound to BBMV's from S. frugiperda after being separated by SDS-PAGE. Samples done in duplicate. Concentration of 125 I Cry1Fa was 1 nM. Control represents level of binding of 125 I Cry1Fa to BBMV's in the absence of any competitive ligand. 1,000 nM Cry1Fa represents the level of binding of 125 I Cry 1Fa to BBMV's in the presence of 1,000 nM non-radiolabeled Cry1Fa, showing complete displacement of the radiolabeled ligand from the BBMV protein. 1,000 nM Vip3Ab1 represents the level of binding of 125 I Cry1Fa to BBMV's in the presence of 1,000 nM non-radiolabeled Vip3Ab1, showing that this protein does not have the ability to displace 125 I Cry1Fa from S. frugiperda BBMV's even when added at 1,000-times the concentration of the radiolabeled ligand. FIG. 3 . Phosphor-image of 125 I Cry1Fa bound to BBMV's from wild type S. frugiperda (FAW) or Cry1Fa resistant S. frugiperda (rFAW), after being separated by SDS-PAGE. Samples done in duplicate. Concentration of 125 I Cry1Fa was 2.5 nM. FAW-0 represents level of binding of 125 I Cry1Fa to wild type S. frugiperda BBMV's in the absence of any competitive ligand. FAW-1,000 nM Cry1Fa represents the level of binding of 125 I Cry1Fa to wild type S. frugiperda BBMV's in the presence of 1,000 nM non-radiolabeled Cry1Fa, showing displacement of the radiolabeled ligand from the BBMV protein. rFAW-0 represents level of binding of 125 I Cry1Fa to Cry1Fa resistant S. frugiperda BBMV's in the absence of any competitive ligand. Note the absence of binding of 125 I Cry1Fa to the BBMV's from resistant FAW. rFAW-1,000 nM Cry1Fa represents the level of binding of 125 I Cry1Fa to BBMV's in the presence of 1,000 nM non-radiolabeled Vip3Ab1, again showing the inability of 125 I Cry1Fa to bind to BBMV's from Cry1Fa resistant S. frugiperda. DETAILED DESCRIPTION OF THE INVENTION As reported herein, a Vip3Ab toxin produced in transgenic corn (and other plants; cotton and soybeans, for example) can be very effective in controlling fall armyworm (FAW; Spodoptera frugiperda ) that have developed resistance to Cry1Fa activity. Thus, the subject invention relates in part to the surprising discovery that fall armyworm resistant to Cry1Fa are susceptible (i.e., are not cross-resistant) to Vip3Ab. Stated another way, the subject invention also relates in part to the surprising discovery that Vip3Ab toxin is effective at protecting plants (such as maize plants) from damage by Cry1Fa-resistant fall armyworm. For a discussion of this pest, see e.g. Tabashnik, PNAS (2008), vol. 105 no. 49, 19029-19030. The subject invention includes the use of Vip3Ab toxin to protect corn and other economically important plant species (such as soybeans) from damage and yield loss caused by fall armyworm feeding or to fall armyworm populations that have developed resistance to Cry1Fa. The subject invention thus teaches an IRM stack comprising Vip3Ab to prevent or mitigate the development of resistance by fall armyworm to Cry1Fa. The present invention provides compositions for controlling lepidopteran pests comprising cells that produce a Cry1Fa core toxin-containing protein and a Vip3Ab core toxin-containing protein. The invention further comprises a host transformed to produce both a Cry1Fa insecticidal protein and a Vip3Ab insecticidal protein, wherein said host is a microorganism or a plant cell. The subject polynucleotide(s) are preferably in a genetic construct under control of (operably linked to/comprising) a non-Bacillus-thuringiensis promoter(s). The subject polynucleotides can comprise codon usage for enhanced expression in a plant. It is additionally intended that the invention provides a method of controlling lepidopteran pests comprising contacting said pests or the environment of said pests with an effective amount of a composition that contains a Cry1Fa core toxin-containing protein and further contains a Vip3Ab core toxin-containing protein. An embodiment of the invention comprises a maize plant comprising a plant-expressible gene encoding a Vip3Ab core toxin-containing protein and a plant-expressible gene encoding a Cry1Fa core toxin-containing protein, and seed of such a plant. A further embodiment of the invention comprises a maize plant wherein a plant-expressible gene encoding a Vip3Ab core toxin-containing protein and a plant-expressible gene encoding a Cry1Fa core toxin-containing protein have been introgressed into said maize plant, and seed of such a plant. As described in the Examples, competitive binding studies using radiolabeled Vip3Ab core toxin protein show that the Cry1Fa core toxin protein does not compete for binding in FAW insect tissues to which Vip3Ab binds. These results also indicate that the combination of Cry1Fa and Vip3Ab proteins is an effective means to mitigate the development of resistance in FAW populations to Cry1Fa (and likewise, the development of resistance to Vip3Ab), and would likely increase the level of resistance to this pest in corn plants expressing both proteins. Thus, based in part on the data described herein, it is thought that co-production (stacking) of the Vip3Ab and Cry1Fa proteins can be used to produce a high dose IRM stack for FAW. With Cry1Fa being active against both FAW and European cornborer (ECB), the subject pair of toxins provides non-competitive action against the FAW. Other proteins can be added to this pair to expand insect-control spectrum. Another deployment option would be to use Cry1Fa and Vip3Ab proteins in combination with another, third toxin/gene, and to use this triple stack to mitigate the development of resistance in FAW to any of these toxins. Thus, another deployment option of the subject invention would be to use two, three, or more proteins in crop-growing regions where FAW can develop resistant populations. Accordingly, the subject invention also relates in part to triple stacks or “pyramids” of three (or more) toxins, with Cry1Fa and Vip3Ab toxins being the base pair. In some preferred pyramid embodiments, the three selected proteins provide non-cross-resistant action against FAW. Some preferred “triple action” pyramid combinations are Cry1Fa plus Vip3Ab plus either Cry1C or Cry1D. See U.S. Ser. No. 61/284,281 (filed Dec. 16, 2009), which shows that Cry1C is active against Cry1F-resistant FAW, and U.S. Ser. No. 61/284,252 (filed Dec. 16, 2009), which shows that Cry1D is active against Cry1F-resistant FAW. These two applications also show that Cry1C does not compete with Cry1F for binding in FAW membrane preparations, and that Cry1D does not compete with Cry1F for binding in FAW membrane preparations. In some embodiments, Cry1Be or Cry1E could be combined with Vip3A and Cry1F as the third anti-FAW protein. For use of Cry1Be with Cry1F, see U.S. Ser. No. 61/284,290 (filed Dec. 16, 2009). For use of Cry1E with Cry1F, see U.S. Ser. No. 61/284,278 (filed Dec. 16, 2009). These particular triple stacks would, according to the subject invention, advantageously and surprisingly provide three proteins providing non-cross-resistant action against FAW. This can help to reduce or eliminate the requirement for refuge acreage. In light of the data presented herein, a quad (four-way) stack could also be selected to provide three proteins with non-cross-resistant action against ECB and three proteins with non-cross-resistantaction against FAW. This could be obtained by using Cry1Be (active against both ECB and FAW) together with Cry1Fa (active against both ECB and FAW) together with the subject Vip3Ab (active against FAW) and a fourth protein—having ECB-toxicity (See U.S. Ser. No. 61/284,290, filed Dec. 16, 2009, which relates to combinations of Cry1Fa and Cry1Be.) Examples of quad stacks, according to the subject invention, are: Cry1F plus Cry1Be plus Vip3 (active against FAW) plus (Cry1Ab, Cry2A, Cry1I, or DIG-3—all active against ECB). DIG-3 is disclosed in US 2010 00269223. Plants (and acreage planted with such plants) that produce any of the subject combinations of proteins are included within the scope of the subject invention. Additional toxins/genes can also be added, but the particular stacks discussed above advantageously and surprisingly provide multiple modes of action against FAW and/or ECB. This can help to reduce or eliminate the requirement for refuge acreage. A field thus planted of over 10 acres is thus included within the subject invention. GENBANK can also be used to obtain the sequences for any of the genes and proteins disclosed or mentioned herein. See Appendix A, below. U.S. Pat. No. 5,188,960 and U.S. Pat. No. 5,827,514 describe Cry1Fa core toxin containing proteins suitable for use in carrying out the present invention. U.S. Pat. No. 6,218,188 describes plant-optimized DNA sequences encoding Cry1Fa core toxin-containing proteins that are suitable for use in the present invention. Cry1Fa is in the Herculex®, SmartStax™, and WidesStrike™ products. A vip3Ab gene could be combined into, for example, a Cry1Fa product such as Herculex®, SmartStax™, and WideStrike™. Accordingly, use of Vip3Ab could be significant in reducing the selection pressure on these and other commercialized proteins. Vip3Ab could thus be used as in the 3 gene combination for corn and other plants (cotton and soybeans, for example). Combinations of proteins described herein can be used to control lepidopteran pests. Adult lepidopterans, for example, butterflies and moths, primarily feed on flower nectar and are a significant effector of pollination. Nearly all lepidopteran