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(12) Patent Application Publication (10) Pub. No.: US 2012/0331590 A1 Meade Et Al US 20120331590A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2012/0331590 A1 Meade et al. (43) Pub. Date: Dec. 27, 2012 (54) USE OF CRY1DAN COMBINATION WITH Publication Classification CRY1BE FORMANAGEMENT OF RESISTANT INSECTS (51) Int. Cl. (75) Inventors: Thomas Meade, Zionsville, IN (US); AOIN37/18 (2006.01) Kenneth Narva, Zionsville, IN (US); Nicholas P. Storer, Kensington, MD AOIH 5/00 (2006.01) (US); Joel J. Sheets, Zionsville, IN AOIC II/00 (2006.01) (US); Aaron T. Woosley, Fishers, IN CI2N5/10 (2006.01) (US); Stephanie L. Burton, Indianapolis, IN (US) AOIGI/00 (2006.01) (73) Assignee: Dow AgroSciences LLC, Indianaoplis, AOIP 7/04 (2006.01) IN (US) AOIH 5/10 (2006.01) (52) U.S. Cl. ........ 800/302: 514/4.5; 435/419:47/58.1 R (21) Appl. No.: 13/516,665 (22) PCT Fled: Dec. 16, 2010 (57) ABSTRACT (86) PCT NO.: PCT/US10/60829 S371 (c)(1), The Subject invention includes methods and plants for con (2), (4) Date: Aug. 27, 2012 trolling fall army worm insects, said plants comprising a Related U.S. Application Data Cry 1Da insecticidal protein and a Cryl Be insecticidal pro (60) Provisional application No. 61/284.252, filed on Dec. tein, and various combinations of other proteins comprising 16, 2009, provisional application No. 61/284,290, this pair of proteins, to delay or prevent development of filed on Dec. 16, 2009. resistance by the insects. Patent Application Publication Dec. 27, 2012 US 2012/0331590 A1 s O.O1 O1 1 1O 1OO 1OOO Concentration of Ligand (nM) Figure l 120 g 1OO 8 O 6 O O O.O1 0.1 1 10 1OO 1OOO Concentration (nM) Figure 2 US 2012/0331590 A1 Dec. 27, 2012 USE OF CRY1DA IN COMBINATION WITH identifying insecticidal proteins likely to not exhibit cross CRY1BE FOR MANAGEMENT OF resistance has been suggested (van Mellaert et al. 1999). The RESISTANT INSECTS key predictor of lack of cross resistance inherent in this approach is that the insecticidal proteins do not compete for BACKGROUND OF THE INVENTION receptors in a sensitive insect species. 0001 Humans grow corn for food and energy applica 0007. In the event that two Bt toxins compete for the same tions. Humans also grow many other crops, including Soy receptor, then if that receptor mutates in that insect so that one beans and cotton. Insects eat and damage plants and thereby of the toxins no longer binds to that receptor and thus is no undermine these human efforts. Billions of dollars are spent longer insecticidal against the insect, it might be the case that each year to control insect pests and additional billions are the insect will also be resistant to the second toxin (which lost to the damage they inflict. Synthetic organic chemical competitively bound to the same receptor). That is, the insect insecticides have been the primary tools used to control insect is said to be cross-resistant to both Bt toxins. However, if two pests but biological insecticides, such as the insecticidal pro toxins bind to two different receptors, this could be an indi teins derived from Bacillus thuringiensis (Bt), have played an cation that the insect would not be simultaneously resistant to important role in some areas. The ability to produce insect those two toxins. resistant plants through transformation with Bt insecticidal 0008 For example, Cry 1Fa protein is useful in controlling protein genes has revolutionized modern agriculture and many lepidopteran pests species including the European corn heightened the importance and value of insecticidal proteins borer (ECB; Ostrinia nubilalis (Hübner)) and the FAW, and is and their genes. active against the Sugarcane borer (SCB; Diatraea sacchara 0002. Several Bt proteins have been used to create the lis). The Cry1 Fa protein, as produced in transgenic corn insect-resistant transgenic plants that have been Successfully plants containing event TC1507, is responsible for an indus registered and commercialized to date. These include try-leading insect resistance trait for FAW control. Cry1 Fa is Cry1Ab, Cry1Ac, Cry 1F and Cry3Bb in corn, Cry1Ac and further deployed in the Herculex(R, SmartStaxTM, and Wide Cry2Ab in cotton, and Cry3A in potato. StrikeTM products. 