CHIMERIC INSECTICIDAL PROTEINS.

Abstract

The invention discloses vegetative insecticidal toxins IRDIG35563, polynucleotides encoding said toxins, the use of said toxins for pest control, and transgenic plants that produce said toxins. The invention includes variants, fragments, and analogues of IRDIG35563.

Description

CHIMERIC INSECTICIDAL PROTEINS Cross reference to related applications This Application claims the benefit of priority to U.S. Provisional Application No. 62 / 563,228 filed on September 26, 2017 which is incorporated herein by reference in its entirety. Reference to electronically submitted sequence listing The official copy of the sequence listing is submitted electronically via EFS-Web as a sequence listing in ASCII format with a file named ”§0144J#VO_PCT_Sequ&rroe created on September 25, 2018 and size:® 17 kilobytes and is presented concurrently with the descriptive memory. The sequence listing contained in this document in ASCII format is part of the descriptive menu and is incorporated herein by reference in its entirety, field.d^ The invention relates generally to the field of molecular biotology. More specifically, the invention relates to novel insecticidal protein toxins developed from vegerative insecticidal protein toxins found in BaciHus thuringiensis and their use to control insects. Background of your invention Insects and other pests cost farmers thousands of thousands of dollars annually in crop losses and expenses to keep these pests under control. In addition to the losses in the 20 fields of «ΛΜ, quaking insect pests are a burden to vegetable and fruit growers, to growers of ornamental flowers and to home gardeners. Losses caused by insect pests in agricultural production environments include decreased crop yield, reduced crop quality, and increased harvest costs. Insect pests are mainly controlled by intensive applications of 25 chemical pesticides, which are active through inhibiting the growth of the insect, preventing the insect from attaching or reproducing or causing death. In this way, good control can be achieved. insects, but these chemicals can sometimes affect other beneficial insects as well. Another problem resulting from the widespread use of chemical pesticides is the emergence of resistant insect populations. This I know has relieved the hands partially m^ diverse 3Q resistance management practices, but there is an increasing need for control agents? alternative pests. Biological pest control agents, such as Baciii strains expressing pesticidal toxins as delta-endotoxins, have also been applied to crop trials with satisfactory results, offering an alternative or complement to chemical pesticides. The genes encoding some of these delta endotoxins have been isolated and their expression in heterologous hosts has been shown to provide another tool for the control of economically important insect pests. In particular, the expression of insecticidal toxins, such as the delta-syndotexiiras in transgenic plants has provided widespread protection against selected insect pests, and transgenic plants expressing such toxins have been commercialized, allowing farmers to reduce applications of insecticidal agents. against chemicals! of insects. £1 scare microbe Eac / te Wmbgiensb is a spit-forming bacterium, characterized by parasporal crystalline protein jneutones. bacilas fhunng®nsfe continues to be the main source of novel insecticidal proteins e.| development of pesticides incorporated into plants. In the North American mate insect resistance market. Spodo^era fn^^a (fall armyworm), Ostonte nyOía / ís Hübner (European mate borer ΈΕΒ* (Eurapesa coró borer)) and Mp / icpvew zea Boddie (CBAC mate worm) are key driver pests, although there are other key insect pests in other Geographic Idealities (for example, Ηρ^ονοτρη armigera (bollworm cation *C8We) or earworm) and additional secondary but important insect pests, Yes toxins account for more than 90% of bioinsecticide products on the market and essentially the entire gene source of transgenic crops that have been developed to provide resistance to insect feed St bacteria produce delta endotoxins that include the Cristel toxins (CrystsÁ Cytotoxin (Cyt< of English Qytótoxin) and Prbtetna Vegetative Insecticide (VIP) i Proton), depending on its gene and protein structure. Cry toxins are produced during spore formation as insoluble crystalline proteins. VIP toxins, on the other hand, are produced as soluble proteins during the vegetative phase of Et bacterial growth. W proteins are distinct from Cry proteins in their structure, but they share the property with Cry toxins of being pore-formers that act on cells located in the midgut of the insect. The classification of the VlR protein was previously based on its target insect types. The currently used nomenclature systematically classifies VIP genes based on amino acid sequence homology rather than insect specificities, Crickmere, N., Baum, J., Bravo, A<, Leteclus, D„ Narva, K. , Sampson, K.(Schnepf, E., Sun, M. and Zeigten D.R. *Sacfcs ttanngfeasáí texto nomenclatore'' (2016); http: / / www.btnomenctetúre.mfo / and httpte^sw.iif®sci.sussex. ac.uk / home.W The continued use of chemical and biological agents to control insect pests increases the likelihood that insects will develop resistance to such control measures. Also, the high selectivity of biological control agents often results in only a few specific insect pests being controlled by each agent. Despite the success of EC8-resistant transgenic mate, the possibility of the development of resistant insect populations threatens the long-term durability of Cry proteins in ECB control and creates a need to discover and develop new Cry or other types of agents. of ©antro! biological to control ECB and other control pests. There remains a need to discover and develop new and ethical pest control agents that provide economic benefit to farmers and that are environmentally acceptable. There is a particular need for site agents directed at a broad spectrum of economically important insect pests that efficiently control populations of insects that are, and could become, resistant to existing insect control agents and those with equal or increased potency compared to with current control agents. Brief summary of the invention The present invention provides Insecticidal chimeric Vi P toxins, including the protein toxin designated IRDIG35SS3 (SED 1D NO:2j which was constructed by Passaging in the first 6 1 3 amino acid residues of VIP3AÓ1 and a CAerminsi portion of another VIP toxin, variants of IRDIG35563 nucleic acids encoding these chimeric toxins-, methods of pest control using the toxins, methods of production of the toxins in transgenic host cells and genetic plants expressing the toxins, the invention further provides a pheo-oombinal nucleic acid construct comprising one or plus heterologous regulatory etemenphos that direct the expression of a nucleic acid sequence encoding SEQ ID NO:2 and nucleic acid sequences selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3 and SEQ ID NO;4 In another embodiment, the invention provides nucleic acid constructs comprising a nucleotide sequence encoding a toxin. IRDIG35563 chimeric insect gene operatively linked to one or more tefes regulatory regions as a promoter that is not derived from ® and is capable of directing expression in a host cell, preferably a plant cell. The invention includes an insecticidal chimeric toxin comprising residues 1 to 789 of SEQ ID NO:2 and plants or plant parts comprising such rwiefic acid constructs. The invention further provides plants or parts of plants in which the chimeric toxin has insecticidal activity against insects selected from the group consisting of Sporfoptera exigua (BAW), Spodoptera endan / a (Southern Worm, SAW). Southern armyworm), Spodoptero frugipertia (FAW), CrylF resistant Spodépfera frugipa (rFAW), Hetísoverpa zea (CEW). Pséitoopfesfe ínc / orfens (Soybean Looperworm. SBL (Soybean looperp. Anticarsia g&mmataHs (VWetbean Caterpillar), VBC), Me¿Ws virescens (Tobacco Worm, TBW (dei English, Tobacco budwotm)) and Ffefówerpd atrmgwa (cotton bollworm, CBW) Also provided by the invention is a method of controlling susceptible insects which comprises contacting the gut of said insect with an effective amount of a chimeric toxin di vulgar as well as a method of controlling an insect pest population comprising contacting the intestine of individuals of said pest population with an insecticidally effective amount of the disclosed chimeric toxin. Also provided is a method of producing an insect resistant or insect tolerant plant comprising crossing a non-transgenic plant with a transgenic plant comprising a disclosed DNA construct stably incorporated into the plant genome and selecting progeny which condemn the construction of disclosed nucleic acid. Description of the sequences •SEO ID ΝΟΊ A chimeric DNA sequence encoding IRD1G35563; SEQ ID NO:2 The chimeric protein toxin sequence of IRDIG35563. SEQ ID. NQ:3 An optimized high GG AON sequence from maize encoding ÍRDIG35563. SEQ ID MO:4 A most preferred codon optimized AON sequence from soybean encoding IRGIG36663. Detailed description of your invention DEFINITIONS As used herein, fes form the singular uní uno” or *una* and “οΓ o la* include plural referents, unless the context clearly indicates that they do so, therefore, for example, upa references a cell. Include a plurality of such cells and a reference to Ίδ 10 protein” includes references to one or more proteins and equivalents thereof, and so on. All technical and scientific terms used in this document have the same meaning as that understood by a person normally versed in the matter to which this document belongs, unless clearly indicated otherwise. Sufficiently identical is used herein to refer to an f§ amino acid sequence that is at least about 40¾ long. 45%, 50%, 51%. 52%, 53%, 54%, 55%, 563¾. 57%, 58%, 59%, 50%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73% , 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%. 83% Wow, 85%, 86%, 87%, 88%, 89%. 90%, 91%, 92%, 93%, 94%. 95% 96% 97%, 98%. 