larvae, i.e., caterpillars, feed on plants, and many are serious pests. Caterpillars feed on or inside foliage or on the roots or stem of a plant, depriving the plant of nutrients and often destroying the plant's physical support structure. Additionally, caterpillars feed on fruit, fabrics, and stored grains and flours, ruining these products for sale or severely diminishing their value. As used herein, reference to lepidopteran pests refers to various life stages of the pest, including larval stages. Some chimeric toxins of the subject invention comprise a full N-terminal core toxin portion of a Bt toxin and, at some point past the end of the core toxin portion, the protein has a transition to a heterologous protoxin sequence. The N-terminal, insecticidally active, toxin portion of a Bt toxin is referred to as the “core” toxin. The transition from the core toxin segment to the heterologous protoxin segment can occur at approximately the toxin/protoxin junction or, in the alternative, a portion of the native protoxin (extending past the core toxin portion) can be retained, with the transition to the heterologous protoxin portion occurring downstream. As an example, one chimeric toxin of the subject invention, is a full core toxin portion of Cry1Fa (roughly the first 600 amino acids) and a heterologous protoxin (the remainder of the protein to the C-terminus). In one preferred embodiment, the portion of a chimeric toxin comprising the protoxin is derived from a Cry1Ab protein toxin. In a preferred embodiment, the portion of a chimeric toxin comprising the protoxin is derived from a Cry1Ab protein toxin. A person skilled in this art will appreciate that Bt toxins, even within a certain class such as Cry1F, will vary to some extent in length and the precise location of the transition from core toxin portion to protoxin portion. Typically, the Cry1Fa toxins are about 1150 to about 1200 amino acids in length. The transition from core toxin portion to protoxin portion will typically occur at between about 50% to about 60% of the full length toxin. The chimeric toxin of the subject invention will include the full expanse of this N-terminal core toxin portion. Thus, the chimeric toxin will comprise at least about 50% of the full length of the Cry1Fa Bt toxin protein. This will typically be at least about 590 amino acids. With regard to the protoxin portion, the full expanse of the Cry1Ab protoxin portion extends from the end of the core toxin portion to the C-terminus of the molecule. Genes and Toxins The genes and toxins useful according to the subject invention include not only the full length sequences disclosed but also fragments of these sequences, variants, mutants, and fusion proteins which retain the characteristic pesticidal activity of the toxins specifically exemplified herein. As used herein, the terms “variants” or “variations” of genes refer to nucleotide sequences which encode the same toxins or which encode equivalent toxins having pesticidal activity. As used herein, the term “equivalent toxins” refers to toxins having the same or essentially the same biological activity against the target pests as the claimed toxins. As used herein, the boundaries represent approximately 95% (Cry1Fa's and Vip3Ab's), 78% (Cry1F's and Vip3A's), and 45% (Cry1's and Vip3's) sequence identity, per “Revision of the Nomenclature for the Bacillus thuringiensis Pesticidal Crystal Proteins,” N. Crickmore, D. R. Zeigler, J. Feitelson, E. Schnepf, J. Van Rie, D. Lereclus, J. Baum, and D. H. Dean. Microbiology and Molecular Biology Reviews (1998) Vol 62: 807-813. These cut offs can also be applied to the core toxins only (for Cry1Fa, for example). It should be apparent to a person skilled in this art that genes encoding active toxins can be identified and obtained through several means. The specific genes or gene portions exemplified herein may be obtained from the isolates deposited at a culture depository. These genes, or portions or variants thereof, may also be constructed synthetically, for example, by use of a gene synthesizer. Variations of genes may be readily constructed using standard techniques for making point mutations. Also, fragments of these genes can be made using commercially available exonucleases or endonucleases according to standard procedures. For example, enzymes such as Bal31 or site-directed mutagenesis can be used to systematically cut off nucleotides from the ends of these genes. Genes that encode active fragments may also be obtained using a variety of restriction enzymes. Proteases may be used to directly obtain active fragments of these protein toxins. Fragments and equivalents which retain the pesticidal activity of the exemplified toxins would be within the scope of the subject invention. Also, because of the redundancy of the genetic code, a variety of different DNA sequences can encode the amino acid sequences disclosed herein. It is well within the skill of a person trained in the art to create these alternative DNA sequences encoding the same, or essentially the same, toxins. These variant DNA sequences are within the scope of the subject invention. As used herein, reference to “essentially the same” sequence refers to sequences which have amino acid substitutions, deletions, additions, or insertions which do not materially affect pesticidal activity. Fragments of genes encoding proteins that retain pesticidal activity are also included in this definition. A further method for identifying the genes encoding the toxins and gene portions useful according to the subject invention is through the use of oligonucleotide probes. These probes are detectable nucleotide sequences. These sequences may be detectable by virtue of an appropriate label or may be made inherently fluorescent as described in International Application No. WO93/16094. As is well known in the art, if the probe molecule and nucleic acid sample hybridize by forming a strong bond between the two molecules, it can be reasonably assumed that the probe and sample have substantial homology. Preferably, hybridization is conducted under stringent conditions by techniques well-known in the art, as described, for example, in Keller, G. H., M. M. Manak (1987) DNA Probes, Stockton Press, New York, N.Y., pp. 169-170. Some examples of salt concentrations and temperature combinations are as follows (in order of increasing stringency): 2×SSPE or SSC at room temperature; 1×SSPE or SSC at 42° C.; 0.1×SSPE or SSC at 42° C.; 0.1×SSPE or SSC at 65° C. Detection of the probe provides a means for determining in a known manner whether hybridization has occurred. Such a probe analysis provides a rapid method for identifying toxin-encoding genes of the subject invention. The nucleotide segments which are used as probes according to the invention can be synthesized using a DNA synthesizer and standard procedures. These nucleotide sequences can also be used as PCR primers to amplify genes of the subject invention. Variant Toxins Certain toxins of the subject invention have been specifically exemplified herein. Since these toxins are merely exemplary of the toxins of the subject invention, it should be readily apparent that the subject invention comprises variant or equivalent toxins (and nucleotide sequences coding for equivalent toxins) having the same or similar pesticidal activity of the exemplified toxin. Equivalent toxins will have amino acid homology with an exemplified toxin. This amino acid homology will typically be greater than 75%, preferably be greater than 90%, and most preferably be greater than 95%. The amino acid homology will be highest in critical regions of the toxin which account for biological activity or are involved in the determination of three-dimensional configuration which ultimately is responsible for the biological activity. In this regard, certain amino acid substitutions are acceptable and can be expected if these substitutions are in regions which are not critical to activity or are conservative amino acid substitutions which do not affect the three-dimensional configuration of the molecule. For example, amino acids may be placed in the following classes: non-polar, uncharged polar, basic, and acidic. Conservative substitutions whereby an amino acid of one class is replaced with another amino acid of the same type fall within the scope of the subject invention so long as the substitution does not materially alter the biological activity of the compound. Below is a listing of examples of amino acids belonging to each class. TABLE 1Class of Amino AcidExamples of Amino AcidsNonpolarAla, Val, Leu, Ile, Pro, Met, Phe, TrpUncharged PolarGly, Ser, Thr, Cys, Tyr, Asn, GlnAcidicAsp, GluBasicLys, Arg, His In some instances, non-conservative substitutions can also be made. The critical factor is that these substitutions must not significantly detract from the biological activity of the toxin. Recombinant Hosts. The genes encoding the toxins of the subject invention can be introduced into a wide variety of microbial or plant hosts. Expression of the toxin gene results, directly or indirectly, in the intracellular production and maintenance of the pesticide. Conjugal transfer and recombinant transfer can be used to create a Bt strain that expresses both toxins of the subject invention. Other host organisms may also be transformed with one or both of the toxin genes then used to accomplish the synergistic effect. With suitable microbial hosts, e.g., Pseudomonas , the microbes can be