0003. The commercial products expressing these proteins 0009. The ability to conduct (competitive or homologous) express a single protein except in cases where the combined receptor binding studies using Cryl Fa protein is limited insecticidal spectrum of 2 proteins is desired (e.g., Cry1Ab because the most common technique available for labeling and Cry3Bb in corn combined to provide resistance to lepi proteins for detection in receptor binding assays inactivates dopteran pests and rootworm, respectively) or where the inde the insecticidal activity of the Cryl Fa protein. pendent action of the proteins makes them useful as a tool for 0010 Additional Cry toxins are listed at the website of the delaying the development of resistance in Susceptible insect official B.t. nomenclature committee (Crickmore et al.: populations (e.g., Cry1Ac and Cry2Ab in cotton combined to lifesci. Sussex.ac.uk/home/Neil Crickmore/Bt/). There are provide resistance management for tobacco budworm). See currently nearly 60 main groups of “Cry toxins (Cry1 also U.S. Patent Application Publication No. 2009/0313717, Crys9), with additional Cyt toxins and VIP toxins and the which relates to a Cry2 protein plus a Vip3Aa, Cry 1F, or like. Many of each numeric group have capital-letter Sub Cry1A for control of Helicoverpa zea or armigerain. WO groups, and the capital letter Subgroups have lower-cased 2009/132850 relates to Cry1F or Cry1A and Vip3Aa for letter Sub-Subgroups. (Cry1 has A-L, and Cry1A has a-i, for controlling Spodoptera frugiperda. U.S. Patent Application example). Publication No. 2008/0311096 relates in part to Cry1Ab for controlling Cry1 F-resistant ECB. BRIEF SUMMARY OF THE INVENTION 0004 That is, some of the qualities of insect-resistant transgenic plants that have led to rapid and widespread adop 0011. The subject invention relates in part to the surprising tion of this technology also give rise to the concern that pest discovery that Cry 1Da and Cry 1Be do not compete for bind populations will develop resistance to the insecticidal pro ing sites infall armyworm (FAW; Spodoptera frugiperda) gut teins produced by these plants. Several strategies have been cell membrane preparations. As one skilled in the art will Suggested for preserving the utility of Bt-based insect resis recognize with the benefit of this disclosure, plants that pro tance traits which include deploying proteins at a high dose in duce both of these proteins (including insecticidal portions of combination with a refuge, and alternation with, or co-de the full-length proteins) can delay or prevent the development ployment of different toxins (McGaughey et al. (1998), “B.t. of resistance to any of these insecticidal proteins alone. Corn Resistance Management.” Nature Biotechnol. 16:144-146). and soybean are some preferred plants. 0005. The proteins selected for use in an insect resistant 0012. Thus, the subject invention relates in part to the use management (IRM) stack need to exert their insecticidal of a Cry 1Da protein in combination with a Cry 1Be protein. effect independently so that resistance developed to one pro Plants (and acreage planted with Such plants) that produce tein does not confer resistance to the second protein (i.e., both of these proteins are included within the scope of the there is not cross resistance to the proteins). If, for example, a Subject invention. pest population selected for resistance to “Protein A' is sen 0013 The subject invention also relates in part to triple sitive to “Protein B, one would conclude that there is not stacks or "pyramids” of three (or more) toxins, with Cry 1Da cross resistance and that a combination of Protein A and and Cry 1Be being the base pair. In some preferred pyramid Protein B would be effective in delaying resistance to Protein embodiments, the combination of the selected toxins pro A alone. vides three sites of action against FAW. Some preferred “three 0006. In the absence of resistant insect populations, sites of action’ pyramid combinations include the Subject assessments can be made based on other characteristics pre base pair of proteins plus Cry1 Fa, Vip3 Ab, or Cry1E as the Sumed to be related to mechanism of action and cross-resis third protein for targeting FAW. These particular triple stacks tance potential. The utility of receptor-mediated binding in would, according to the Subject invention, advantageously US 2012/0331590 A1 Dec. 27, 2012 and Surprisingly provide three sites of action against FAW. also indicate that the combination of Cry 1Da and Cry1 Be This can help to reduce or eliminate the requirement for proteins can be an effective means to mitigate the develop refuge acreage. ment of resistance in FAW populations to either of these 0014. Additional toxins/genes can also be added accord proteins. Thus, based in part on the data described herein, it is ing to the subject invention. For example, if Cry1 Fa is stacked thought that co-production (stacking) of the Cryl Be and with the subject pair of proteins (both Cry1 Fa and Cry 1Beare Cry 1Da proteins can be used to produce a high dose IRM both active against both FAW and European cornborer Stack for FAW. (ECB)), adding one additional protein to this triple stack 0023. Other proteins can be added to this pair. For wherein the fourth added protein targets ECB, would provide example, the Subject invention also relates in part to triple three sites of action against FAW, and three sites of action stacks or "pyramids” of three (or more) toxins, with Cry 1Da against ECB.
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