99% or greater sequence identity compared to a reference sequence using one of the alignment programs described herein using 20 standard parameters. As used herein, the term protein, "peptide molecule" or polypeptide refers to those molecules that undergo modification, including post-translational modifications. such as, but not limited to, disulfide bond formation, glycosypheolon, phosphorylation or oligomerization, The terms "amino acid" and amphoteric refer to all naturally occurring L-amino acids. Retains insecticidal activity is used herein to refer to a polypeptide having at least about 16%, at least about 30%. at least about 50%, at least about 70%, 80%, 90%, 95% or more of the insecticidal activity of the full length IRDIG35563 polypeptide. Fragments or "biologically active pardons" include polypeptide fragments comprising amino acid sequences sufficiently identical to an IRDfG35563 polypeptide and having insecticidal activity and polynucleotides encoding the fragments. Biologically Active Fragments or Portions of RDIG35583 Polypeptides includes fragments comprising 35 amino acid sequences sufficiently identical to the amino acid sequence set forth in the 1RDIG35563 polypeptides of the disclosure, wherein the polypeptide has insecticidal activity. An isolated nucleic acid molecule (fo DNA) is used herein to refer to 3 a nudfeicp acid (or DNA) sequence that is no longer found in its natural environment and has been brought into focus in an environment of difference by the hand of the starvation, for example, in vitro. A recombinant nucleic acid (or DNA) molecule is used herein to refer to a nucleic acid (or AON) sequence found in a recombinant bacterial or plant host cell. In some embodiments, an isolated1' or recombinant'' nucleic acid is free of sequences (preferably protein-coding sequences) that naturally flank the nucleic acid (i.e., sequences located at the 5' and 3' ends of the nucleic acid) in the genomic NAO of the organism from which the nucleic acid is obtained. "Contiguous nucleotides" is used herein to refer to nucleotide residues that lie immediately adjacent to one another. As used herein, non-genomic nucleic acid sequence, nucleic acid molecule, or polynucleotide refers to a nucleic acid molecule that has one or more nucleic acid sequence changes compared to a native nucleic acid sequence. or genomics. In some embodiments, the change to a native or genomic nucleic acid molecule includes, but is not limited to: changes in nucleic acid sequence due to degeneracy of the genetic code; optimization of the nucleic acid sequence for its expression in plants* changes in the nucleic acid sequence to introduce at least one amino acid substitution, insertion, deletion and / or addition compared to the native or genomic sequence: deletion give one more p upstream or downstream regulatory regions associated with the genome nucleic acid sequence; insertion of one or more hetsróioggs upstream or downstream regulatory regions; removal of the 5' and / or 3' untranslated region associated with the genome nucleic acid sequence; insertion of a heterogeneous 5' and / or 3' untranslated region; and modification of a poiiadenylation site. In some embodiments, the non-genomic nucleic acid molecule is a synthetic nucleic acid sequence. The present invention provides insecticidal grotesque toxins and methods of administering these toxins which are functionally active and effective against many orders of insects, especially lepidopteran insects. By activity function insecticidal or active against it is meant that the protein is functional as an orally activated toxin or insect control agent, that the protein has a toxic effect or is capable of interrupting or stopping the growth and feeding of the insect . When an effective amount of a toxin of the subject invention is ingested by an insect administered through the expression of the phrasgenic plant, composition, formulated protein compositions, purivable protein composition(s), a bait matrix, or other delivery system, the results they are typically death to! insect, inhibition of growth or proliferation give! insect or preventing insects from feeding on the source, preferably a transgenic plant, which makes the toxins available to insects. The functional proteins of the subject invention may also function together or with soybeans to potentiate or enhance the activity of one or more other toxin proteins. The terms “toxic0, toxicity* or “toxin” are intended to convey that the toxins: object have phonoíomh activity as defined in this document. Complete lethality to feeding insects is preferred but not required to achieve functional activity. If an insect avoids the toxin or ceases feeding, that avoidance will be useful in some embodiments. even if the effects are subbietates or fetility is delayed or indirect. For example, if plants are desired -^308^1038..^88^1^68: to insects, the reluctance of insects to feed on plants is so Useful as fetal toxicity to insects because the ultimate goal is to prevent insect-induced plant damage. Using various strains of bacterial isolates, the present inventors have invented new chimeric toxins that are active against an unexpectedly large array of commercially important insect pests. The present inventors herein describe the invention of novel VIP toxins that have unexpectedly broad-spectrum insecticidal activity, including insecticidal activity against Spodoptera exigua(gardarna, BAW)< Spodeptara aridania (southern bollworm, 10 SAW), Sp&dopÍ&d frugipérds (fall armyworm, . FAW) and FAW resistant to protectors incorporated into deregulated plants, He / fcowpd zea (corn stalk, CEW), Pset / sfc^usia indudeos (soybean looper, SBL), Andcsrsta gammata / is (legume caterpillar , VBC), Hel / afhís «resceos (tobacco worm, TBW) and Hé / icoverpa érmtgerp (cotton caterpillar, CBW). An otase of insecticidal proteins called VIP3 has been described. See, for example, EStruch et al (1996, Proc, Nati, Acad. Sci. 93:5389-5394) and Yu et al (1997, Appl. Environ. Microbiol. 83:532-536), VIP3 germs encode proteins of approximately 88 Wa that are expressed by 8fe during the vegetative growth phases. These toxins are reported to be distinct from the crystal-forming delta-endotoxins. Reference to VIP toxins designated VIPlA(a), νΐΡΊΑφ). VIP2Aia). VIP2A(b), VlP3A(a) and VIP3A(b) are known in the literature. See also Lee et al. AEM yol. 69, no. S 20 (August 2003), pages 4648-4657, for a discussion of the mechanism of action and truncation of VIP proteins. VIP3A progeny toxins possess insecticidal activity against many tepidoptres pests, including FAW, CEW, Huínagel (biack cutworm) and HeífaWs víresews Fabñcius (tobacco cutworm TBW*). . More recently, 2§ VIP proteins have been found to be toxic to certain species of Hemipteran insect pests (Nanasaheb, P. ét al, Tóxíns (Base!) vol 4, n,“8 (Jun 2012), pages 405- 429, Saltar S. and Msíti MK„ J. MiorobloL Bípteciínoi. 2011, 21:937-946), In this way, the VIP class of protein toxins show a unique spectrum of insecticidal activities. Other disclosures, fes documents WO 98 / 1893? WO 99(33991, WO 98(00546 and WO 99 / 57282, have now also identified homologues of the class of 3S VIP3 proteins. IRDIG3S563 Polypeptides A novel VIP-based chimeric insecticidal protein, IRD1G35563, was created by combining the 613 N-terminal amino acids of VtP3Ab1 with the 176 C-terminal amino acids of IRDIG W870 (also known as DiG740). Due to redundancy ce! genetic code, a variety of different nucleic acid sequences can encode the amino acid sequences disclosed herein readily. It is well known to those skilled in the art how to screen for these alternative nucleic acid sequences that encode the same, or essentially the same, toxins once the amino acid sequences are known. Active insect variants of the IRDIQ35563 toxin are also described herein and are collectively referred to as IRDIG35563 insect toxins or rRDIG35563 variants and include truncated forms that have Met Nlerminal residues added to the N-terminal truncations. in SEQID NO2. For full length toxins, amino acid substitutions varying by no more than 5% from SEQ ID NQ:2 that retain activity are within the scope of the present invention. In some embodiments, the IR0IG35563 polypeptide is at least about 40%; 45%, 50%, 51%. 52%, 53%, 54%, 55%, 56%, 57%. 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 86%, 67%, 70 %, 71%, 72%. 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, S3%, 84%, 85%, 86%, 87%, 88%, 89%, 90%. 91%, 92%, 93%, 94%, 95%, .96%, 97%, 98%, 99% or greater sequence identity compared to SEQ ID NO: 2, as well as substitutions, deletions, insertions of amino acids, fragments of themselves and combinations thereof. The term "about" when used herein in context with percent sequence identity means +A 0.5%. These values ​​can be adjusted as appropriate to determine corresponding protein homology considering amino acid similarity and Similar. In some embodiments, the identity of seéuenplá is centered on the full length sequence of a polypépiidc IRDIG35563. In some embodiments, the ÍRDIG35563 polypeptide fragments comprise an amino acid sequence sufficiently identical to the amino acid sequence set forth in the polypeptides. IRDIG35563 gives the disclosure, wherein the polypeptide has insecticidal activity. Said biologically active portions can be prepared by recombinant techniques and evaluated for their insecticidal activity. In some embodiments, the 1RDIG35563 polypeptide retains insecticidal activity against a lepidopteran species. In some embodiments, the insecticidal activity is against one or more insect pests selected from BAW; SáW, FáW, rFAW.CÉW, TBW, SBL, V8C and CBW. In some embodiments, the polypeptide fragment is an N-terminal and or or O-terminal truncation of ai minus 1,2, 3, 4, 5, 6, 7, & 9, 10, 11, 12, 13, 14, 1S, 16,17,18 ,19, 20. 21,22, 23,24, 25, 26, 27, 28, 29, 30, 31 or more amino acids from the N-terminus and / or the C-terminus, by proteolysis, or by insertion of a start podon , by deletion of the codons that encode the deleted amino acids and concomitant insertion of a start codon and / or insertion of a stop codon in the sequence that encodes the polypeptide fragment.,. In some embodiments, the fragment of the ÍRDIG35563 polypoptide is an N-ferminal truncation of at least 1, 2, 3, 4, 5, 6, 7, 8, 9, W, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21.22, 23, 24 amino acids from the N-terminus of the polypeptide IRDIG35563 of SEQ ID NO: 2. In some embodiments, the 1RDIG35563 polypeptide fragment is an N-terminal 35 and / or C^erminal truncation of ai minus 1,2, 3,4, 5, 6.7, 8,9.10, 11, 12,13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34 or more amino acids from the N-terminus and / or the C-terminus with respect to ai polypseptide IRDIG35563 of SEQ ID NO: 2. In some embodiments, an IRD1G35563 polypeptide comprises an amino acid sequence having at least .about 40% .Á^^ 50¾. 54%, S2%,53%, 54%, 55%, 56%, 57%,:58%, 59%, 60%, 81% 62%, 63%, 34%, 85%, .66%, 67 %, 68%. 68%, 70%, 71%, 72%, 73%, 74%, 75%, 78%, 77%. 78% 79%, 80%, 81%, 82%. 83% 84%, 85%, 86%, 87%, 88%. 89% 90%, 91%, 92%, 93%. 