applied to the situs of the pest, where they will proliferate and be ingested. The result is control of the pest. Alternatively, the microbe hosting the toxin gene can be treated under conditions that prolong the activity of the toxin and stabilize the cell. The treated cell, which retains the toxic activity, then can be applied to the environment of the target pest. Where the Bt toxin gene is introduced via a suitable vector into a microbial host, and said host is applied to the environment in a living state, it is essential that certain host microbes be used. Microorganism hosts are selected which are known to occupy the “phytosphere” (phylloplane, phyllosphere, rhizosphere, and/or rhizoplane) of one or more crops of interest. These microorganisms are selected so as to be capable of successfully competing in the particular environment (crop and other insect habitats) with the wild-type microorganisms, provide for stable maintenance and expression of the gene expressing the polypeptide pesticide, and, desirably, provide for improved protection of the pesticide from environmental degradation and inactivation. A large number of microorganisms are known to inhabit the phylloplane (the surface of the plant leaves) and/or the rhizosphere (the soil surrounding plant roots) of a wide variety of important crops. These microorganisms include bacteria, algae, and fungi. Of particular interest are microorganisms, such as bacteria, e.g., genera Pseudomonas, Erwinia, Serratia, Klebsiella, Xanthomonas, Streptomyces, Rhizobium, Rhodopseudomonas, Methylophilius, Agrobactenum, Acetobacter, Lactobacillus, Arthrobacter, Azotobacter, Leuconostoc , and Alcaligenes ; fungi, particularly yeast, e.g., genera Saccharomyces, Cryptococcus, Kluyveromyces, Sporobolomyces, Rhodotorula , and Aureobasidium . Of particular interest are such phytosphere bacterial species as Pseudomonas syringae, Pseudomonas fluorescens, Serratia marcescens, Acetobacter xylinum, Agrobactenium tumefaciens, Rhodopseudomonas spheroides, Xanthomonas campestris, Rhizobium melioti, Alcaligenes entrophus , and Azotobacter vinlandii ; and phytosphere yeast species such as Rhodotorula rubra, R. glutinis, R. marina, R. aurantiaca, Cryptococcus albidus, C. diffluens, C. laurentii, Saccharomyces rosei, S. pretoriensis, S. cerevisiae, Sporobolomyces roseus, S. odorus, Kluyveromyces veronae , and Aureobasidium pollulans . Of particular interest are the pigmented microorganisms. A wide variety of methods is available for introducing a Bt gene encoding a toxin into a microorganism host under conditions which allow for stable maintenance and expression of the gene. These methods are well known to those skilled in the art and are described, for example, in U.S. Pat. No. 5,135,867, which is incorporated herein by reference. Treatment of Cells. Bacillus thuringiensis or recombinant cells expressing the Bt toxins can be treated to prolong the toxin activity and stabilize the cell. The pesticide microcapsule that is formed comprises the Bt toxin or toxins within a cellular structure that has been stabilized and will protect the toxin when the microcapsule is applied to the environment of the target pest. Suitable host cells may include either prokaryotes or eukaryotes, normally being limited to those cells which do not produce substances toxic to higher organisms, such as mammals. However, organisms which produce substances toxic to higher organisms could be used, where the toxic substances are unstable or the level of application sufficiently low as to avoid any possibility of toxicity to a mammalian host. As hosts, of particular interest will be the prokaryotes and the lower eukaryotes, such as fungi. The cell will usually be intact and be substantially in the proliferative form when treated, rather than in a spore form, although in some instances spores may be employed. Treatment of the microbial cell, e.g., a microbe containing the B.t. toxin gene or genes, can be by chemical or physical means, or by a combination of chemical and/or physical means, so long as the technique does not deleteriously affect the properties of the toxin, nor diminish the cellular capability of protecting the toxin. Examples of chemical reagents are halogenating agents, particularly halogens of atomic no. 17-80. More particularly, iodine can be used under mild conditions and for sufficient time to achieve the desired results. Other suitable techniques include treatment with aldehydes, such as glutaraldehyde; anti-infectives, such as zephiran chloride and cetylpyridinium chloride; alcohols, such as isopropyl and ethanol; various histologic fixatives, such as Lugol iodine, Bouin's fixative, various acids and Helly's fixative (See: Humason, Gretchen L., Animal Tissue Techniques, W. H. Freeman and Company, 1967); or a combination of physical (heat) and chemical agents that preserve and prolong the activity of the toxin produced in the cell when the cell is administered to the host environment. Examples of physical means are short wavelength radiation such as gamma-radiation and X-radiation, freezing, UV irradiation, lyophilization, and the like. Methods for treatment of microbial cells are disclosed in U.S. Pat. Nos. 4,695,455 and 4,695,462, which are incorporated herein by reference. The cells generally will have enhanced structural stability which will enhance resistance to environmental conditions. Where the pesticide is in a proform, the method of cell treatment should be selected so as not to inhibit processing of the proform to the mature form of the pesticide by the target pest pathogen. For example, formaldehyde will crosslink proteins and could inhibit processing of the proform of a polypeptide pesticide. The method of treatment should retain at least a substantial portion of the bio-availability or bioactivity of the toxin. Characteristics of particular interest in selecting a host cell for purposes of production include ease of introducing the B.t. gene or genes into the host, availability of expression systems, efficiency of expression, stability of the pesticide in the host, and the presence of auxiliary genetic capabilities. Characteristics of interest for use as a pesticide microcapsule include protective qualities for the pesticide, such as thick cell walls, pigmentation, and intracellular packaging or formation of inclusion bodies; survival in aqueous environments; lack of mammalian toxicity; attractiveness to pests for ingestion; ease of killing and fixing without damage to the toxin; and the like. Other considerations include ease of formulation and handling, economics, storage stability, and the like. Growth of Cells. The cellular host containing the B.t. insecticidal gene or genes may be grown in any convenient nutrient medium, where the DNA construct provides a selective advantage, providing for a selective medium so that substantially all or all of the cells retain the B.t. gene. These cells may then be harvested in accordance with conventional ways. Alternatively, the cells can be treated prior to harvesting. The B.t. cells producing the toxins of the invention can be cultured using standard art media and fermentation techniques. Upon completion of the fermentation cycle the bacteria can be harvested by first separating the B.t. spores and crystals from the fermentation broth by means well known in the art. The recovered B.t. spores and crystals can be formulated into a wettable powder, liquid concentrate, granules or other formulations by the addition of surfactants, dispersants, inert carriers, and other components to facilitate handling and application for particular target pests. These formulations and application procedures are all well known in the art. Formulations. Formulated bait granules containing an attractant and spores, crystals, and toxins of the B.t. isolates, or recombinant microbes comprising the genes obtainable from the B.t. isolates disclosed herein, can be applied to the soil. Formulated product can also be applied as a seed-coating or root treatment or total plant treatment at later stages of the crop cycle. Plant and soil treatments of B.t. cells may be employed as wettable powders, granules or dusts, by mixing with various inert materials, such as inorganic minerals (phyllosilicates, carbonates, sulfates, phosphates, and the like) or botanical materials (powdered corncobs, rice hulls, walnut shells, and the like). The formulations may include spreader-sticker adjuvants, stabilizing agents, other pesticidal additives, or surfactants. Liquid formulations may be aqueous-based or non-aqueous and employed as foams, gels, suspensions, emulsifiable concentrates, or the like. The ingredients may include rheological agents, surfactants, emulsifiers, dispersants, or polymers. As would be appreciated by a person skilled in the art, the pesticidal concentration will vary widely depending upon the nature of the particular formulation, particularly whether it is a concentrate or to be used directly. The pesticide will be present in at least 1% by weight and may be 100% by weight. The dry formulations will have from about 1-95% by weight of the pesticide while the liquid formulations will generally be from about 1-60% by weight of the solids in the liquid phase. The formulations will generally have from about 10 2 to about 10 4 cells/mg. These formulations will be administered at about 50 mg (liquid or dry) to 1 kg or more per hectare. The formulations can be applied to the environment of the lepidopteran