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WO 2018/075269 Al 26 April 2018 (26.04.2018) W ! P O P C T

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WO 2018/075269 Al 26 April 2018 (26.04.2018) W ! P O P C T (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2018/075269 Al 26 April 2018 (26.04.2018) W ! P O P C T (51) International Patent Classification: KENNEDY, Robert M. 3564 Lexington Circle, Dexter, A01H 5/00 (2018.01) A61K 35/742 (2015.01) Michigan 48130 (US). A01N 63/02 (2006.01) C07K 14/32 (2006.01) (74) Agent: ALBERDI, Fernando; Suite 300, 350 East Michi A61K 35/66 (2015.01) C07K 14/325 (2006.01) gan Avenue, Kalamazoo, Michigan 49007-3800 (US). (21) International Application Number: (81) Designated States (unless otherwise indicated, for every PCT/US2017/055596 kind of national protection available): AE, AG, AL, AM, (22) International Filing Date: AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, 06 October 2017 (06.10.2017) CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, (25) Filing Language: English HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, (26) Publication Language: English KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (30) Priority Data: OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, 62/41 1,1 17 2 1 October 2016 (21 .10.2016) US SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, (71) Applicant: VESTARON CORPORATION [US/US]; TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. Suite 1200, 4717 Campus Drive, Kalamazoo, Michigan (84) Designated States (unless otherwise indicated, for every 49008 (US). kind of regional protection available): ARIPO (BW, GH, (72) Inventors: CARLSON, Alvar R.; 1406 Hillcrest Av GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, enue, Kalamazoo, Michigan 49008 (US). HAASE, Alexan¬ UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, dra M.; 478 116th Ave., Martin, Michigan 49070 (US). TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, (54) Title: CLEAVABLE PEPTIDES AND INSECTICIDAL AND NEMATICIDAL PROTEINS COMPRISING SAME FIG. 2 first aspect second aspect © (57) Abstract: A peptide comprised of either a binary or a tertiary peptide, the peptide contains at least 4 amino acids and up to a 00 maximum of 16 amino acids, comprised of 2 or 3 different regions, wherein the binary peptides have 2 different regions and the tertiary o peptides have 3 different regions; wherein, the peptide can be cleaved by both an animal gut protease and an insect or nematode gut protease. o [Continued on nextpage] WO 2018/075269 Al llll II II 11III II I II III 11III 11III II I II MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, KM, ML, MR, NE, SN, TD, TG). Published: — with international search report (Art. 21(3)) — before the expiration of the time limit for amending the claims and to be republished in the event of receipt of amendments (Rule 48.2(h)) — with sequence listing part of description (Rule 5.2(a)) CLEAVABLE PEPTIDES AND INSECTICIDAL AND NEMATICIDAL PROTEINS COMPRISING SAME CROSS REFERENCE TO RELATED APPLICATIONS [0001] This application is a PCT Application, which claims the benefit of, and priority to, United States Provisional Application Serial No. 62/411,117, filed on October 21, 2016, the disclosure of which is incorporated by reference herein in its entirety. SEQUENCE LISTING [0002] This application incorporates by reference in its entirety the Sequence Listing entitled "FAM_O_PCT_225312_417641_SEQ_LIST_2017_09_29_ST25.txt" (5.37 MB), which was created on September 29, 2017, and filed electronically herewith." FIELD OF THE INVENTION [0003] New insecticidal and nematicidal proteins, cleavable peptides, DNA constructs encoding same, transgenic proteins, their expression in plants, methods of producing the transgenic proteins, new processes, production techniques, new peptides, new formulations, and combinations of new and known insecticidal and nematicidal proteins contained within transgenic proteins that produce greater pest resistance than would be expected of related insecticidal and nematicidal proteins for the control of insects and nematodes are described and claimed. BACKGROUND [0004] The global security of food produced by modem agriculture and horticulture is challenged by insect pests. Farmers rely on insecticides to suppress insect damage, yet commercial options for safe and functional insecticides available to farmers are diminishing through the removal of dangerous chemicals from the marketplace and the evolution of insect strains that are resistant to all major classes of chemical and biological insecticides. New insecticides are necessary for farmers to maintain crop protection. [0005] Insecticidal and nematicidal peptides, polypeptides and proteins are peptide and protein polymers that are toxic to their targets, usually insects or nematodes. The insecticidal peptides or toxins commonly derive from arthropod origins such as from