94% 95%, 96%, 97%, 98%, 99%. or more of sequence identity to the amino acid sequence of the IRDIG35563 polypeptide of SEQ ID NO: 2. wherein the 1RDIG35563 polypeptide has insecticidal activity. A surprising property of 1RD1G35583 is that it was found to be active against FAW populations that have become resistant to certain Cry toxins, especially CrylF. Consequently, the 1RDIG35563 toxins are ideal candidates for the control and prevention of resistant lepidopteran pest populations. Another surprising property of bottlenose dolphins IRD1G35563 is their broad spectrum of activity against many lepidopteran pests on crops. Another surprising property of these chimeric toxins is their activity against Lepidopteran species that are pests of both corn and soybean including BAW, SAW, FAW, rFAW, CEW, TBW, SSL, VBC and CBW, IRDIG35563 Toxins and Insecticidally Active Variants In addition to the full length IRDIG35563 toxin of SEQ ID NO:2, the invention encompasses insecticidally active variants of SEQ ID NO:2. By the term variant, applicants intend to imply certain detection, substitution and insertion mutants. An ÍRDÍG35563 fragment is any protein sequence found in the 20; SEQ ID NO:2 which is less than the full length of the amino acid sequence IRDIG35563 and which has insecticidal properties. Variant fragments of IRD1G35563 are also contemplated as part of the invention and are defined as fragments of IRDIG355S3 that contain certain delecten, substitution and insertion mutants described herein and that have Insecticidal activity. Variants of.IRDIG35563 created by performing a limited number of detectones^ substitutions or 25 amino acid dietenes. Amino acid detections, substitutions and additions to the amino acid sequence ds SEQ ID NQ:2 can easily be performed in a sequential manner and the effects of variations in insecticidal activity can be tested per bioassay. The invention also includes insecticidally active variants of ia SEQ ID NO :2 in phases in which up to 39 independent conservative substitutions have been made. Amino acid sequence variants of an IRDIG35563 pelipeptide can be prepared by mutations in the DNA. This can also be accomplished by one of several forms of mutagenesis and / or directed evolution. In some aspects, the encoded changes in the amino acid sequence will not substantially affect the function of the protein. Such variants will possess the desired pesticidal activity. However, it is understood that the ability of an iRDIG35563 polypeptide to confer pesticidal activity can be enhanced by the use of such techniques in the compositions of the present disclosure. In some embodiments, the methionine translation initiator of the IRDIG35S63 polypeptide is cleaved posttranslationally, for example, by a methionine aminopeptidase in many cellular expression systems, Variants can be made by performing random mutations in the variants or § vanants can be engineered. In the case of engineered killants, there is a high probability of generating variants with similar activity to the native toxin when amino acid identity is maintained in critical regions of the toxin that represent biological activity or are involved in determination of biological activity. three-dimensional configuration that is ultimately responsible for biological activity. An alias probability of retention activity will also occur if the substitutions are conservative. Amino acids can be placed into the following classes: nonpolar, polar uncharged, basic, and acidic. Conservative substitutions, whereby one amino acid of one class is replaced by another amino acid of the same type, are less likely to materially alter the biological activity of the variant. Table 1 provides a list of examples of amino acids that belong to each class. Table 1 amino acid classes Type of amino acid Examples of amino acids Nonpolar side chains Ala (A), Val (V). Leu (L>, fie (f). Pro (P). Met (Mj. Phe (F), Trp (W) „ ................. _.. ..........................1 Non-Gly (G) Polar Side Chains Ser (S), Thr (T) Cys (C) .Tyr (Y) .Asn | charged (N), Gln (Q) | Acidic side chains Asp (Dj, Glu (E) Basic side chains Lys (Kj, Arg (R), His (H} | Branched side chains Thr , Val, lie in beta Aromatic side chains Tyr Phe, Trp, His Alternatively, alterations can be made to the protein sequence of many proteins at the amino or carboxyl terminus without substantially affecting activity. This may include insertions, deletions, or alterations introduced by modern molecular methods, such as PCR, including PCR ampliftealones that alter or prolong the protein coding sequence by including amino acid coding sequences in the oligonucleotides used in PCR amplification. Alternatively, these added protein sequences can include entire protein coding sequences to generate protein scallops. Such fusion proteins are typically used to (1) increase the expression of a protein of interest {2} introduce a binding domain, enzyme activity, or epitope to facilitate protein purification, protein detection, or other experimental uses ( 3) direct the secretion or translation of a protein to a subcetal organ, such as the penplasmic space of gram-negative bacteria. the mitochondria or ctoropias of foot or the endoplasmic reticulum of eukaryotic cells. resulting in the latter glycosyfection efe the protein, The nudeotide and vanant amino acid sequences of the disclosure also encompass sequences obtained from mutagenic and replaceable procedures such as DNA rearrangement. With said ptocsdimfe^ an o. More different regions that the IRDIG35563 polypeptide would encode can be used to create a new IRDIG35563 polypeptide possessing the 5 desired properties. Thus, racombinant polynucleotide libraries are generated from a population of related polynucleotide sequences that comprise regions of sequence that have substantial sequence identity and can recombine homologously-in vitro or in vivo. For example, using this approach, sequence motifs encoding a domain of interest can be ordered between a pesticidal gene and other known pesticidal genes to obtain 1G a new gene encoding a protein with a purple property of interest, such as as an increased insecticidal activity. Strategies for such DNA ordering include, for example, Stemmeo (1994)PteC. M. Mari Sel. USA 91.10747-10751; Stemmer, (1994) Afetere 370:389491; Cramed, et a / ., {1997} WureBfefecte 15:436-438; Moore, the ai,, (1997) Z Mol. Biol. 272:336447: Zhang, et ah, (199?) Nati. Acad. sa. L / SA 94:4504-4509; Craméri, et!., (1996) Natura 391:288-291- and US Patent Numbers 5,605,793 and 5,837,458. Domain swapping or rearrangement is another mechanism for generating altered IRDIG35563 polypeptides. Domains can be interchanged between IRDtó3556a polypeptides resulting in additional Pill or chimeric toxins with improved insecticidal activity or target spectrum. The pesticidal proteins of the present invention are encoded by a nucleotide sequence sufficiently identical to the nucleotide sequence of SEQ ID NO:1 or the pesticidal proteins are sufficiently identical to the amino acid sequence set forth in SEQ ID NO:2. To determine the parallel identity of two amino acid sequences or two nucleic acids, the sequences are aligned for the purpose of optimal alignment. The percent identity between the two sequences is a function of the number of identical positions shared by the three sequences (ie, percent identity "number of identical positions / 'total number of positions (eg, overlapping positions) x 100), In one look, the two sequences are the same length. In another embodiment > percent identity is calculated across the entire reference Séguenciá. Percent identity between two sequences can be determined using gap-like techniques described below, allowing for gaps or not. When calculating percent identity, exact matches are normally counted. A gap, (a position in an alignment where a residue is present in one sequence but not in the other) is considered to be a position with non-identical residues. Determination of percent identity between two sequences can be accomplished using a mathematical algorithm. A non-limiting example of a mathematical algorithm used for the comparison of two sequences is the algorithm incorporated in the programs 8LASTN and 8LASTX. Karlin and Aitschul (1990) Proc. Nat'i. Asad. Sel. USA 87:2264. Altschul eí a / . (1990) J. Mol Βίοι. 215,493 and Karlin and Altschul (1993} Proo. Nafí. Acad. B&, USA 90:5873-5877. BLAST nucleotide searches can be performed with the BLASTN program, score - 100, word length 12, to obtain thanotogase antileotide sequences. Acid Molecules: Pesticide-like Nucleic of the Invention BLAST c-bn protein searches can be performed using the BLASTX program, score ~ ​​SO, wordlength ® 3, to obtain amino acid sequences homologous to pesticidal protein molecules of the invention. To obtain gapped alignments with comparison stains, Gapped BLAST can be used (in BLAST 2.0} as described in Aiíscbul, ef a / „ (1997) Afeicte / c Acida Ras. 2S-33S9, Alternatively, PSi- Blast to perform an iterated search that detects distant relationships between molecules See Altschul, ata!, (1997) supra, When using the three BLAST, Gapped BLAST and PSI-Blast programs, the three default parameters of the respective programs can be used. assets (eg. BLASTX and BLASTN). Alignment can also be done manually by inspection. Another non-limiting example of a mathematical algorithm used for sequence comparison is the CtústaW algorithm (Híggins éf al (1994) Nucteic Acida Res. 22:4673-4680). ClustalW compares sequences and aligns the entire DNA or amino acid sequence and can therefore provide data about the sequence conservation of the entire amino acid sequence. The ClustalW algorithm is used in several commercially available DNA and amino acid analysis software packages, such as the ALIGNX module of the Vector NTl software suite (Invitnsgen Corporation, Garisbad, CA), after alignment of the DNA sequences. amino acids with CiuslalW, percent amino acid identity can be assessed. A non-limiting example of a program Useful informatics 2Q for if analysis of alignments of CiustalW ss GENEDOC^. GENEOGC'^ (Kart Midiolas) allows the evaluation of amino acid (or DNA) similarity and identity between multiple prptsins. Another non-limiting example of a mathematical algorithm used for sequence comparison is the algorithm of Myers and MHIer, (1983): DARIOS 4(1):14-17. Said algorithm I know: it incorporates into the ALIGN program (version 2.0), which is part of the GCG Wisconsin Genetics Software package, version 10 (available from Accelrys, Inc., San Diego, CA, USA). When using the ALIGN program to compare amino acid sequences, a weighting table of PAM129 residues, a gap length penalty of 12, and a gap penalty of 4 may be used. uses the algorithm of Needteman and Wunsch, (1970) J. M. Bial 48(3) 443-453, will be used to determine sequence identity or similarity using the following parameters: %identity and %similarity for a sequence of nucleotides using gap weighting of 50 and length weighting of 3 and the scoring matrix nwsgapdna.smp: %. of identity or % similarity for an amino acid sequence using gap weight of 8 and length weight of 2, and the BLQSUM32 scoring matrix. Equivalent programs can also be used. By equivalent program is meant any sequence comparison program that, for any two sequences in question, generates an alignment that has identical matches of nuGleotide residues and a percentage sequence identity: identical compared to the corresponding alignment generated by GAP Version 10, In another embodiment of the invention, protease cleavage sites can be designed at desired locations to affect protein processing within the midgut of susceptible larvae of certain insect pests. These protease cleavage sites can be introduced by methods such as gene synthesis. chemical or PCR overlapping splicing (Horton et al, 1989). The recognition sequences of serine proiease. For example. they can optionally be inserted at specific sites in the Cry protein structure to affect protein processing at desired reporting points within the midgut of susceptible larvae. Senna proteases that can be exploited in this way include Lepidopteran midgut seri^^ such as trypsin or trypsin-like enzymes, chymotrypsin. elastase etc tChristelfer era / ., 1992). In addition, 1G report sites identified empirically by sequencing Cry protein digests generated with preparations of larval midgut protease either unfractionated or bound to brush border membrane vesicles, can be engineered to effect protein activation. Lepidopteran and coleopteran serte® proteases such as trypsin, chemotnpsin, and cathepsin G-type protease, lepidopteran and coleopteran cisternae proteases such as cathepsins (B-type, L-type, O-type, and K-type proteases) (Koiwa et al. , £20013} and Bown ef a / ., (2004)), lepidopteran and ooteopteran metatoproteases such as ABAM10 (Gchoa-Oampuzans ef di., (2007)) and lepidopteran and coleopteran aspartic acid proteases such as eatepslnás type O and E-type pepsin, pyasmin, and