pest, e.g., foliage or soil, by spraying, dusting, sprinkling, or the like. Plant Transformation. A preferred recombinant host for production of the insecticidal proteins of the subject invention is a transformed plant. Genes encoding Bt toxin proteins, as disclosed herein, can be inserted into plant cells using a variety of techniques which are well known in the art. For example, a large number of cloning vectors comprising a replication system in Escherichia coli and a marker that permits selection of the transformed cells are available for preparation for the insertion of foreign genes into higher plants. The vectors comprise, for example, pBR322, pUC series, M13mp series, pACYC184, inter alia. Accordingly, the DNA fragment having the sequence encoding the Bt toxin protein can be inserted into the vector at a suitable restriction site. The resulting plasmid is used for transformation into E. coli . The E. coli cells are cultivated in a suitable nutrient medium, then harvested and lysed. The plasmid is recovered. Sequence analysis, restriction analysis, electrophoresis, and other biochemical-molecular biological methods are generally carried out as methods of analysis. After each manipulation, the DNA sequence used can be cleaved and joined to the next DNA sequence. Each plasmid sequence can be cloned in the same or other plasmids. Depending on the method of inserting desired genes into the plant, other DNA sequences may be necessary. If, for example, the Ti or Ri plasmid is used for the transformation of the plant cell, then at least the right border, but often the right and the left border of the Ti or Ri plasmid T-DNA, has to be joined as the flanking region of the genes to be inserted. The use of T-DNA for the transformation of plant cells has been intensively researched and sufficiently described in EP 120 516, Lee and Gelvin (2008), Hoekema (1985), Fraley et al., (1986), and An et al., (1985), and is well established in the art. Once the inserted DNA has been integrated in the plant genome, it is relatively stable. The transformation vector normally contains a selectable marker that confers on the transformed plant cells resistance to a biocide or an antibiotic, such as Bialaphos, Kanamycin, G418, Bleomycin, or Hygromycin, inter alia. The individually employed marker should accordingly permit the selection of transformed cells rather than cells that do not contain the inserted DNA. A large number of techniques are available for inserting DNA into a plant host cell. Those techniques include transformation with T-DNA using Agrobacterium tumefaciens or Agrobacterium rhizogenes as transformation agent, fusion, injection, biolistics (microparticle bombardment), or electroporation as well as other possible methods. If Agrobacteria are used for the transformation, the DNA to be inserted has to be cloned into special plasmids, namely either into an intermediate vector or into a binary vector. The intermediate vectors can be integrated into the Ti or Ri plasmid by homologous recombination owing to sequences that are homologous to sequences in the T-DNA. The Ti or Ri plasmid also comprises the vir region necessary for the transfer of the T-DNA. Intermediate vectors cannot replicate themselves in Agrobacteria . The intermediate vector can be transferred into Agrobacterium tumefaciens by means of a helper plasmid (conjugation). Binary vectors can replicate themselves both in E. coli and in Agrobacteria . They comprise a selection marker gene and a linker or polylinker which are framed by the Right and Left T-DNA border regions. They can be transformed directly into Agrobacteria (Holsters et al., 1978). The Agrobacterium used as host cell is to comprise a plasmid carrying a vir region. The vir region is necessary for the transfer of the T-DNA into the plant cell. Additional T-DNA may be contained. The bacterium so transformed is used for the transformation of plant cells. Plant explants can advantageously be cultivated with Agrobacterium tumefaciens or Agrobacterium rhizogenes for the transfer of the DNA into the plant cell. Whole plants can then be regenerated from the infected plant material (for example, pieces of leaf, segments of stalk, roots, but also protoplasts or suspension-cultivated cells) in a suitable medium, which may contain antibiotics or biocides for selection. The plants so obtained can then be tested for the presence of the inserted DNA. No special demands are made of the plasmids in the case of injection and electroporation. It is possible to use ordinary plasmids, such as, for example, pUC derivatives. The transformed cells grow inside the plants in the usual manner. They can form germ cells and transmit the transformed trait(s) to progeny plants. Such plants can be grown in the normal manner and crossed with plants that have the same transformed hereditary factors or other hereditary factors. The resulting hybrid individuals have the corresponding phenotypic properties. In a preferred embodiment of the subject invention, plants will be transformed with genes wherein the codon usage has been optimized for plants. See, for example, U.S. Pat. No. 5,380,831, which is hereby incorporated by reference. While some truncated toxins are exemplified herein, it is well-known in the Bt art that 130 kDa-type (full-length) toxins have an N-terminal half that is the core toxin, and a C-terminal half that is the protoxin “tail.” Thus, appropriate “tails” can be used with truncated/core toxins of the subject invention. See e.g. U.S. Pat. No. 6,218,188 and U.S. Pat. No. 6,673,990. In addition, methods for creating synthetic Bt genes for use in plants are known in the art (Stewart and Burgin, 2007). One non-limiting example of a preferred transformed plant is a fertile maize plant comprising a plant expressible gene encoding a Cry1Fa protein, and further comprising a second plant expressible gene encoding a Vip3Ab protein. Transfer (or introgression) of the Cry1Fa- and Vip3Ab-determined trait(s) into inbred maize lines can be achieved by recurrent selection breeding, for example by backcrossing. In this case, a desired recurrent parent is first crossed to a donor inbred (the non-recurrent parent) that carries the appropriate gene(s) for the Cry1F- and Vip3Ab-determined traits. The progeny of this cross is then mated back to the recurrent parent followed by selection in the resultant progeny for the desired trait(s) to be transferred from the non-recurrent parent. After three, preferably four, more preferably five or more generations of backcrosses with the recurrent parent with selection for the desired trait(s), the progeny will be heterozygous for loci controlling the trait(s) being transferred, but will be like the recurrent parent for most or almost all other genes (see, for example, Poehlman & Sleper (1995) Breeding Field Crops, 4th Ed., 172-175; Fehr (1987) Principles of Cultivar Development, Vol. 1: Theory and Technique, 360-376). Insect Resistance Management (IRM) Strategies. Roush et al., for example, outlines two-toxin strategies, also called “pyramiding” or “stacking,” for management of insecticidal transgenic crops. (The Royal Society. Phil. Trans. R. Soc. Lond. B. (1998) 353, 1777-1786). On their website, the United States Environmental Protection Agency (epa.gov/oppbppdl/biopesticides/pips/bt_corn_refuge — 2006.htm) publishes the following requirements for providing non-transgenic (i.e., non-B.t.) refuges (a section of non-Bt crops/corn) for use with transgenic crops producing a single Bt protein active against target pests. “The specific structured requirements for corn borer-protected Bt (Cry1Ab or Cry1F) corn products are as follows:Structured refuges: 20% non-Lepidopteran Bt corn refuge in Corn Belt; 50% non-Lepidopteran Bt refuge in Cotton BeltBlocks Internal (i.e., within the Bt field)External (i.e., separate fields within ½ mile (¼ mile if possible) of theBt field to maximize random mating)In-Field Strips Strips must be at least 4 rows wide (preferably 6 rows) to reduce the effects of larval movement” In addition, the National Corn Growers Association, on their website: (ncga.com/insect-resistance-management-fact-sheet-bt-corn) also provides similar guidance regarding the refuge requirements. For example: “Requirements of the Corn Borer IRM:Plant at least 20% of your corn acres to refuge hybridsIn cotton producing regions, refuge must be 50%Must be planted within ½ mile of the refuge hybridsRefuge can be planted as strips within the Bt field; the refuge strips must be at least 4 rows wideRefuge may be treated with conventional pesticides only if economic thresholds are reached for target insectBt-based sprayable insecticides cannot be used on the refuge cornAppropriate refuge must be planted on every farm with Bt corn” As stated by Roush et al. (on pages 1780 and 1784 right column, for example), stacking or pyramiding of two different proteins each effective against the target pests and with little or no cross-resistance can allow for use of a smaller refuge. Roush suggests that for a successful stack, a refuge size of less than 10% refuge, can provide comparable resistance management to about 50% refuge for a single (non-pyramided) trait. For currently available pyramided Bt corn products, the U.S. Environmental Protection Agency requires significantly less (generally 5%) structured refuge of non-Bt corn be planted than for single trait products (generally 20%). There are various ways of providing the IRM effects of a