scorpions or spiders. The toxins can be delivered directly to the insect's gut or internal organs by injection or by inducing the insect to consume the toxin from its food, for example an insect feeding upon a transgenic plant. These toxins have been known to have the ability to inhibit the growth, impair the movement, or even kill an insect when the toxin is delivered to the insect by spreading the toxin to the locus inhabited by the insect or to the insect's environment by spraying, or other means. Through direct exposure, or ingestion, the insect comes into some form of contact with the toxic peptide, polypeptide or protein. [0006] Insecticidal peptides however have enormous problems reaching the commercial market and to date there have been few if any insecticidal peptides approved and marketed for the commercial market, with one notable exception, peptides derived from Bacillus thuringiensis or Bt. There is presently, great concern over rising insect resistance to Bt proteins. [0007] Bt proteins, or Bt peptides, are effective insecticides used for crop protection in the form of both plant incorporated protectants and foliar sprays. Commercial formulations of Bt proteins are widely used to control insects at the larval stage. Inhibitory cysteine knot motif (ICK) proteins are also a class of insecticidal peptides which are derived from arthropod origins, such as the venoms of scorpions or spiders. [0008] Other classes and types of potential peptides have been identified, such as Trypsin modulating oostatic factor (TMOF) peptides. TMOF peptides have to be delivered to their physiological site of action for insecticidal activity to ensue. TMOF peptides have been identified as potential larvicides, with great potential, see D . Borovsky, Journal of Experimental Biology 206, 3869-3875, but like nearly all other insecticidal peptides, TMOF has not been commercialized or widely used by farmers and there are reasons for this. [0009] The ability to successfully produce insecticidal peptides on a commercial scale, with reproducible peptide formation and folding, at a reasonable and economical price, can be a significant obstacle to commercialization. The wide variety, unique properties and special nature of insecticidal peptides, combined with the huge variety of possible production techniques, can present an overwhelming number of approaches to peptide application and production, but few, if any, are commercially successful. [0010] There are several reasons why so few of the multitude insecticidal peptides that have been identified have ever made it to market. First, most insecticidal peptides are either too delicate or not toxic enough to be used commercially. Second, insecticidal peptides are difficult and costly to produce commercially. Third, many insecticidal peptides quickly degrade and have a short half-life. Fourth, very few insecticidal peptides fold properly when then are expressed by a plant, thus they lose their toxicity in genetically modified organisms (GMOs) such as genetically modified plants. Fifth, most of the identified insecticidal peptides are blocked from systemic distribution in the insect and/or lose their toxic nature when consumed by insects. Bt proteins are an exception to this last problem and because they disrupt insect feeding they have been widely used. [0011] The present invention provides several solutions to these major problems which have prevented commercialization and wide spread use of insecticidal peptides. The present invention provides transgenic proteins that enable the synthesis and release of insecticidal and nematicidal toxic peptides in relatively large numbers at the site of activity, i.e., the gut or other organs of the insect or nematode. The synthesis in the host is facilitated by directed expression in regions of the host cell that enables proper folding of the transgenic protein and enhances synthesis in the host cell. SUMMARY OF THE EXEMPLARY EMBODIMENTS OF THE INVENTION [0012] The present invention provides cleavable peptides that are fused to toxic insecticidal and/or nematicidal toxic peptides and proteins that can be expressed and synthesized in a host cell, for example a plant cell that is subject to consumption by an insect or nematode pest. The cleavable peptides may be cleaved in the gut environment and/or hemolymph environment of an insect and/or nematode and in the gastrointestinal system of a human being thereby releasing its payload comprising one or more insecticidal and/or nematicidal toxic peptides and proteins. [0013] In a first aspect, the present invention provides cleavable peptides comprising a binary or a tertiary peptide that contains at least 4 amino acids and up to a maximum of 16 amino acids, comprised of 2 or 3 different regions. In one example, the binary peptides have two different regions (an insect or nematode cleavable region and an animal (e.g.
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