chymosin can be further exploited by engineering appropriate recognition sequences at desired processing sites to affect Cry protein processing within the midgut of susceptible larvae of certain insect pests and can that also works by providing activity against non-susceptible insect pests. IROIG35563 variants can be produced by introducing or removing protease processing sites at appropriate positions in the coding sequence to allow, or eliminate, proleolylic cleavage of a larger variant protein by insect, plant, or microorganism proteases that are within the scope of the invention. The end result of such manipulation is understood to be the generation of toxin fragment molecules that have the same or better function and / or activity as the intact (full-length) toxin protein. In another embodiment, fusion proteins are provided that include within their 30 amino acid sequence an amino acid sequence comprising an IRDIG35563 polypeptide of the disclosure. Polynucleotides encoding an IRDIG35563 polypeptide can be fused to signal sequences that will direct localization of the IRDIG35563 polypeptide to particular compartments of a prokaryotic or aukaryotic cell and / or direct secretion of the IRDIG35563 polypeptide from the realteacin of a prokaryotic or eukaryotic cell. For example, in B coft, one may wish to direct protein expression to the periplasmic space too. Give examples of serious sequences or proteins! (or fragments thereof) to which the IRDIG35563 polypeptide can be fused to direct expression of the polypeptide in the peripiasmic space of bacteria include, but are not limited to, the signal sequence! of pe!B. the signal sequence of the maltose-binding protein (MSPj. MBP. the signal sequence of ompA, the signal sequence of the.subunldad 8 of the thermobii enterotoxin of E. ü&ti peñ^smica and the signal sequence of alkaline phosphatase Various vectors are commonly available for the construction of fusion proteins that will direct the production of a protein, such as the pMAL series of vectors (particularly I will be pMAL-p) available from New England Bioabs. The IRDIG35563 polypeptide can be fused to the te liase pe® pectate signal sequence to increase the efficiency of te expression and purification of such polypeptides in gram-negative bacteria (see, for example, US Patent Nos. 5,576,195 and 5,848,818). The fusion may be plant plastid peptide / pelipeptide fusions and apoplasium transit septics such as secretion signal alpha-amitese from rice or barley. plating trans4o is generally fused N-terminally to the polypeptide to be targeted (eg, the fusion partner). In one embodiment, the fusion protein consists essentially of the piastide transit peptide and the 1RDIG35563 polypeptide to be targeted. In another embodiment, the fusion protein comprises the peptide transit peptide and the polypeptide to be targeted. In such embodiments, the ptesphidium transit peptide is preferentially located at the N-terminus. 1S terminus of the fusion protein. However, there may be additional N-terminal amino acid residues to the plastid transit peptide if the fusion protein is at least partially targeted to a plastid. In a specific embodiment, the piastid transit peptide is located in the Merminal half in the N-terminal third or in the N-terminal fourth of the fusion protein. Most or all of the plasfid transit peptide is generally cleaved from the fusion protein after its insertion into the peptide. The position of cleavage may vary slightly between plant species, at different stages of plant development, due to conditions specific intercellular or fusion partner peptide combination used. In one embodiment, the cleavage of the pfestidip transit peptide is homogeneous, such that the cleavage site is identical in a population of fusion proteins. In another embodiment, the plastid transit peptide is not homogeneous, such that the cleavage site varies by 1-W amino acids within a population of fusion proteins. The plastid transit peptide can be recombinantly fused to a second protein in one of several ways. For example, a restriction endonuclease recognition site can be introduced into the node sequence of the transit peptide at a position corresponding to its C-terminus and can be engineered into the same site or a compatible nucleotide sequence. of the protein that is going to be directed to its N-terminal end. Care must be taken when designing these sirens to ensure that the coding sequences for the transit peptide and the second protein are kept in frame to allow synthesis of the desired fusion protein. In some cases, it may be preferable to remove the initiator methionins from the second protein when the new restriction site is introduced. The introduction of recognition sites of 35 endonases of résWeíóm^ both pragenítoras molecules and their postete union by means of tecméás of Recombinant DNA can result in the addition of one or more additional amino acids between the transiting peptic and the second protein. This does not significantly affect the targeting activity if the transit peptide cleavage site remains accessible and the function of the second uncle protein is impaired by the addition of these added amino acids at its N-terminus. The precise cleavage site between the transit peptide and the second protein (cpn or without its initial mettalna) can be mapped using gene synthesis (Stemmar, ef a, (1995) Gene 164:49-53) or similar methods. In addition, the transit fusion peptide may intimately affect amino acids, downstream of the cleavage site. The amino acids at the N-terminus of the mature protein may affect the ability of the transit peptide to target proteins to pestidiae and / or the efficiency of cleavage after importation of the protein. This may depend on the protein to be targeted. See for example. Gums, ef a / . (1988) J. Btoí Chem 283(29):15104-9. In some embodiments, the IRDIG35563 polypeptide is fused to a heterologous serial peptide or a heterologous transit peptide. Nucleic acid molecules and variants and fragments thereof. Isolated or recombinant nucleic acid molecules comprising nucleic acid sequences encoding 1RDIG35563 polypeptides or biologically active portions thereof, as well as nucleic acid molecules sufficient to be used as hybridization probes to identify protein-encoding nucleic acid mottles are provided. with regions of sequence homology. As used herein, the term "nucfeW acid molecule" refers to AON molecules (eg, recombinant DNA, cDNA, gsnomic AON, piastid DNA, mftocendhal DNA) and RNA molecules (eg, mRNA) and analogues of DNA or RNA generated using nucleotide analogues. The nucleic acid molecule can be single-stranded or double-stranded, but is preferably double-stranded DNA. The nucleotide sequences encoding ÍRDIG35563, its variants and truncations, can be synthesized and cloned into conventional ptesmid vectors by conventional means or can be obtained by manipuiacKm. from conventional molecular biology of other constructs containing the nucleoside sequences. Internal unique restriction sites for an IRD1G355S3 coding region can be identified and the DNA fragments comprising the sequences within the restriction sites of the RQIG35563 coding region can be synthesized, encoding each fragment as a specific detected insertion or other variation. of tRDIG35583, The DNA fragments encoding the modified IRDIG35563 fragments can be joined to other fragments of the coding region of IRDIG35563 or other fragments of the coding region of Cry or VIP at appropriate restriction sites to obtain a coding region that encodes the protein IRDIG35563 gives desired full length, deleted or variant IRDIG35§63 protein. For example, one can identify an appropriate restriction recognition site at the start of a first coding region of ÍRDIG35563 and a second restriction site internal to the coding region of IRDIG3S563. Cleavage of this first coding region of 1RD1G35563 at these recognition sites restriction would generate an AON fragment comprising part of the first coding region of IROIG35563. A second DNA fragment flanked by similarly located compatible restriction sites specific for: the IRDIG355S3 coding region can be used in combination with the first DNA restriction fragment to construct a variant. In some embodiments, the nudeic acid molecule encoding a IR0IG35563 polypeptide is a polypeptide that stains the sequence set forth in SEQ ID NO; 1 and variants, fragments and compíementgs of the same. They are also covered. nucleic acid sequences that are complementary to a nucleic acid sequence of the embodiments or that hybridize with a sequence of the embodiments. The nucleic acid sequences can be used in DNA constructs or expression cassettes for transformation and expression in organisms, including microorganisms and plaques. The nucleotide or amino acid sequences may be synthetic sequences that have been designed for expression in an organism including, but not limited to, a microorganism or plant. In some embodiments, the nucleic acid molecule encoding the IRDIG35563 polypeptide is a non-genomic nucleic acid sequence. In some embodiments, the nucleic acid molecule encoding a fRD1G356B3 polypeptide is a non-genomic polyinudeotide having a nucleotide sequence that is at least 50%, 51%, 52%. 53%, 54%, 65%, 56%. 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%. 67%, 68%, 69%, 15 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, '78%, 7”, 80%, 81%. 32% 83% 84%, §6%, 86%, 87%, .88%, 89%, 9034,,91%, 92%, 93%, -94%, 95%, 96%, 97%, 98%, 99% © further identity, to the nucleic acid sequence of SEQ ID NO: 1, where the encoded IRD1G35563 polypeptide has insecticidal activity. In some embodiments, the IRDIG355S3 poimudeotide encodes an IRDIG35563 polypeptide that is at least about 40%. 45%, 50%, 51%, 52%, 53%,... 54%, 55%. 56%, 57%, 58%, 59%, 6β%, 61% 62%. 63%, 64%, -65%, 66%, 67%, 68%, 69%, 70%. 71%, 72%, ?3%, 74%, 75%. 76%, 77%, 78%. 79%, 80%, 81%,82%, 83%, 84%, 85%, 86%, 87%, 88%. 89% 98%, 91%, 92%, 93%. 94%, 95%, 96%, 97%, 98%, 99% or more sequence identity compared to te SEQ 10 NO: 2 and has at least one amino acid substitution, detection, insertion or combination therefore, in Compare 25 with the native sequence. In some repeats. This nucleic acid molecule encodes an IRDIG35563 polypeptide comprising an amino acid sequence that is at least about 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%. 98%, 91%, 92%, 99%, 94%. 