refuge, including various geometric planting patterns in the fields (as mentioned above) and in-bag seed mixtures, as discussed further by Roush et al. (supra), and U.S. Pat. No. 6,551,962. The above percentages, or similar refuge ratios, can be used for the subject double or triple stacks or pyramids. For triple stacks with three modes of action against a single target pest, a goal would be zero refuge (or less than 5% refuge, for example). This is particularly true for commercial acreage—of over 10 acres for example. All patents, patent applications, provisional applications, and publications referred to or cited herein are incorporated by reference in their entirety to the extent they are not inconsistent with the explicit teachings of this specification. Unless specifically indicated or implied, the terms “a”, “an”, and “the” signify “at least one” as used herein. Following are examples that illustrate procedures for practicing the invention. These examples should not be construed as limiting. All percentages are by weight and all solvent mixture proportions are by volume unless otherwise noted. All temperatures are in degrees Celsius. EXAMPLES Example 1 Summary of Examples Examples are given showing that Vip3Ab1 is active against Spodoptera frugiperda (fall armyworm) wild type larvae, and against a field collected strain of Spodoptera frugiperda found in Puerto Rico that is resistant to the Bacillus thuringiensis crystal toxin Cry1Fa. This biological data supports the utility of Vip3Ab1 to be used to combat the development of Cry1 resistance in insects, since insects developing resistance to the Cry1Fa toxins would continue to be susceptible to the toxicity of Vip3Ab1. Similarly, in Spodoptera frugiperda, 125 I radiolabeled Cry1Fa binds to receptor proteins and the binding can be displaced using non-radiolabeled Cry1Fa. However, Vip3Ab1 cannot displace the binding of 125 I Cry1Fa from its receptor in these experiments. These results indicate that Vip3Ab1 has a unique binding site as compared to Cry1Fa. The ability of Vip3Ab1 to exert toxicity against insects that are resistant to Cry1Fa stems from its demonstrated non-interaction at the site where these toxins bind. Further data is presented that shows the nature of Cry1Fa resistance in Spodoptera frugiperda is due to the inability of Cry1Fa to bind to BBMV's prepared from this insect. The biological activity of Vip3Ab1 against Cry1Fa resistant S. frugiperda larvae that lost their ability to bind Cry1Fa, further supports the non-interacting target site of Vip3Ab1 as compared to Cry1Fa. Example 2 Purification and Trypsin Processing of Cry1Fa and Vip3Ab1 Proteins The genes encoding the Cry1Fa and Vip3Ab1 pro toxins were expressed in Pseudomonas fluorescens expression strains and the full length proteins isolated as insoluble inclusion bodies. The washed inclusion bodies were solubilized by stirring at 37° C. in buffer containing 20 mM CAPS buffer, pH 11, +10 mM DDT, +0.1% 2-mercaptoethanol, for 2 hrs. The solution was centrifuged at 27,000×g for 10 min. at 37° C. and the supernatant treated with 0.5% (w/v) TCPK treated trypsin (Sigma). This solution was incubated with mixing for an additional 1 hr. at room temperature, filtered, then loaded onto a Pharmacia Mono Q 1010 column equilibrated with 20 mM CAPS pH 10.5. After washing the loaded column with 2 column volumes of buffer, the truncated toxin was eluted using a linear gradient of 0 to 0.5 M NaCl in 20 mM CAPS in 15 column volumes at a flow rate of 1.0 ml/min. Purified trypsin truncated Cry proteins eluted at about 0.2-0.3 M NaCl. The purity of the proteins was checked by SDS PAGE and with visualization using Coomassie brilliant blue dye. In some cases, the combined fractions of the purified toxin were concentrated and loaded onto a Superose 6 column (1.6 cm dia., 60 cm long), and further purified by size exclusion chromatography. Fractions comprising a single peak of the monomeric molecular weight were combined, and concentrated, resulting in a preparation more than 95% homogeneous for a protein having a molecular weight of about 60,000 kDa. Processing of Vip3Ab1 was achieved in a similar manner starting with the purified full length 85 kDa protein (DIG-307) provided by Monte Badger. The protein (12 mg) was dialyzed into 50 mM sodium phosphate buffer, pH 8.4, then processed by adding 1 mg of solid trypsin and incubating for 1 hrs. at room temperature. The solution was loaded onto a MonoQ anion exchange column (1 cm dia., 10 cm. long), and eluted with a linear gradient of NaCl from 0 to 500 mM in 20 mM sodium phosphate buffer, pH 8.4 over 7 column volumes. Elution of the protein was monitored by SDS-PAGE. The major processed band had a molecular weight of 65 kDa, as determined by SDS-PAGE using molecular weight standards for comparison. Example 3 Insect Bioassays Purified proteins were tested for insecticidal activity in bioassays conducted with neonate Spodoptera frugiperda (J. E. Smith) larvae on artificial insect diet. The Cry1F-resistant FAW were collected from fields of Herculex I (Cry1Fa) corn in Puerto Rico, and brought into the Dow AgroSciences Insectary for continuous rearing. Characterization of this strain of resistant-FAW is outlined in the internal report by Schlenz, et al (Schlenz et al., 2008). Insect bioassays were conducted in 128-well plastic bioassay trays (C-D International, Pitman, N.J.). Each well contained 0.5 mL of multi-species lepidoptera diet (Southland Products, Lake Village, Ark.). A 40 μL aliquot of the purified Cry or Vip3Ab1 protein diluted to various concentrations in 10 mM CAPS, pH 10.5, or control solution was delivered by pipette onto the 1.5 cm 2 diet surface of each well (26.7 μL/cm 2 ). Sixteen wells were tested per sample. The negative control was a buffer solution blank containing no protein. Positive controls included preparations of Cry1F. The treated trays were held in a fume hood until the liquid on the diet surface had evaporated or was absorbed into the diet. Within a few hours of eclosion, individual larvae were picked up with a moistened camelhair brush and deposited on the treated diet, one larva per well. The infested wells were then sealed with adhesive sheets of clear plastic that are vented to allow gas exchange (C-D International, Pitman, N.J.). The bioassay trays were held under controlled environmental conditions (28° C., ˜40% RH, 16:8 [L:D] photoperiod). After 5 days, the total number of insects exposed to each protein sample, the number of dead insects, and the weight of surviving insects were recorded. Example 4 Iodination of Cry1Fa Toxins Iodination of Cry1F has been reported to destroy both the toxicity and the binding capacity of this protein when tested against tobacco budworm larvae and BBMV's prepared from these insects (Luo et al., 1999; Sheets and Storer, 2001). The inactivation is presumably due to the need for unmodified tyrosine residues near its binding site. When Cry1F was iodinated using the Iodo-bead method, the protein lost all of its ability to exhibit specific binding characteristics using BBMV's from H. virescens . Using non-radiolabeled NaI to iodinate Cry1F employing the Iodo-bead method, the iodinated Cry1F also lost its insecticidal activity against H. virescens. Earlier studies in our laboratories demonstrated that Cry1Fa could be fluorescently labeled using maleimide conjugated labeling reagents that specifically alkylate proteins at cysteine residues. Since the Cry1Fa trypsin core toxin contains a single cysteine residue at position 205, labeling the protein with such a reagent would result in alkylation of the protein at a single specific site. It was determined that Cry1Fa could be fluorescently labeled with fluorescein-5-maleimide and that the labeled protein retained insecticidal activity. Based upon the retention of biological activity of the cysteine fluorescein labeled Cry1Fa, it was determined that we could also radioiodinate the fluorescein portion of the label by the method of Palmer et al., (Palmer et al., 1997), and attach it to the cysteine of Cry1Fa and have a radiolabeled Cry1Fa that retains biological activity. Fluorescein-5-maleimide was dissolved to 10 mM (4.27 mg/ml) in DMSO, then diluted to 1 mM in PBS as determined by its molar extinction coefficient of 68,000 M −1 cm −1 . To a 70 μl solution of PBS containing two Iodobeads, 0.5 mCi of Na 125 I was added behind lead shielding. The solution was allowed to mix at room temperature for 5 min., then 10 μl of the 1 mM fluorescein-5-maleimide was added. The reactants were allowed to react for 10 min., and then removed from the iodobeads. To the reacted solution was added 2 μg of highly purified trypsin truncated Cry1Fa core toxin in PBS. The protein was incubated with the iodinated fluorescein-5-maleimide solution for 48 hrs at 4° C. The reaction was stopped by adding 2-mercapto ethanol to 14 mM. The reaction mixture was then added to a Zebra spin column equilibrated in 20 mM CAPS, 150 mM KCl, pH 9, and centrifuged at 1,500×g for 2 min. to separate non-reacted iodinated dye from the protein. The 125 I radiolabeled fluorescein-Cry1Fa was counted in a gamma counter to determine its specific activity determined based upon an assumed 80% recovery of the input toxin. The protein was also characterized by SDS-PAGE and visualized by phosphor imaging to assure that the radioactivity measured was covalently associated with the Cry1Fa protein. Example 5 Preparation and Fractionation of Solubilized BBMV's Standard methods of protein quantification and SDS-polyacrylamide gel electrophoresis were employed as taught, for example, in Sambrook et al. (Sambrook and Russell, 2001) and updates thereof. Last instar S. frugiperda larvae were fasted overnight and then dissected after chilling on ice for 15 minutes. The midgut tissue was removed from the body cavity, leaving behind the hindgut attached to the integument. The midgut was placed in a 9× volume of ice cold homogenization buffer (300 mM mannitol, 5 mM EGTA, 17 mM Tris base, pH7.5), supplemented with Protease Inhibitor Cocktail (Sigma-Aldrich P-2714) diluted as recommended by the supplier. The tissue was homogenized with 15 strokes of a glass tissue homogenizer. BBMV's were prepared by the MgCl 2 precipitation method of Wolfersberger (Wolfersberger, 1993). Briefly, an equal volume of a 24 mM MgCl 2 solution in 300 mM mannitol was mixed with the midgut homogenate, stirred for 5 minutes and allowed to stand on ice for 15 min. The solution was centrifuged at 2,500×g for 15 min at 4° C. The supernatant was saved and the pellet suspended into the original volume of 0.5× diluted homogenization buffer and centrifuged again. The two supernatants were combined and centrifuged at 27,000×g for 30 min at 4° C. to form the BBMV fraction. The pellet was suspended into BBMV Storage Buffer (10 mM HEPES, 130 mM KCl, 10% glycerol, pH 7.4) to a concentration of about 3 mg/ml protein. Protein concentration was determined using BSA as the standard. L-leucine-p-nitroanilide aminopeptidase activity (a marker enzyme for the BBMV fraction) was determined prior to freezing the samples. Briefly, 50 μl of L-leucine-p-nitroanilide (1 mg/ml in PBS) was added to 940 ml 50 mM Tris HCl in a standard cuvette. The cuvette was placed in a Cary 50 Bio spectrophotometer, zeroed for absorbance reading at 405 nm, and the reaction initiated by adding 10 μl of either insect midgut homogenate or insect BBMV preparation. The increase in absorbance at 405 nm was monitored for 5 minutes at room temperature. The specific activity of the homogenate and BBMV preparations was determined based upon the kinetics of the absorbance increase over time during a linear increase in absorbance per unit total protein added to the assay based upon the following equation: ΔOD/(min*mg)=Aminopeptidase Rate(ΔOD/ml*min)/[protein](mg/ml) The specific activity of this enzyme typically increased 7-fold compared to that found in the starting midgut homogenate fraction. The BBMV's were aliquoted into 250 μl samples, flash frozen in liquid N 2 and stored at −80° C. Example 6 Electrophoresis Analysis of proteins by SDS-PAGE was conducted under reducing (i.e. in 5% β-mercaptoethanol, BME) and denaturing (i.e. heated 5 minutes at 90° in the presence of 4% SDS) conditions. Proteins were loaded into wells of a 4% to 20% tris-glycine polyacrylamide gel (BioRad; Hercules, Calif.) and separated at 200 volts for 60 minutes. Protein bands were detected by staining with Coomassie Brilliant Blue R-250 (BioRad) for one hour, and destained with a solution of 5% methanol in 7% acetic acid. The gels were imaged and analyzed using a BioRad Fluoro-S Multi Imager™. Relative molecular weights of the protein bands were determined by comparison to the mobilities of known molecular weight proteins observed in a sample of BenchMark™ Protein Ladder (Invitrogen, Carlsbad, Calif.) loaded into one well of the gel. Example 7 Imaging Radio-purity of the iodinated Cry proteins and measurement of radioactive Cry1Fa in pull down assays was determined by SDS-PAGE and phosphorimaging. Briefly, SDS-PAGE gels were imaged by wrapping the gels in Mylar film (12 μm thick), after separation and fixation of the protein, then exposing the gel under a Molecular Dynamics storage phosphor screen (35 cm×43 cm) for at least overnight, and up to 4 days. The plates were developed using a Molecular Dynamics Storm 820 phosphor-imager and the image was analyzed using ImageQuant™ software. Example 8 Summary of Results Mortality results from bioassays of the full length Vip3Ab1 protein tested at a variety of doses against wild type and Cry1Fa resistant S. frugiperda larvae are shown in FIG. 1 . Against wild type S. frugiperda larvae, we obtained 100% mortality at the highest concentration tested (9,000 ng/cm 2 ), and lower levels of mortality at lower doses. The LC-50 was estimated at about 2,000 ng/cm 2 . Vip3Ab1 was highly effective against S. frugiperda in inhibiting growth of the larvae, with greater than 95% growth inhibition at concentrations of 1,000 ng/cm 2 and higher. The high level of growth inhibition observed for both S. frugiperda larvae suggests that these insects would most likely progress to mortality if left for a longer time period. A bioassay was also conducted to compare the biological activity of Vip3Ab1 against wild type S. frugiperda versus Cry1Fa resistant S. frugiperda ( FIG. 1 ). Percent growth inhibition is indicated by the vertical bars, and percent mortality by the diamond symbols. Mortality measured 5 days after exposure to the toxin was below 50% for both insect types at all concentrations tested. A clear dose response was obtained for growth inhibition. Vip3Ab1 resulted in >95% inhibition of larval growth of both Cry1Fa sensitive and Cry1Fa resistant S. frugiperda larvae at concentrations above 1,000 ng/cm 2 , and resulted in about 50% inhibition of larval growth of the wild type S. frugiperda at approximately 40 ng/cm 2 . Vip3Ab1 resulted in more than 50% growth inhibition of Cry1Fa resistant S. frugiperda at all concentrations tested, down to the lowest of 4.1 ng/cm 2 . Thus, Vip3Ab1 has high activity against Cry1Fa resistant S. frugiperda larvae. Additional bioassay replications were conducted to generate median lethal concentrations (LC50), median growth inhibition concentrations. Table 2 shows (GI50) and 95% confidence intervals of Cry1F-suseptible Spodoptera frugiperda and Cry1F-resistant Spodoptera frugiperda to Vip3Ab1 compared to controls. TABLE 2InsectLC-5095% CIGI-595% CIFAW3966.3(2150.3-9406.6)21.9(18.5-25.6)Cry1Fa pos57.3(43.6-77.4)<13ctrl vs FAWrFAW499.9(338.9-748.6)7.7(5.5-10.7)Cry1Fa posno mortality seen withinno growth inhibition seenctrl vs rFAWeach tested dosewithin each tested doseBufferno mortalityAVG. Wt53.2 mg (FAW)(FAW,per insect38.3 mg (rFAW)rFAW)Waterno mortalityAVG. Wt53.1 mg (FAW)(FAW,per insect35.9 mg (rFAW)rFAW) Radiolabeled competition binding assays were conducted to determine if Vip3Ab1 interacts at the same site that Cry1Fa binds in FAW. A competition assay was developed to measure the ability of Vip3Ab to compete with the binding of 125 I radiolabeled Cry1Fa. FIG. 2 shows the phosphorimage of radioactive Cry1Fa separated by SDS-PAGE after binding to BBMV proteins. In the absence of any competing ligands, 125 I Cry1Fa can be detected associated with the BBMV protein. When incubated in the presence of 1,000 nM unlabeled Cry1Fa (500-fold excess compared to the concentration of labeled protein used in the assay), very little radioactivity is detected corresponding to 125 I Cry1Fa. Thus, this result shows that the unlabeled Cry1Fa effectively competes with the radiolabeled Cry1Fa for binding to the receptor proteins, as would be expected since these homologous proteins bind to the same site. When the same experiment is conducted using 1,000 nM unlabeled Vip3Ab1 protein as the competing protein, we see no change in the level of 125 I Cry1Fa binding to the BBMV proteins from S. frugiperda , indicating that Vip3Ab1 does not compete with the binding of 125 I Cry1Fa. This result is interpreted to indicate that Vip3Ab1 does not bind at the same site as Cry1Fa. Insects can develop resistance to the toxicity of Cry proteins through a number of different biochemical mechanisms, but the most common mechanism is due to a reduction in the ability of the Cry toxin protein to bind to its specific receptor in the gut of the insect (Heckel et al., 2007; Tabashnik et al., 2000; Xu et al., 2005). This can be brought about thought small point mutations, large gene deletions, or though other genetic or biochemical mechanisms. When we investigated the BBMV proteins from Cry1Fa resistant S. frugiperda to understand the nature of their resistance to Cry1Fa, we discovered that BBMV's prepared from Cry1Fa resistant insects were much less able to bind 125 I radiolabeled Cry1Fa as compared to BBMV's prepared from the wild type insects ( FIG. 3 ). Thus, the mechanism of resistance to Cry1Fa in S. frugiperda is due to a greatly reduced level of binding of Cry1Fa to the BBMV's from the resistant insects. Since we show in FIG. 2 that Vip3Ab1 does not compete with the binding of Cry1Fa, this further demonstrates that the Vip3Ab1 should not be affected by a resistance mechanism that is involved with the binding of Cry1Fa to its specific receptor. This is born out in the bioassays. Thus, Vip3Ab1 complements the activity of Cry1Fa, in that it has biological activity against similar insects, yet does not bind to the same receptor sites as these Cry proteins, and thus is not affected by resistance mechanisms that would involve reduction of Cry toxin binding. We concluded from these studies that Vip3Ab1 is an excellent insect toxin to combine with Cry1Fa as an insect resistance management approach to provide biological activity against insects that may have developed resistance to either one of these proteins, and also to prevent resistant insects. REFERENCE LIST Heckel, D. G., Gahan, L. J., Baxter, S. W., Zhao, J. Z., Shelton, A. M., Gould, F., and Tabashnik, B. E. (2007). The diversity of Bt resistance genes in species of Lepidoptera. J Invertebr Pathol 95, 192-197.Luo, K., Banks, D., and Adang, M. J. (1999). Toxicity, binding, and permeability analyses of four bacillus thuringiensis cryl delta-endotoxins using brush border membrane vesicles of spodoptera exigua and spodoptera frugiperda . Appl. Environ. Microbiol. 