95%, 96%, 97%, 98%, 99% or more identity throughout the entire length of the amino acid sequence of the 30 SEQ ID NO: 2, Bacterial genes very often have multiple methionine start codons close to the start of the open reading frame. Often, translation initiation at one or more of these start codons will result in the generation of a functional protein. . The initiation codans may be ATG codons. Certain bacteria such as Satil / us sp. They also recognize the GTG codon as a start codon. On rare occasions, translation into bacterial systems may be infected in a TTQ cell. Furthermore, is normally not determined a prior? which of these codons are used naturally in the bacterium. Therefore, it is understood that the use of one of the alternate methionine codes may also leak the generation of pesticidal proteins. These: pesticidal proteins are encompassed in this disclosure and may be used in the methods of this disclosure. Ss will understand that. When they are expressed by plants, it will be necessary to alter the alternative initiation podon to ATG for adequate translation. The polynucleotide coding sequence can be modified to add a cutoff at the penultimate position after the methionine start cedon to create a restriction enzyme site for recombinant cloning and / or expression purposes. In some embodiments, the IRDÍG35563 polypeptide further comprises an atenine residue at the position after te methionine of the translation iniole. Nucleic acid molecules that are fragments of these nucleic acid sequences that encode insecticidal IROIG35563 polypeptides are also encompassed by the embodiments. A fragment of a nucleic acid sequence may encode a biologically active portion of an IRDIG35553 polypeptide or may be a fragment that can be used as a hybridization probe or PCR primer using methods disclosed below. Nucleic acid molecules that are fragments of a nucleic acid sequence that are contiguous or up to the number of nucleotides present in a full-length nucleic acid sequence disclosed herein, depending on the intended use. Fragments of nucleic acid sequences from these embodiments will encode protein fragments that maintain the biological activity of the IRDIG35663 polypeptide and thus maintain iosectic activity. In some embodiments, the IRpiG36§S3 polypeptide sprouts at least about 15%. at least about 30%, at least about 50%, at least about 70%, 50%, 90%, 95% or more of the insecticidal activity of the full-length ÍRDÍG35563 polypeptide. In some embodiments, the insecticidal activity is against a lepidopteran species. In some embodiments, the insecticidal activity is against one or more insect pests selected from BAW. SAW, FAW. GEW, TBW, SBL, V8C and C8W. In some embodiments, the nucleic acid encodes an IRD1G35563 polypeptide that is at least about 5S%. 55% 60%, 65%^ 70%, 75%, 80%, 81%, 82%. 83%, 84%, 85%, 86%, 87%, 88%, 89%. 90% 91%, 92%. 93%, 94%. 95% 96%, 97%, 98%. 99% or greater sequence identity compared to SEQ ID HO: 2. In some embodiments, sequence identity is calculated using the ClustalW algorithm in the ALIGNX® module of the Vector NTib software package (invltrogen Corporation, Cartsbad, CaliE) with all default parameters. In some embodiments, the sequence diversity is along the entire length of the polypeptide, calculated using the QlustalW aigontm in the ALIQNX module of the Vector NTI software package (Invitrogan Corporation, Carisbad. Gaif.) with all default parameters. The embodiments also encompass nucleic acid molecules that encode variants of the IRDIG35563 polypeptide. Variant nucleic acid sequences encoding the IRDIG35583 polypeptide include those sequences that encode the IR OIG35563 polypeptides disclosed herein but that differ conservatively due to the aegeneraclén of the genetic code, as well as agüites that. they are identical enough as previously disclosed. The varfeotic nucleic acid sequences also include acid: nucteicp sequences obtained: synthetically that have been generated, eg, using site-directed mutagenesis but still encode the polypeptides IRD1G35563 diyuigadqa and described below. The present disclosure provides isolated or crossbinant polypeptides encoding any of the insecticidal IRD1G35563' polypeptides disclosed herein. Endowed with the degeneracy of the genetic code, there are a multitude of nucleotide sequences that encode the IRDK335563 polypeptides of the present disclosure. Changes can be introduced by mutation of the nucleic acid sequences, thus giving rise to changes in the amino acid sequence of the IRDiG35563 polypeptides, without compromising the functional activity of the proteins. Thus, variant nucleic acid molecules can be created by introducing one or more ~11 edit substitutions, additions and / or deletions into the corresponding nucleic acid sequence described herein, of γκλ. r. When one or more substitutes are introduced, cut or deleted, the encoded protein, Mutations can be introduced using conventional techniques, such as mock site genesis and PCR-mediated mutagenesis. Said variant nucleic acid sequences are also covered by the present disclosure. As áltárriativa. Variant nucleic acid sequences may be produced without random mutations along all or part of the coding sequence, such as by saturation mutagenesis, and the resulting mutants may be explored for their ability to confer pesticidal activity to identify mutants that maintain the activity. After mutagenesis, the encoded protein can be expressed recombinantly and the activity of the protein can be determined using standard assay techniques. The polynucleotides of the disclosure and fragments thereof are optionally used as substrates for a variety of recombination and recursive recombination reactions, in addition to conventional cloning methods, as disclosed in, for example, Ausubei, Bergsr and Sambradk. ie, to produce additional plagdioid polypeptide homologues and fragments thereof with desired properties. A variety of such reactions are shortened. Methods of producing a variant of any nucleic acid listed herein comprising recuratively recpmbining said polynucleotide with a second (or more) polynucleotide thereby forming a library of variant polynucleotides are also embodiments of the disclosure, as are libraries. produced, the cells comprising these libraries and any polymuc-tette ^combinant produced: by said methods. Furthermore, said methods optionally comprise selecting a variant polynucleotide from said libraries based on pesticidal activity as well as where said recursive recombination is performed in vitro or ir? live. A number of protocols for generating diversity, including 35 racursive recombination protocols, are available for nucleic acids and have been described in detail in the art. These procedures can be used separately and / or in combination to produce one or more variants of a nucleic acid or a combination of nucleic acids, as well as variants of encoded proteins. Individually and collectively. these. These tools provide robust forms that are widely applicable for generating diverse nucleic acids and pools (including, for example, nuclear acid libraries). For example, for genetic engineering or rapid evolution of nucleic acids, proteins, · pathways, cells and / or organisms with new and / or improved characteristics. S Although distinctions and classifications are made during the accompanying description for clarity, it will be appreciated that the techniques are not normally mutually exclusive. In fact, the various methods can be used individually or in combination, in parallel or in series, to access various variants of sequence. The result of any of the three diversity generation attempts described in e| .0 present document can be the generation of one or more nucleic acids, which can be selected or screened for nucleic acids with. or which confer desirable properties or which encode proteins with or which confer desirable properties. After diversification by one or more of the methods herein or otherwise available to a skilled practitioner, any nucleic acid that occurs with respect to a desired activity or property, eg, pesticidal activity, or such activity at a desired pH, can be selected. , etc. This may include identifying any activity that can be detected, for example, in an automated or automated format, by any of the assays in the art: see, for example, the description of screening for insecticidal activity, below. A series of related (or even unrelated) properties can be evaluated in series or in parallel, according to the expert's criteria. Descriptions of a number of methods for generating varieties for generating modified nucleic acid sequences, for example, those encoding polypeptides having pesticidal activity or fragments thereof, are found in the following publications and the references called therein; Soong, ef aL, (2000) Nat Gepef 25(4):436-439: Stemmer, et al, (1998) Tumor Targetifig 4:1-4; Ness, et a / „ (1999) Nat Biotecmol 17:893-896; Chang, et al., (1999) Nal B / ofecAnóf 17;793-797; MinShuil and Stemmer, (1999) CurrQpy Chem Biol 3:284-290; Christians, et af, (1999) NalBiQtechnd 17:259-264; Chromen. et a!., (1998} Matura 391:288-291: Crameri, éta / ., (1997) W Bíol&oh^l 15:436-438; Zhang, et sí, (1997) PNAS USA 94:45844509; Paiten. et ai, (1997) Ciar Dpm Bibtechno / 8:724-733; Crameri, et a / ,, (1996) Maf ftfed 2:1Q&-103; Crameri, ataL, (1996) Nat Biatechnal 14:315-319; Gates , et a / .. (1996) J Mof B / o¡ 255:373-386: Stemmer, (1996) Sexual POR and Assembiy PCR eri: The Encydüpedia afMoleeuJar8íolo¡¡^ Pubhshers, New York, p. 447-457; Crameri and Stemmer, (1995) StoWteipiteS 16:194-195; Stemmer, etai.. (1995} Gene, 164:49-53; Stemmer, (1995) Science 270:1510: Stemmer, (1995) BI&Techñ&lo^ 13:549-553; Stemmer, (1994} Natare 370'389-391 and Stemmer, (1994) PAMS ÜS.A 91:10747-10751. Mutation methods to generate diversity include, for example, site-directed mutagenesis (Llng, et ai, (1997) Ana / Siar-hem 254(2): 157-178; Date, et al., (1996) Methods Μΰί B¡Ql 57:369-374' Smith, (1985) Ámr f?ev Ggweí'19:423-462;Sotstein and Sbortte, (1985) Setene® 229:1193-1291: Cárter, (1986) Bischem J 237: 1-7 and Kunkel, (1987) The éfficiency of eligenucteotÍde direct mutagenesis'' in filíetele Acids & Mplecii / or Bfology (Eckstein and Lüley, sds., Spripger Védeg, Seriin))* mutagérisis using motoes that condemn (KankeL (1985) AMAS USA 82:488-482: HunkeL et qL, (1987) M&M Enéymo / 154:367-382 and Bass. efe / ., (1988) Scteca 242:249-245): oligonuclide-directed mutagenesis (Zolter and Smith, (1983) Maidocte &zyrho¡ 190:468*500; Zolfer and Smifh, (1987) We / doda Enzymo / 154:329-350 (1987); Zoller and Smifh, (1982) Nudeic Acitls Res 10:6487-65-30 ). mutagenesis of §DNA mottled by fcsforótioats (Tayfer, oí &L (1985) Nucí Acid Res 13:8749-8764; Tayíor, et al., (1985) NuclA^s Res 13:8765-8787 (1965); Nakamaye and Eckstefe, ( 1966) Nucí Acíds Res 14:9679-9698; Sayers, siaL, (1968) Nucí Ací^s Res 16:791-892 and Sayers, et sk, (1988) Nucí Aads R&s 16:803-814): mutagenesis using DNA duplex with holes (Kramer, st AÍ . (1984) Nucí Acáte Res 12:9441-9456; Kratw and Frite, (1987) MóOiods Enzyw / 154:350*367; Kramer, qt af (1988) Roe / Acáte Res 16:7207 and 10 Frite, éf M, (1998) Roe / Acáte Res 16:6W-6999). Additional suitable methods include repair of point mismatches (Kramer, et al. (1984) Ce / / 38:879-887), mutagersis using repair-deficient host strains (Cárter, et al, (1985) Nucí Acid Res 13: 4431-4443 and Cárter, (1987) MetAüds in Enzymó / 154:382-403}, nuítagénes^ (Eghtedarzadeh and (1986) Nucí Acáte Res 14:5115), restriction ssfection and restriction purification (Weife, et al, ( 1986) PPH Tráns R Soc Lund A 317:415-423), total gene synthesis mutagenesis (Nambuir, et al, (ÍSM) &^we 223:1299-1301' SakamaryKhoraná, (19gS) Red AcW Res 14 Wells, efal, (1985) Gene 34*315-323 and Grundstróm, et al, (1985) Rute Acáte Res 13:3305-3316), double-strand break repair (Mandedá, (1986) ARAS USA, 83:7177-7181 and Arnoíd, (1993) CuírOpin Bíof&cti 4:450-455) . Additional details about many of the earlier methods can be found in Wtfiods EnzymN, Volume 154, which also describes controls useful for troubleshooting ccm various mutagenesis methods, Development of olionucleotide probes. An additional method to identify the toxins and smell genes of the invention is through the use of oligonuclidetide probes. These probes are datetable nucleotide sequences. These sequences can be made detectable by virtue of giving an appropriate radioactive label or by being