65, 457-464.Palmer, M., Buchkremer, M, Valeva, A, and Bhakdi, S. Cysteine-specific radioiodination of proteins with fluorescein maleimide. Analytical Biochemistry 253, 175-179. 1997. 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APPENDIX AList of delta-endotoxins - from Crickmore et al. website (cited in application)Accession Number is to NCBI entryNameAcc No.AuthorsYearSource StrainCommentCry1Aa1AAA22353Schnepf et al1985Bt kurstaki HD1Cry1Aa2AAA22552Shibano et al1985Bt sottoCry1Aa3BAA00257Shimizu et al1988Bt aizawai IPL7Cry1Aa4CAA31886Masson et al1989Bt entomocidusCry1Aa5BAA04468Udayasuriyan et al1994Bt Fu-2-7Cry1Aa6AAA86265Masson et al1994Bt kurstaki NRD-12Cry1Aa7AAD46139Osman et al1999Bt C12Cry1Aa8I26149Liu1996DNA sequence onlyCry1Aa9BAA77213Nagamatsu et al1999Bt dendrolimusT84A1Cry1Aa10AAD55382Hou and Chen1999Bt kurstaki HD-1-02Cry1Aa11CAA70856Tounsi et al1999Bt kurstakiCry1Aa12AAP80146Yao et al2001Bt Ly30Cry1Aa13AAM44305Zhong et al2002Bt sottoCry1Aa14AAP40639Ren et al2002unpublishedCry1Aa15AAY66993Sauka et al2005Bt INTA Mol-12Cry1Ab1AAA22330Wabiko et al1986Bt berliner 1715Cry1Ab2AAA22613Thorne et al1986Bt kurstakiCry1Ab3AAA22561Geiser et al1986Bt kurstaki HD1Cry1Ab4BAA00071Kondo et al1987Bt kurstaki HD1Cry1Ab5CAA28405Hofte et al1986Bt berliner 1715Cry1Ab6AAA22420Hefford et al1987Bt kurstaki NRD-12Cry1Ab7CAA31620Haider & Ellar1988Bt aizawai IC1Cry1Ab8AAA22551Oeda et al1987Bt aizawai IPL7Cry1Ab9CAA38701Chak & Jen1993Bt aizawai HD133Cry1Ab10A29125Fischhoff et al1987Bt kurstaki HD1Cry1Ab11I12419Ely & Tippett1995Bt A20DNA sequence onlyCry1Ab12AAC64003Silva-Werneck et al1998Bt kurstaki S93Cry1Ab13AAN76494Tan et al2002Bt c005Cry1Ab14AAG16877Meza-Basso &2000Native Chilean BtTheodulozCry1Ab15AAO13302Li et al2001Bt B-Hm-16Cry1Ab16AAK55546Yu et al2002Bt AC-11Cry1Ab17AAT46415Huang et al2004Bt WB9Cry1Ab18AAQ88259Stobdan et al2004BtCry1Ab19AAW31761Zhong et al2005Bt X-2Cry1Ab20ABB72460Liu et al2006BtC008Cry1Ab21ABS18384Swiecicka et al2007Bt IS5056Cry1Ab22ABW87320Wu and Feng2008BtS2491AbCry1Ab-AAK14336Nagarathinam et al2001Bt kunthala RX24uncertain sequencelikeCry1Ab-AAK14337Nagarathinam et al2001Bt kunthala RX28uncertain sequencelikeCry1Ab-AAK14338Nagarathinam et al2001Bt kunthala RX27uncertain sequencelikeCry1Ab-ABG88858Lin et al2006Bt ly4a3insufficient sequencelikeCry1Ac1AAA22331Adang et al1985Bt kurstaki HD73Cry1Ac2AAA22338Von Tersch et al1991Bt kenyaeCry1Ac3CAA38098Dardenne et al1990Bt BTS89ACry1Ac4AAA73077Feitelson1991Bt kurstakiPS85A1Cry1Ac5AAA22339Feitelson1992Bt kurstakiPS81GGCry1Ac6AAA86266Masson et al1994Bt kurstaki NRD-12Cry1Ac7AAB46989Herrera et al1994Bt kurstaki HD73Cry1Ac8AAC44841Omolo et al1997Bt kurstaki HD73Cry1Ac9AAB49768Gleave et al1992Bt DSIR732Cry1Ac10CAA05505Sun1997Bt kurstaki YBT-1520Cry1Ac11CAA10270Makhdoom &1998RiazuddinCry1Ac12I12418Ely & Tippett1995Bt A20DNA sequence onlyCry1Ac13AAD38701Qiao et al1999Bt kurstaki HD1Cry1Ac14AAQ06607Yao et al2002Bt Ly30Cry1Ac15AAN07788Tzeng et al2001Bt from TaiwanCry1Ac16AAU87037Zhao et al2005Bt H3Cry1Ac17AAX18704Hire et al2005Bt kenyae HD549Cry1Ac18AAY88347Kaur & Allam2005Bt SK-729Cry1Ac19ABD37053Gao et al2005Bt C-33Cry1Ac20ABB89046Tan et al2005Cry1Ac21AAY66992Sauka et al2005INTA Mol-12Cry1Ac22ABZ01836Zhang & Fang2008Bt W015-1Cry1Ac23CAQ30431Kashyap et al2008BtCry1Ac24ABL01535Arango et al2008Bt 146-158-01Cry1Ac25FJ513324Guan Peng et al2008Bt Tm37-6No NCBI link July 09Cry1Ac26FJ617446Guan Peng et al2009Bt Tm41-4No NCBI link July 09Cry1Ac27FJ617447Guan Peng et al2009Bt Tm44-1BNo NCBI link July 09Cry1Ac28ACM90319Li et al2009Bt Q-12Cry1Ad1AAA22340Feitelson1993Bt aizawai PS81ICry1Ad2CAA01880Anonymous1995Bt PS81RR1Cry1Ae1AAA22410Lee & Aronson1991Bt alestiCry1Af1AAB82749Kang et al1997Bt NT0423Cry1Ag1AAD46137Mustafa1999Cry1Ah1AAQ14326Tan et al2000Cry1Ah2ABB76664Qi et al2005Bt alestiCry1Ai1AAO39719Wang et al2002Cry1A-AAK14339Nagarathinam et al2001Bt kunthala nags3uncertain sequencelikeCry1Ba1CAA29898Brizzard & Whiteley1988Bt thuringiensisHD2Cry1Ba2CAA65003Soetaert1996Bt entomocidusHD110Cry1Ba3AAK63251Zhang et al2001Cry1Ba4AAK51084Nathan et al2001Bt entomocidusHD9Cry1Ba5ABO20894Song et al2007Bt sfw-12Cry1Ba6ABL60921Martins et al2006Bt S601Cry1Bb1AAA22344Donovan et al1994Bt EG5847Cry1Bc1CAA86568Bishop et al1994Bt morrisoniCry1Bd1AAD10292Kuo et al2000Bt wuhanensisHD525Cry1Bd2AAM93496Isakova et al2002Bt 834Cry1Be1AAC32850Payne et al1998Bt PS158C2Cry1Be2AAQ52387Baum et al2003Cry1Be3FJ716102Xiaodong Sun et al2009BtNo NCBI link July 09Cry1Bf1CAC50778Arnaut et al2001Cry1Bf2AAQ52380Baum et al2003Cry1Bg1AAO39720Wang et al2002Cry1Ca1CAA30396Honee et al1988Bt entomocidus60.5Cry1Ca2CAA31951Sanchis et al1989Bt aizawai 7.29Cry1Ca3AAA22343Feitelson1993Bt aizawai PS81ICry1Ca4CAA01886Van Mellaert et al1990Bt entomocidusHD110Cry1Ca5CAA65457Strizhov1996Bt aizawai 7.29Cry1Ca6AAF37224Yu et al2000Bt AF-2Cry1Ca7AAG50438Aixing et al2000Bt J8Cry1Ca8AAM00264Chen et al2001Bt c002Cry1Ca9AAL79362Kao et al2003Bt G10-01ACry1Ca10AAN16462Lin et al2003Bt E05-20aCry1Ca11AAX53094Cai et al2005Bt C-33Cry1Cb1M97880Kalman et al1993Bt galleriae HD29DNA sequence onlyCry1Cb2AAG35409Song et al2000Bt c001Cry1Cb3ACD50894Huang et al2008Bt 087Cry1Cb-AAX63901Thammasittirong et2005Bt TA476-1insufficient sequencelikealCry1Da1CAA38099Hofte et al1990Bt aizawai HD68Cry1Da2I76415Payne & Sick1997DNA sequence onlyCry1Db1CAA80234Lambert1993Bt BTS00349ACry1Db2AAK48937Li et al2001Bt B-Pr-88Cry1Dc1ABK35074Lertwiriyawong et al2006Bt JC291Cry1Ea1CAA37933Visser et al1990Bt kenyae 4F1Cry1Ea2CAA39609Bosse et al1990Bt kenyaeCry1Ea3AAA22345Feitelson1991Bt kenyae PS81FCry1Ea4AAD04732Barboza-Corona et1998Bt kenyae LBIT-al147Cry1Ea5A15535Botterman et al1994DNA sequence onlyCry1Ea6AAL50330Sun et al1999Bt YBT-032Cry1Ea7AAW72936Huehne et al2005Bt JC190Cry1Ea8ABX11258Huang et al2007Bt HZM2Cry1Eb1AAA22346Feitelson1993Bt aizawaiPS81A2Cry1Fa1AAA22348Chambers et al1991Bt aizawaiEG6346Cry1Fa2AAA22347Feitelson1993Bt aizawai PS81ICry1Fb1CAA80235Lambert1993Bt BTS00349ACry1Fb2BAA25298Masuda & Asano1998Bt morrisoniINA67Cry1Fb3AAF21767Song et al1998Bt morrisoniCry1Fb4AAC10641Payne et al1997Cry1Fb5AAO13295Li et al2001Bt B-Pr-88Cry1Fb6ACD50892Huang et al2008Bt 012Cry1Fb7ACD50893Huang et al2008Bt 087Cry1Ga1CAA80233Lambert1993Bt BTS0349ACry1Ga2CAA70506Shevelev et al1997Bt wuhanensisCry1Gb1AAD10291Kuo & Chak1999Bt wuhanensisHD525Cry1Gb2AAO13756Li et al2000Bt B-Pr-88Cry1GcAAQ52381Baum et al2003Cry1Ha1CAA80236Lambert1993Bt BTS02069AACry1Hb1AAA79694Koo et al1995Bt morrisoniBF190Cry1H-AAF01213Srifah et al1999Bt JC291insufficient sequencelikeCry1Ia1CAA44633Tailor et al1992Bt kurstakiCry1Ia2AAA22354Gleave et al1993Bt kurstakiCry1Ia3AAC36999Shin et al1995Bt kurstaki HD1Cry1Ia4AAB00958Kostichka et al1996Bt AB88Cry1Ia5CAA70124Selvapandiyan1996Bt 61Cry1Ia6AAC26910Zhong et al1998Bt kurstaki S101Cry1Ia7AAM73516Porcar et al2000BtCry1Ia8AAK66742Song et al2001Cry1Ia9AAQ08616Yao et al2002Bt Ly30Cry1Ia10AAP86782Espindola et al2003Bt thuringiensisCry1Ia11CAC85964Tounsi et al2003Bt kurstaki BNS3Cry1Ia12AAV53390Grossi de Sa et al2005BtCry1Ia13ABF83202Martins et al2006BtCry1Ia14ACG63871Liu & Guo2008Bt11Cry1Ia15FJ617445Guan Peng et al2009Bt E-1BNo NCBI link July2009Cry1Ia16FJ617448Guan Peng et al2009Bt E-1ANo NCBI link July2009Cry1Ib1AAA82114Shin et al1995Bt entomocidusBP465Cry1Ib2ABW88019Guan et al2007Bt PP61Cry1Ib3ACD75515Liu & Guo2008Bt GS8Cry1Ic1AAC62933Osman et al1998Bt C18Cry1Ic2AAE71691Osman et al2001Cry1Id1AAD44366Choi2000Cry1Ie1AAG43526Song et al2000Bt BTC007Cry1If1AAQ52382Baum et al2003Cry1I-likeAAC31094Payne et al1998insufficient sequenceCry1I-likeABG88859Lin & Fang2006Bt ly4a3insufficient sequenceCry1Ja1AAA22341Donovan1994Bt EG5847Cry1Jb1AAA98959Von Tersch &1994Bt EG5092GonzalezCry1Jc1AAC31092Payne et al1998Cry1Jc2AAQ52372Baum et al2003Cry1Jd1CAC50779Arnaut et al2001BtCry1Ka1AAB00376Koo et al1995Bt morrisoniBF190Cry1La1AAS60191Je et al2004Bt kurstaki K1Cry1-likeAAC31091Payne et al1998insufficient sequenceCry2Aa1AAA22335Donovan et al1989Bt kurstakiCry2Aa2AAA83516Widner & Whiteley1989Bt kurstaki HD1Cry2Aa3D86064Sasaki et al1997Bt sottoDNA sequence onlyCry2Aa4AAC04867Misra et al1998Bt kenyae HD549Cry2Aa5CAA10671Yu & Pang1999Bt SL39Cry2Aa6CAA10672Yu & Pang1999Bt YZ71Cry2Aa7CAA10670Yu & Pang1999Bt CY29Cry2Aa8AAO13734Wei et al2000Bt Dongbei 66Cry2Aa9AAO13750Zhang et al2000Cry2Aa10AAQ04263Yao et al2001Cry2Aa11AAQ52384Baum et al2003Cry2Aa12ABI83671Tan et al2006Bt Rpp39Cry2Aa13ABL01536Arango et al2008Bt 146-158-01Cry2Aa14ACF04939Hire et al2008Bt HD-550Cry2Ab1AAA22342Widner & Whiteley1989Bt kurstaki HD1Cry2Ab2CAA39075Dankocsik et al1990Bt kurstaki HD1Cry2Ab3AAG36762Chen et al1999Bt BTC002Cry2Ab4AAO13296Li et al2001Bt B-Pr-88Cry2Ab5AAQ04609Yao et al2001Bt ly30Cry2Ab6AAP59457Wang et al2003Bt WZ-7Cry2Ab7AAZ66347Udayasuriyan et al2005Bt 14-1Cry2Ab8ABC95996Huang et al2006Bt WB2Cry2Ab9ABC74968Zhang et al2005Bt LLB6Cry2Ab10EF157306Lin et al2006Bt LyDCry2Ab11CAM84575Saleem et al2007Bt CMBL-BT1Cry2Ab12ABM21764Lin et al2007Bt LyDCry2Ab13ACG76120Zhu et al2008Bt ywc5-4Cry2Ab14ACG76121Zhu et al2008Bt BtsCry2Ac1CAA40536Aronson1991Bt shanghai S1Cry2Ac2AAG35410Song et al2000Cry2Ac3AAQ52385Baum et al2003Cry2Ac4ABC95997Huang et al2006Bt WB9Cry2Ac5ABC74969Zhang et al2005Cry2Ac6ABC74793Xia et al2006Bt wuhanensisCry2Ac7CAL18690Saleem et al2008Bt SBSBT-1Cry2Ac8CAM09325Saleem et al2007Bt CMBL-BT1Cry2Ac9CAM09326Saleem et al2007Bt CMBL-BT2Cry2Ac10ABN15104Bai et al2007Bt QCL-1Cry2Ac11CAM83895Saleem et al2007Bt HD29Cry2Ac12CAM83896Saleem et al2007Bt CMBL-BT3Cry2Ad1AAF09583Choi et al1999Bt BR30Cry2Ad2ABC86927Huang et al2006Bt WB10Cry2Ad3CAK29504Saleem et al2006Bt 5_2AcT(1)Cry2Ad4CAM32331Saleem et al2007Bt CMBL-BT2Cry2Ad5CAO78739Saleem et al2007Bt HD29Cry2Ae1AAQ52362Baum et al2003Cry2Af1ABO30519Beard et al2007Bt C81Cry2AgACH91610Zhu et al2008Bt JF19-2Cry2AhEU939453Zhang et al2008BtNo NCBI link July 09Cry2Ah2ACL80665Zhang et al2009Bt BRC-ZQL3Cry2AiFJ788388Udayasuriyan et al2009BtNo NCBI link July 09Cry3Aa1AAA22336Herrnstadt et al1987Bt san diegoCry3Aa2AAA22541Sekar et al1987Bt tenebrionisCry3Aa3CAA68482Hofte et al1987Cry3Aa4AAA22542McPherson et al1988Bt tenebrionisCry3Aa5AAA50255Donovan et al1988Bt morrisoniEG2158Cry3Aa6AAC43266Adams et al1994Bt tenebrionisCry3Aa7CAB41411Zhang et al1999Bt 22Cry3Aa8AAS79487Gao and Cai2004Bt YM-03Cry3Aa9AAW05659Bulla and Candas2004Bt UTD-001Cry3Aa10AAU29411Chen et al2004Bt 886Cry3Aa11AAW82872Kurt et al2005Bt tenebrionisMm2Cry3Aa12ABY49136Sezen et al2008Bt tenebrionisCry3Ba1CAA34983Sick et al1990Bt tolworthi 43FCry3Ba2CAA00645Peferoen et al1990Bt PGSI208Cry3Bb1AAA22334Donovan et al1992Bt EG4961Cry3Bb2AAA74198Donovan et al1995Bt EG5144Cry3Bb3I15475Peferoen et al1995DNA sequence onlyCry3Ca1CAA42469Lambert et al1992Bt kurstakiBtI109PCry4Aa1CAA68485Ward & Ellar1987Bt israelensisCry4Aa2BAA00179Sen et al1988Bt israelensisHD522Cry4Aa3CAD30148Berry et al2002Bt israelensisCry4A-AAY96321Mahalakshmi et al2005Bt LDC-9insufficient sequencelikeCry4Ba1CAA30312Chungjatpornchai et1988Bt israelensisal4Q2-72Cry4Ba2CAA30114Tungpradubkul et al1988Bt israelensisCry4Ba3AAA22337Yamamoto et al1988Bt israelensisCry4Ba4BAA00178Sen et al1988Bt israelensisHD522Cry4Ba5CAD30095Berry et al2002Bt israelensisCry4Ba-ABC47686Mahalakshmi et al2005Bt LDC-9insufficient sequencelikeCry4Ca1EU646202Shu et al2008No NCBI link July 09Cry4Cb1FJ403208Jun & Furong2008Bt HS18-1No NCBI link July 09Cry4Cb2FJ597622Jun & Furong2008Bt Ywc2-8No NCBI link July 09Cry4Cc1FJ403207Jun & Furong2008Bt MC28No NCBI link July 09Cry5Aa1AAA67694Narva et al1994Bt darmstadiensisPS17Cry5Ab1AAA67693Narva et al1991Bt darmstadiensisPS17Cry5Ac1I34543Payne et al1997DNA sequence onlyCry5Ad1ABQ82087Lenane et al2007Bt L366Cry5Ba1AAA68598Foncerrada & Narva1997Bt PS86Q3Cry5Ba2ABW88932Guo et al2008YBT 1518Cry6Aa1AAA22357Narva et al1993Bt PS52A1Cry6Aa2AAM46849Bai et al2001YBT 1518Cry6Aa3ABH03377Jia et al2006Bt 96418Cry6Ba1AAA22358Narva et al1991Bt PS69D1Cry7Aa1AAA22351Lambert et al1992Bt galleriaePGSI245Cry7Ab1AAA21120Narva & Fu1994Bt dakota HD511Cry7Ab2AAA21121Narva & Fu1994Bt kumamotoensis867Cry7Ab3ABX24522Song et al2008Bt WZ-9Cry7Ab4EU380678Shu et al2008BtNo NCBI link July 09Cry7Ab5ABX79555Aguirre-Arzola et al2008Bt monterrey GM-33Cry7Ab6ACI44005Deng et al2008Bt HQ122Cry7Ab7FJ940776Wang et al2009No NCBI link Sept 09Cry7Ab8GU145299Feng Jing2009No NCBI link Nov 09Cry7Ba1ABB70817Zhang et al2006Bt huazhongensisCry7Ca1ABR67863Gao et al2007Bt BTH-13Cry7Da1ACQ99547Yi et al2009Bt LH-2Cry8Aa1AAA21117Narva & Fu1992Bt kumamotoensisCry8Ab1EU044830Cheng et al2007Bt B-JJXNo NCBI link July 09Cry8Ba1AAA21118Narva & Fu1993Bt kumamotoensisCry8Bb1CAD57542Abad et al2002Cry8Bc1CAD57543Abad et al2002Cry8Ca1AAA21119Sato et al.1995Bt japonensisBuibuiCry8Ca2AAR98783Shu et al2004Bt HBF-1Cry8Ca3EU625349Du et al2008Bt FTL-23No NCBI link July 09Cry8Da1BAC07226Asano et al2002Bt galleriaeCry8Da2BD133574Asano et al2002BtDNA sequence onlyCry8Da3BD133575Asano et al2002BtDNA sequence onlyCry8Db1BAF93483Yamaguchi et al2007Bt BBT2-5Cry8Ea1AAQ73470Fuping et al2003Bt 185Cry8Ea2EU047597Liu et al2007Bt B-DLLNo NCBI link July 09Cry8Fa1AAT48690Shu et al2004Bt 185also AAW81032Cry8Ga1AAT46073Shu et al2004Bt HBF-18Cry8Ga2ABC42043Yan et al2008Bt 145Cry8Ga3FJ198072Xiaodong et al2008Bt FCD114No NCBI link July 09Cry8Ha1EF465532Fuping et al2006Bt 185No NCBI link July 09Cry8Ia1EU381044Yan et al2008Bt su4No NCBI link July 09Cry8Ja1EU625348Du et al2008Bt FPT-2No NCBI link July 09Cry8Ka1FJ422558Quezado et al2008No NCBI link July 09Cry8Ka2ACN87262Noguera & Ibarra2009Bt kenyaeCry8-likeFJ770571Noguera & Ibarra2009Bt canadensisDNA sequence onlyCry8-likeABS53003Mangena et al2007BtCry9Aa1CAA41122Shevelev et al1991Bt galleriaeCry9Aa2CAA41425Gleave et al1992Bt DSIR517Cry9Aa3GQ249293Su et al2009Bt SC5(D2)No NCBI link July 09Cry9Aa4GQ249294Su et al2009Bt T03C001No NCBI link July 09Cry9AaAAQ52376Baum et al2003incomplete sequencelikeCry9Ba1CAA52927Shevelev et al1993Bt galleriaeCry9Bb1AAV28716Silva-Werneck et al2004Bt japonensisCry9Ca1CAA85764Lambert et al1996Bt tolworthiCry9Ca2AAQ52375Baum et al2003Cry9Da1BAA19948Asano1997Bt japonensisN141Cry9Da2AAB97923Wasano & Ohba1998Bt japonensisCry9Da3GQ249295Su et al2009Bt T03B001No NCBI link July 09Cry9Da4GQ249297Su et al2009Bt T03B001No NCBI link July 09Cry9Db1AAX78439Flannagan & Abad2005Bt kurstakiDP1019Cry9Ea1BAA34908Midoh & Oyama1998Bt aizawai SSK-10Cry9Ea2AAO12908Li et al2001Bt B-Hm-16Cry9Ea3ABM21765Lin et al2006Bt lyACry9Ea4ACE88267Zhu et al2008Bt ywc5-4Cry9Ea5ACF04743Zhu et al2008BtsCry9Ea6ACG63872Liu & Guo2008Bt 11Cry9Ea7FJ380927Sun et al2008No NCBI link July 09Cry9Ea8GQ249292Su et al2009GQ249292No NCBI link July 09Cry9Eb1CAC50780Arnaut et al2001Cry9Eb2GQ249298Su et al2009Bt T03B001No NCBI link July 09Cry9Ec1AAC63366Wasano et al2003Bt galleriaeCry9Ed1AAX78440Flannagan & Abad2005Bt kurstakiDP1019Cry9Ee1GQ249296Su et al2009Bt T03B001No NCBI link Aug 09Cry9-likeAAC63366Wasano et al1998Bt galleriaeinsufficient sequenceCry10Aa1AAA22614Thorne et al1986Bt israelensisCry10Aa2E00614Aran & Toomasu1996Bt israelensisDNA sequence onlyONR-60ACry10Aa3CAD30098Berry et al2002Bt israelensisCry10A-DQ167578Mahalakshmi et al2006Bt LDC-9incomplete sequencelikeCry11Aa1AAA22352Donovan et 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al2009Bt MC28Cry55Aa1ABW88931Guo et al2008YBT 1518Cry55Aa2AAE33526Bradfisch et al2000BT Y41Cry56Aa1FJ597621Jun & Furong2008Bt Ywc2-8No NCBI link July09Cry56Aa2GQ483512Guan Peng et al2009Bt G7-1No NCBI link Aug09Cry57Aa1ANC87261Noguera & Ibarra2009Bt kimCry58Aa1ANC87260Noguera & Ibarra2009Bt entomocidusCry59Aa1ACR43758Noguera & Ibarra2009Bt kim LBIT-980Vip3Aa1Vip3AaAAC37036Estruch et al1996PNAS 93,AB885389-5394Vip3Aa2Vip3AbAAC37037Estruch et al1996PNAS 93,AB4245389-5394Vip3Aa3Vip3AcEstruch et al2000U.S. Pat. No. 6,137,033October 2000Vip3Aa4PS36A SupAAR81079Feitelson et al1998U.S. Pat. No. 6,656,908Bt PS36AWO9818932(A2,December 2003A3) 7 May1998Vip3Aa5PS81F SupAAR81080Feitelson et al1998U.S. Pat. No. 6,656,908Bt PS81FWO9818932(A2,December 2003A3) 7 May1998Vip3Aa6Jav90 SupAAR81081Feitelson et al1998U.S. Pat. No. 6,656,908BtWO9818932(A2,December 2003A3) 7 May1998Vip3Aa7Vip83AAK95326Cai et al2001unpublishedBt YBT-833Vip3Aa8Vip3AAAK97481Loguercio et al2001unpublishedBt HD125Vip3Aa9VipSCAA76665Selvapandiyan2001unpublishedBt A13et alVip3Aa10Vip3VAAN60738Doss et al2002Protein Expr.BtPurif. 26, 82-88Vip3Aa11Vip3AAAR36859Liu et al2003unpublishedBt C9Vip3Aa12Vip3A-WB5AAM22456Wu and Guan2003unpublishedBtVip3Aa13Vip3AAAL69542Chen et al2002Sheng WuBt S184Gong ChengXue Bao 18,687-692Vip3Aa14VipAAQ12340Polumetla et al2003unpublishedBt tolworthiVip3Aa15Vip3AAAP51131Wu et al2004unpublishedBt WB50Vip3Aa16Vip3LBAAW65132Mesrati et al2005FEMS MicroBtLett 244,353-358Vip3Aa17Jav90Feitelson et al1999U.S. Pat. No. 6,603,063Javelin 1990WO9957282(A2,August 2003A3) 11Nov1999Vip3Aa18AAX49395Cai and Xiao2005unpublishedBt 9816CVip3Aa19Vip3ALDDQ241674Liu et al2006unpublishedBt ALVip3Aa19Vip3A-1DQ539887Hart et al2006unpublishedVip3Aa20Vip3A-2DQ539888Hart et al2006unpublishedVip3Aa21VipABD84410Panbangred2006unpublishedBt aizawaiVip3Aa22Vip3A-LS1AAY41427Lu et al2005unpublishedBt LS1Vip3Aa23Vip3A-LS8AAY41428Lu et al2005unpublishedBt LS8Vip3Aa24BI 880913Song et al2007unpublishedBt WZ-7Vip3Aa25EF608501Hsieh et al2007unpublishedVip3Aa26EU294496Shen and Guo2007unpublishedBt TF9Vip3Aa27EU332167Shen and Guo2007unpublishedBt 16Vip3Aa28FJ494817Xiumei Yu2008unpublishedBt JF23-8Vip3Aa29FJ626674Xieumei et al2009unpublishedBt JF21-1Vip3Aa30FJ626675Xieumei et al2009unpublishedMD2-1Vip3Aa31FJ626676Xieumei et al2009unpublishedJF21-1Vip3Aa32FJ626677Xieumei et al2009unpublishedMD2-1..Vip3Ab1Vip3BAAR40284Feitelson et al1999U.S. Pat. No. 6,603,063Bt KB59A4-6WO9957282(A2,August 2003A3) 11Nov1999Vip3Ab2Vip3DAAY88247Feng and Shen2006unpublishedBt..Vip3Ac1PS49CNarva et al.USapplication20040128716..Vip3Ad1PS158C2Narva et al.USapplication20040128716Vip3Ad2ISP3BCAI43276Van Rie et al2005unpublishedBt..Vip3Ae1ISP3CCAI43277Van Rie et al2005unpublishedBt..Vip3Af1ISP3ACAI43275Van Rie et al2005unpublishedBtVip3Af2Vip3CADN08753Syngenta.WO03/075655..Vip3Ag1Vip3BADN08758Syngenta.WO02/078437Vip3Ag2FJ556803Audtho et al2008Bt..Vip3Ah1Vip3SDQ832323Li and Shen2006unpublishedBt.Vip3Ba1AAV70653Rang et al2004unpublished.Vip3Bb1Vip3ZADN08760Syngenta.WO03/075655Vip3Bb2EF439819Akhurst et al2007","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}},"description_lang":["en"],"has_description":true,"has_docdb":true,"has_inpadoc":true,"has_full_text":true,"biblio_lang":"en"},"jurisdiction":"US","collections":[],"usersTags":[],"lensId":"071-239-392-036-045","publicationKey":"US_2012_0317682_A1","displayKey":"US 2012/0317682 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