made inherently fluorescent as described, for example, in US Patent No. 6,268,132, As is well known in the art, if the molecule of If the probe and the nucleic acid sample hybridize to form strong base-pairing entities between the two molecules, it can be reasonably assumed that the probe and the sample have substantial sequence homology. Preferably, hybridization is carried out under stringent conditions by 3Ώ techniques well known in the art, as described, for example, in Kelfer and Minale (1993), Te probe detection provides a means of determining in a known manner whether hybridization has occurred. An analysis of tai probes provides a rapid method of identifying genes encoding toxins of the subject invention. The nucleotide segments that are used as probes according to the invention can be synthesized using a DNA synthesizer and conventional procedures. These 35 -Ruéleéfittes sequences can also be used as PCR primers for ampliMcsr genes of the subject invention. Hybridization. As is well known to those skilled in molecular biology, the similarity of two nucleic acids can be characterized by their tendency to hybridize. As used herein the terms "stringent conditions" "stringent hybridization conditions" are intended to refer to conditions under conditions which a probe will hybridize to its target sequence to a delightfully greater degree than to other sequences {eg, at least 2-fold relative to! background). Stringent conditions are sequence dependent and will be different under different circumstances. By controlling the stringency of the hybridization and / or wash conditions, target sequences that are 100% complementary to the probe can be identified (homologous probing). Alternatively, the stringency conditions can be adjusted to allow for some mismatches in sequences, so that lower degrees of similarity are detected (heterologous probing). In general, a probe is less than about 1000 nucleotides in length, preferably less than 500 nucleotides in length, Typically, stringent conditions will be those where the salt concentration is less than about 15 M Na ion, typically about 0.01 to 1.0 M Na ion concentration (or other safes) at pH 7.0 to 8, 3 and the temperature is at least about 30 °C for short probes (eg, 10 to 50 nucleotides) and at least about 60 Q for Lugas probes (eg, longer than 50 nucleotides), Stringent conditions also apply. can be obtained with the addition of destabilizing agents such as formamide. Exemplary low stringency conditions include hybridization with 30 to 35% buffer solution of fermamide, 1 M NaCl, 1% SDS (sodium dodeyl sulfate) at 37 *0 and a wash in 2X IX SSC (20X SSC ~ 3.0 M NaCl / 0.3 M trisodium citraium) at 50 *C to 55 °C, Exemplary conditions of moderate stringency include hybridization in an AO% to 45% fonamide, NaCM.Ó M. 1% SDS at 37°C, and a wash in 0.SX to IX SSC at 55°C to 60°C. Exemplary high stringency conditions include hybridization in 50% formamide, NaC! 1 M< SDS at 1% at 37SC and a wash in 0.1X SSC at 60”C up to 65ñC. Optionally, wash buffers can comprise from about 0.1% to about 1% SOS. The duration of hybridization is generally less than about 24 hours, usually about 4 to 12 hours. Specificity is typically a function of post-hybridization washes, with ionic strength and temperature of the final wash solution being critical factors. For DNA / DNA hybrids. the thermal melting point (Tm) is the temperature (at defined ionic strength and pH) at which 50% of a complementary target sequence hybridizes to a perfectly matched probe. The Tm is reduced by approximately i ’C for each 1% of Incorrect mating; thus, the T-, hybridization conditions, and / or wash conditions can be adjusted to facilitate hybridization of sequences of the desired identity. For example, if sequences with >90% identity are sought, the Tn·! can be decreased 10 *C. Generally, stringent conditions are selected to be 5 C less than T' for the specific sequence and its complement at a defined ionic strength and pH. However, highly stringent conditions may use a hybridization and / or a wash at 1'C, 2C, 3C, or 4C lower than T™; Moderately stringent conditions may utilize a 6 ’C, 7 ’C hybridization and / or wash. 8 *C, 9 ®C or 10 'C less than T» and low stringency conditions may use 11 X, 12 'Q, 13 X, 14 X, 15 X or 20 X less hybridization and / or washes than the T». The Tm (w X) can be determined experimentally or can be approximated by calculation. For DNA-DNA hybrids, the T... can be approximated by asking from the equation Meinkotn and Wahl (1984): T4X) = 81 <5 X í 16.6(log M) + 0.41(% of GC) - 0.61{% of formamide) - 500 / L; where M is the moity of the monovalent cations, % GC is the percentage of guanosine and cltoslha nucleotides in the DNA, % formamide is the percentage of formamide in the hybridization solution, and L is the hybrid length in base pairs. Alternatively, the Tm is described by the following formula (Beliz ef a / ., 1983): K(X) - 81.5 X +16.6(109^1) * 0.41(% of GC) - 0.61(% of formamide) - 600<'L where [Na*] is the molarity of sodium ions, % GC is the percentage of guanosine and cytosine nucleotides in the DNA, % formamide is the percentage of formamide in the hybridization solution and L is the Lenght of! hybrid in base pairs. Using the equations, these hybridization and wash compositions, and the desired Tm, it will be understood by those skilled in the art that variations in the stringency of hybridization and / or wash solutions are inherently described. If the desired degree of mismatch results in a Tm of less than 45X (aqueous solution) or 32X (formamide solution), I prefer to increase the SSC concentration so that a higher temperature can be used. An extensive guide on nucleic acid hybridization is found in Hybridizatfoh wíth Nucleic Acid Probas Valí by P. Tijssén (1993, ISBN* 10:0444898840, ISBN-13: 9 / 80444898845 Hardcoverj and Ausubel et a / . (1995) See also Sambrook et a / (1989). Anti-toxin arithibodies. Antibodies against the toxins disclosed herein, or fragments of these toxins, can be prepared using standard procedures well known in the art. Such antibodies are useful for detecting the presence of IRDIG35563 toxins in plant tissues and a variety of other substances. Such antibodies and antisera are useful in various methods of detection of the claimed IRO1G35563 toxins of the invention and variants or fragments thereof. It is well known that antibodies labeled with a reporter group can be used to identify the presence of antigens in a variety of media. Radioisotope-labeled antibodies have been used in radioimmunoassays to identify, with high precision and sensitivity, the presence of antigens in a variety of biochemical fluids. More recently, enzyme-labeled antibodies have been used as a surrogate for radiolabeled antibodies in the ELiSA assay. In addition, antibodies immunoreactive to the insecticidal Bt toxin of the present invention can be attached to an immobilizing substance such as a polystyrene well or bead and used in immunoassays to determine whether Bt toxin is present in a test sample. anti-MRDIG35583 antibodies are also useful for isolating quantities of 1RD1G35563 toxins from recombinant production systems or natural sources. So provided is a kit for detecting the presence of an IRBIG35563 polypeptide or detecting the presence of a nucleotide sequence encoding an IRDIG35583 polypeptide in a sample. In one embodiment, the kit provides antibody-based reagents for detecting the presence of an iRnifi 35563 polypeptide in a tissue sample. In another addition, the kit provides labeled nucleic acid probes useful for detecting the presence of one or more polynucleotides encoding an IRDIG35563 polypeptide. The kit is provided together with reagents and reagents suitable for performing a detection method, as well as instructions. for the use of the kit. Transgenic expression of IRDiG3?5563. The subject protein toxins can be applied or provided to contact the target insects in a variety of ways. For example, IRD1G355S3 toxins can be used as plant-incorporated protectants in transganic plants (produced by and present in the plant). Expression of the toxin genes can also achieve selectivity in specific plant tissues, such as roots, These leaves, &te, This can be accomplished through the use of tissue-specific promoters. A preferred reaffirmation of the subject invention is this transformation of plants with genes encoding the subject insecticidal protein or its variants. The transformed plants are resistant to prolonged attack by a target insect pest by virtue of the presence of control amounts of the subject insecticidal protein or its variants in the cells of the transformed plant. By incorporating and expressing the genetic material encoding a 1RDIG35563 toxin into the genome of a plant eaten by a particular insect pest. the adult or larvae will die after consuming the food plant. Numerous members of the mnocotsyedonous and dicotyledonous classifications have been transformed. Transgenic agronomic crops as well as fruits and vegetables are of commercial interest, Tatescuítivos include, but are not limited to, mate, rice, soybeans, canola, sunflower, alfalfa, sorghum, wheat, cotton, peanuts, tomatoes, potatoes and the like. . There are numerous well-known techniques for introducing foreign genetic material into monocot or dicot plant cells and for obtaining fertile plants that stably maintain and express the introduced gene. In a preferred embodiment, IRDIG35563 or a variant is administered orally via a transgenic plant comprising a nucleic acid sequence expressing a toxin of the present invention. The present invention provides a method of producing a transgenic plant resistant to insects, which comprises introducing a nucleic acid molecule of the invention into the plant where the toxin is expressed in the transgenic plant in an amount effective to control an insect. In a non-limiting example, a basic donation strategy may be to subdonate full-length or modified IRDIG35563 coding sequences into a plant expression piasm at the Ncai and Sj&i restriction sites. The resulting plant expression cassettes contain the IROIG35563 coding region under the control of plant expression elements (eg, plant-expressing promoters, 3'-terminal transcription termination, and pcyhademlate addition determinants and the like), are sublayered into a pthesmid binary vector, using, for example, the Gateway® technology or standard restriction enzyme fragment cloning procedures, LR Clonase1^ (Iwitrogea, Qarlsbad. CA) for example, can be used to recombine the full-length and modified plant gene expression cassettes into a plant transformation plasmid binary if Gateway®·' technology is used. It is convenient to use a binary plant transformation vector that harbors a bacterial gene that confers resistance to the specific antibiotic as long as the plasmid is present, in E. poli and Apf'ph^et&wm cells. ts It is also convenient to employ a binary vector plasmid containing a plant-expressible cleavable marker gene which is functional in the desired plant hosts. Examples of selectable marker genes expressed in plants include but are not limited to those encoding the Tn5 transposon aminoglycoside phosphotransferase (spMi) gene, which confers resistance to the antibiotics kaaamtein, neomycin and G418. as well as those genes that encode resistance or tolerance to glyphosate, hygromycin, methotrexate, phosphinothricin (bialafosj, ímldszolinones, suifonylureas and tirazolopinmidne herbicides, such as dorosulfurone, bromoxynium, dalapon and the like. Alternatively, the plasmid structure of the binary nsfom rage vector containing the ÍRDIG35563 gene insert is performed by restriction digestion fingerprint adc mapping of plasmid DNA prepared from candidate Agrobactenum isolates by conventional molecular biology methods well known to those skilled in the art. Agrobactertom handling matter, The use of the term "nucleotide construct" herein is not intended to limit the embodiments to nucleotide constructs comprising DNA. Constructions of nucleotides, particularly polynucleotides and oligonucleotides composed of ribonucleotides and combinations of ribonucleotides and deoxyribonucleotides, may also be employed in the methods disclosed herein. The nucleotide constructs, nucleic acids, and nucleotide sequences of the embodiments further encompass all complementary forms of such constructs, molecules, and sequences. In addition, the nucleotide constructs, nucleotide molecules, and nucleotide sequences of the embodiments encompass all nucleotide, molecule, and sequence constructs that may be employed in the methods of the embodiments for transforming plants including, but not limited to, those comprising deoxyribonucleotides, dbonucleotides and combinations tí® the same. Such deoxyribonucleotides and ribonucteophides include both naturally occurring oe molecules and synthetic analogues. The nucleotide constructs, nucleic acids, and nucleotide sequences of the embodiments also encompass all forms of nucleotide constructs including, but not limited to, single-stranded forms, double-stranded forms, hairpins, stem-loop structures, and the like. A further embodiment relates to a transformed organism, such as an organism selected from plant and insect cells, bacteria, yeast, baculovirus, protozoa, nematodes, and algae. The transformed organism comprises a DNA molecule of the embodiments, an expression cassette that It comprises the AON molecule or a vector comprising the expression cassette, which can be stably incorporated into the genome of the transformed organism. The sequences of the embodiments are provided in DNA constructs for expression in the organism of interest; The construct will include 5' and 3' regulatory sequences operably linked to a sequence of the embodiments. The term "operably linked", as used herein, refers to a functional link between a promoter and a second sequence, where the ίηΐοίη promoter mediates the transcription of the DNA sequence which corresponds to the second sequence. In general, operably linked means that the nucleic acid sequences being linked are contiguous and in cases where it is necessary to join two protein-coding regions in the same reading frame, the construct may also contain at least one additional gene that I know of. it will ootransform in the organism. As a matter of fact, the additional gene(s) can be provided in multiple DNA constructs. Said DNA construct is provided with a variety of restriction sites for insertion of the IRDIG3S563 polypeptide gene sequence of the disclosure to be under the transcriptional regulation of regulatory regions. The DNA construct may further contain selection marker genes. The DNA construct will typically include in the S' to 3' direction of transcription a transcription and translation initiation region (i.e., a promoter), a DNA sequence of the embodiments, and a transcription termination region. and translation (ie, termination region) functional in the organism that serves as the host?. The transcription initiation region (ie, the promoter) can be native, analogous, exogenous, or heterologous to the host organism and / or to the sequence of the embodiments. Additionally, the promoter can be the natural sequence or, alternatively, a synthetic sequence. The term "exogenous" as used herein indicates that the promoter is not found in the native organism into which the promoter is introduced. When the promoter is exogenous or heterologous to the sequence of the embodiments, it is intended that the promoter is not the native or naturally occurring promoter for the operably linked sequence of the embodiments. A chimeric gene, as used herein, comprises a coding sequence operably linked to a transcription initiation region that is heterogenic to the coding sequence. When the promoter is a native or natural sequence, the expression of the operably linked sequence will be altered from the naturally occurring expression, resulting in an alteration in e! phenotype, In some embodiments, the DNA construct comprises a polynucleotide encoding an IRDIG35563 polypeptide of the embodiments. In some embodiments, the AON construct comprises a polynucleotide encoding a fusion protein comprising a patipephid 1RDJG35563 of embodiments. In some embodiments, the DNA construct may also include a sequence 3G transcription enhancer. As used herein, the term "enhancer" refers to an AON sequence that can stimulate promoter activity and can be an innate element of the promoter or a heterophobic element inserted to enhance the level or tissue specificity of a promoter. . Various enhancers may also be used including, introns with enhancing properties of gene expression in plants (US Patent Application Publication No. 2009 / 0144863), the ubiquitin íñtóh (i.e., maize ubiquitin iwon 1 (see, for example, the NCR! sequence S94464)), the omega enhancer or the omega prime enhancer (Gailie, et a / ,, (1989) MofeéPfe? Bláto^y of RNA ©d, Cach (Liss, New York) 237-256 and fíalfie, ®f al. (1987) Gene 60:217-25), the QaMV 3&S enhancer : (see, for example, Berifey, he at, (1990) EM8Ó 7.9:1685-96) and faith enhancers US Patent Number 7,803,992, each of dual toes is incorporated by reference. The list of previous enhancers is not intended to be limiting. Any suitable transcriptional enhancer may be used in the embodiments. The temínacíún region can be native to the initiation region of the transoripetón, can be native to the operably linked DNA sequence of interest, can be native to the plant host or can be obtained from another fe source, ie, exogenous or heterologous the promoter, the sequence of interest, the plant host, or any combination thereof). Convenient termination regions can be obtained from the A tomefactens Ti plasmid, such as the oetopin-synthese and thenopaline-synthese termination regions. See also, GuerineaU, et al (1991) AM-.Gen. Genetic 262:141-144; Proudfeot. (1991) Ce# 64:671-674; Sanfason, et ai, (1991) Genes Dev: 5:141-149: Megan, et al, (1996) Ptot Gsff S: 1261-1272: Munroe, et ak, (1990) Gene 91:151-158; Bailas, eta¿, (1989) Nucteic Acid Res, 17:7891-7903 ydcshi, et<> (1987) Nudefc Acid Res. 15:9627-9639, When appropriate, a nucleic acid can be optimized to obtain an increase in its expression in the host crganism. Thus, when the host organism is a plant, synthetic nucleic acids can be synthesized using codons preferred by the plant to obtain improved expression. See, for example, Campbell and Gowri, {1990) Plañí Physíol. 92:1-11 for a discussion of the preferred use of the host. For example, although the nudeic acid sequences of these embodiments may be expressed in both dicot and ptartaff species, the sequences can be modified to account for the specific preferences and GC content preferences of monocots or dicots since these preferences have been shown to differs” (Murray et al (1989) Rugtefc Acáte Res. 17:477-498). In this way, the maize preferred codon for a particular amino acid can be derived from genetic sequences that have died from maize. The use of maize for the 28 genes of maize plants is listed in table 4 efe Mww et a7, 26 cited above. Methods for synthesizing the plant-preferred gene sweep can be found in Murray, et al., (1989) Modfefe AciW Res. 17:477-498 and Liu H el al. Mof Río Rep 37:677684, 2010, incorporated herein by reference. A usa table for Zea marzo can also be found at kazusá.or.jp / fcgi-bín / show.cgi?specfes^677, which can be accessed using the prefix www. A Gfycáw usage table can be found at maxan kazusa.or.jp / í'cgibin / shów.cgí?speciés~3M which can be accessed using the prefix www. In some embodiments. the recombinant nuctelco acid molecule encoding an IRDIG35563 palipeptide is codon-optimized from maize. In some embodiments, the fecombinonts nucleic acid molecule encoding an IRDIG35§63 polypellid has saja-optimized shorts, Additional sequence modifications are known to enhance gene expression in a cellular host. These include the ©gmhadbn of sequences encoding false polladenyladon da signals, de signals. exon-infrench splice sites, transpuson-like repeats, and other sequences that have been well characterized that may be detrimental to gene expression. The GC content of the sequence can be adjusted to medium levels for a host cell. determined., according to. Cátente referring to genes: known expressed^· in the host petate. The expression "host cell", as used herein, refers to a cell that contains a vector and supports the application and / or expression of the expression vector. The 5 host cells may be proc-anos cells. tefes as £. co / i or eukaryotic cells, such as yeast, insect, amphibian or mammalian cells or monocotyledonous or dicotyledonous plant cells. An example of a monocotyledonous host cell is a maize host cell When possible. Sequence $e is modified to avoid the expected hairpin secondary mRNA structures. The expression cassette may further contain 5' leader sequences. Such leader sequences may act to enhance translation. Translation leaders include: picornavirus leaders, eg, EMCV leader (endephaphomyocarditis 5' non-coding region) (Elroy-Stein, et al., (1989) Proc, Nati, Acad. Ser USA 86:6126- 8130); potyvirus leaders, eg, TEV (tobacco etch virus) leader (Gallte, et al., (1995) Gene 165(2):233-238), MDMV (Maize Dwarf Mosaic Virus 15) leader, |a human immunoghebulin heavy chain binding protein (SiP) (Macejak, ef a / ,, (199'1) Natura 353:90-94): untranslated leader of the mRNA of the virus envelope protein alfalfa mosaic (AMV RNA 4) (Jobhng, el si., (1987) Natura 325.622-625): leader of the taffy mosaic virus (TW) (Gallte, et al, (1989) én Molecular Systogy of RNA, ed. Gech (Líss. Hueva ¥órk) < p. 237256) and leader of the maize chlorophye mottle virus (MCW V) (Lommel, et al., (1991) VMogy 81:382-385), 20 See also, Délía-Cíoppa, ef a / ., (198?) Plan! Pay it!. 84.-965-968. Such constructs may also contain a 'signal sequence' or ''leader sequence'' to facilitate either ootranslational or posttranslational transport of the peptide to certain intracellular structures, such as the doroplast (or other plastid), the endoplasmatic reticulum, or the Golgi apparatus. Signal sequence, as used herein, refers to a sequence that is known or suspected to result in cotranslational or posttranslational transport across the cell membrane. In euGariotes, this normally involves secretion into the Golgi apparatus, resulting in some degree of glucosiladon. Insecticidal toxins from bacteria are often synthesized as protoxins, which are protochemically activated in the gut of the target pest (Chang, (1987) Wthods Enzymo / : 153:507-516). In some embodiments, the signal sequence is in the native sequence or can be obtained from a sequence of these embodiments, Leader sequence1', as used herein, refers to any sequence that, when translated, results in an amino acid sequence sufficient to trigger the cotranslational transport of the peptide chain to a subcellular organelle. Thus, this included leader sequences directing transport and / or gtacosylation via endoplasmic reticulum passage, vacuole passage, ptastodes, including cyoroptestans, mifecondnae, and the like. Nuclearly-encoded proteins directed to the lumen of the chloroplast cells have a characteristic bipartite transit peptide composed of a signal peptide for diffGGionaiwnto ss^^ and a signal peptide for directing to the lumen. The eStromal targeting information is found in the aminopraximal portion of the transit peptide. The targeting signal peptide a! The lumen is located in the proximal portion of the transit peptide and provides the information for directing to the lumen. Recent investigations in proteomics of the higher plant chloroptest have succeeded in identifying numerous lumen proteins encoded in the nucleus ( Kieselbach et al. FEBS ί,ΕΤΓ S 480:271-276. 2000; Peltier st ai. Piara Cali 12:319-341, 2000; Sricker et ai. Biochtm. Biophys Acta 1503:350-356,2001}, which lumen-directed signal peptide can potentially be used in accordance with the present disclosure. Approximately 80 Arabid&psis proteins. thus eats homologous protein from spinach and garden pea, are reported by Kieseíbaoh et al, Photasyafftesíx Research. 78:2.49264,2003. Table 2 of this publication, which is incorporated herein by reference, discloses 85 proteins from the lumen of chloroplasts, identified by their reference number (see also United States Patent Publication 2009 / 2009). 09044298). In addition, the recently published sketched version of the rice genome (Goff al ai, Science 296:92-100, 2002) is a suitable source for the lumen-directed signal peptide that can be used in accordance with the present disclosure. Elpropiosate transit peptides (DTPs) include chimeric CTs comprising, but not limited to, an N-terminal domain, an éentráí domain or a C-terminal uri domain of a CTP of 1-deoxy-D xyiose-5-phosphate synthase Oryza saf / va, superoxide dismutase from Óryza sariva, soluble starch synthase from Oíyzasafrya, NADP-dependent ds melic acid enzyme from Oryza sSWé, phospho-S-dohydro3^ésoxyhéptonate aidolséá 2 from Gryzasativa, L-ascorbate peroxidase 5 from Oryza sativa, Hydrosoluble phosphoglucan dikinase from Oryza sativa, ssRUBISCO from Zea maya, beta-glucosidase from Zea maya, killelo dehydrogenase from Zea msys, thioredoxin type M from Zea mays (US Patent Application Publication 2G12(0304336). The IRDIG35563 polypeptide gene to be targeted to the chloroplast can be optimized for its expression in the ctoroplast to account for differences in use between the plant node and this organ. In this way, the nucleic acids of interest can be synthesized using preferred sequences of doropiastcs. In preparing the expression cassette, the various DNA fragments can be manipulated to provide the DNA sequences in the proper orientation and, as appropriate, in the proper reading frame. For allo, adapters or proofreaders can be used to join the fragments. 30 DNA, or other manipulations can be performed to provide convenient restriction sites, remove superfine DNA. remove .restriction or similar sites. For these purposes, mutagenesis, primer repair, restriction, annealing, resuscitation, e.g., -transitions and transversions, can be applied. In the practice of these embodiments, various promoters may be used. Promoters can be selected based on the desired results. Nucleic acids can be combined with constitutive, tissue-preferred, unspeakable, or other promoters for expression in the host organism. Constitutive promoters suitable for use in a plant host cell include, for example, the core promoter of the Rsyri? and other promoters: constituents disclosed in documented WO 1999 / 43838 and in faith US Pat. Number 6,072,050: the central CaMV 35S promoter (Odelí. el ai.. (1985) Natere 313:810-812): rice actin (McEIroy, e / 3 / ., -1990} PteníCefí 2:163-171); ubiquitin (Cnristensen, ef ai., (1989) PlaatMol. Bis!. 12 619-632 and Chnstensen, et al., (1992) Plañí Mol. Blol. 18:675-689); pEMU (Last, el ai., (1991) Táaor. AppK Gandí, 81:581-588); MORE 5 .{Vallen, el a / „ (1984) EMBQ J 3:2723-2730); the ALS promoter (US Patent Number 5,659,026) and the like. Other constitutive promoters include, for example, those described in US Pat. No. 5,608.14; 5,608,144: 5,604,121; 5,569,597; 5,466,785; 5,399,680: 5,268,463; 5,608,142 and 6,177,611. Depending on the desired result, it may be beneficial to express the gene from there; from an induced promoter. To regulate the expression of the nucleic acid sequences of these embodiments in plants, promoters induced by festoon are of particular interest. Such injury-inducible promoters can respond to damage caused by insect feeding, and include the inhibitor gene. of potato proteinase (pin II) (Ryan, (1990) Ano. Rev. PhyiopatR 28:425-449; Cuan, of al, (1996) Nátare BiQt&chnalngy 14:494-498): wunl and wun2. Patent da EE.IJU. Number 5,428,148: win1 15 and win2 (Stantord, ata / ., (1989) Mol. Gen. Geoet 215:200-208): systemin (McGurl, s¿f(1992) Sotence 225:1570-1573); WIP1 (Rohmeier, ef aL (1993) Plañí Mol. BioK 22:783-792; Eckelkamp, ​​et al, (1993) FESS' L&Por$ 323:73-76): MPI gene (Corderok, el al. (1994) Pl&nt J 6(2)141-150} and the like, incorporated herein by reference. In addition, pathogen-induced promoters can be used in the methods and constructions of nucleotide rearleations. Such pathogen-induced promoters include those of the pathogenesis-related proteins (PR proteins), which are induced after infection by a pathogen; by PR proteins, SAR proteins, beta-1(3-glucanase, chyinase, etc. See, for example, Redolfi, &t al. (1983) Neth. J. Plañí Pafiiol. 89'245-254, Uknes, eí aE ( 1992) Plañí Cé / / 4: 645-856 and Van Loen. {1985) Plañí Mol. VM. 4:111-116. See also document WO 1999 / 43819, incorporated herein by reference; Promoters that are highly expressed in the area of ​​the site of infection by the pathogen are of interest. See, for example, Marinean, ét af, (1937) Pía / it Mol. Block 9:335-342; Matton, al., (1989) Molecular Plant-Mlcrobe Int&rac&ws 2'325-331; Somsisch, &t al. , (1988) Proc. nati. Acad. Ser USA 83:2427-2430; Somsisch. et al, (1988) Mol. gene; Gapaf, 2:93-98 and Yang, (1996) Pmc. Nad. acad Said. USA 93:14972-14977. See also Chen. et al. (1996) Plain. 1Ü:855-S66; Zteng, at ai., (1994) Proc. nati. Acad. Sel. USA 91:2507-2511; Warner, al al. (1993) P / anf J. 3:191-201; Stebertz, al., (1989) Plant Cali 1:961-968; US Patent Number 5,750,386 (unspeakable by nematodes) and three references cited therein. Of particular interest is the inducible promoter of the maize PRms gene, whose expression is induced by the pathogen Pusamo?? mopiliform (see, for example, Cordero, al ai, (1992) 35 PtiysiOl. Mol. Piant Paifi.41:189-200). Promoters can be used by chemical agents to modulate the expression of a gene in a plant through the application of a chemical regulator: hexagon. Depending on the. Objectively, the promoter can be a promoter induced by a chemical agent, where the application of the chemical agent induces the expression of the gene, or a promoter repamibie by a chemical agent, where the application of the chemical agent represses the expression of the gene. Chemically inducible promoters include, but are not limited to, the mate ln2-2 promoter, which is activated by protectants from the herbicide benzenesuifonamide, the maize GST promoter, which is activated by hydrophobic ectrophilic compounds: which are used as pre-germination herbicides, and the tobacco PR-1a promoter, which is activated by salicylic acid. Other chemically regulated promoters of interest induce spheroid-responsive promoters (see, for example, the glucoorthioid-induced promoter in Schena, et al., (1991) Proc, Nati. Acad. Ser. USA 88:10421-10425 and McNeis, éí a¿, (1098) Pfant J. 14(2):247-257) and promoters Induced by tetracioline and repressed by tetracycline (see, for example, Gafe, pf af,, (1991) Mol Gen. Gehét 227:229-237 and US Pat. Numbers 5,814,618 and 5,789,156), incorporated herein by reference. Tissue-preferential promoters can be used to target IRDIG35553 polypeptide expression within a plant tissue even if tissue-preferential promoters include those discussed in Yamamoto, efa / „ {1997) Pfentd, 12(2)255-265; Kawamata, al a¿, (1997) Plan / Ce / / Phys / fo. 38(7):792-883: Háhsén, éf afe (1997) Mol Gen Géoet. 254(3): 337-343, Russell, Eiafe (1997) Transgenic Res. 6(2).-157-168; Rmehart, et al. {19®) Tweeted Pbysioi. 112(3): 1331-1341; Van Gamp, huh? al., (1996) Piafó Phyxioi. 112(2):525-5¾ Ganevascint ef a'.. 11996j Piafó Physioi. 112(2):513524; Yántamete, et al, (1994) Piafó: Caí / P / iysifó. 35(5):773-778: Lam, (1994) Ré^sr Probl. QsilBifffó. 20:181-196: Orozco, et al, (1993) P / ant WM 23(6):1129-1138: Matsuoka, eí aL, (1993) Frac W?’ AeM Set USA 90(20):9586-9590 and Guevara-Garcia, ef a¿, (1993) Plan / ¿ 4(3):495-605. Such promoters can be modified, if necessary, so that their expression is lower, Leaf-preferred promoters can be found in Yamamoto, gt at, (1997) PiántJ. 12(2):255 / 265; Kwon. ef afe (1994) Ráht PhysM 105:357-67; Yámamoto, efefe (1994). Plañí Ce# Physioi. 35(5):773-778; Goto?, there. (1993)fWdu, 3509-18. Orazco, I heard the.. (1993) AWfefoL Btol 23(6): 1129-1136 and Matsu&ka, el al, (1993) IW-W». Wow. So, USA 90(20):9586-9590. Promoters with root preference and root specificity are known and can be selected from many that are available in the literature or that have been isolated de novo from various companion species. See, for example. Hire, at a / ., (1992) Plan / Mók Biol. 20(2):207-218 (glutamine simetase gene specified from soybean rafe); Keller and Baumgarlner. (1991) P / am Ce# 3(18):1051-1061 (raphe-specific comroi element in green bean GRP 18 gene); Sanger, et al., (1990) Plant Mo.l. Bio / . 14(3):433-443 (rafe-specific promoter of the AgroSactefium temefecréns mitten synthase (MAS) gene) and Miso, ef a / „ (1991) Piafó Ce# 3{1};11-22 (clone da Full-length cDNA encoding cyiosoil glutamine synthetase (GS), which is expressed in soybean roots and root nodules). See also, Bogusz, el (1990) Rlant Celí 2(7):633-641, describing two root-specific promoters isolated from the non-nitrogen-fixing legume Parasponm andersomi and non-nitrogen-fixing Erame tom^ hemoglobin genes. related nitrogen. The promoters of these genes were linked to a te β-glupronidase indicator gene and were introduced into non-legume Ntoof / ana tabacum as well as into leguminous te omtofetw Lots and in both cases the specific promoter activity of ralees was achieved. Leach and Aóyagl (1991) describe their analysis of the promoters of the highly expressed miC and rc© strain-inducing genes of Agrobacterium rhizogenes (see, Ranf Stínae (Limarte) 79(1):69-76). They concluded that enhancers and tissue-preferential DNA determinants are dissociated at these promoters. synthase is especially active in the epidermis of the root tip and that the TR2 gene is root specific in the intact plant and is stimulated by festoons in leaf tissue, an especially desired combination of characteristics for use with a gene insecticide © lanada (see, EMBO 4,6(2):343-35()), the TR1' gene fused with npf# (neomitea1Q phosphotransfephase H) presented similar characteristics. Promoters with preferential radicular addictanal include the VÍENOD-GRP3 gene promoter (Kuster, et a / .. (1995) Pi&nt Mol Bdl 29(4):759-772) and its ro|8 promoter (Capaba. st al, (1994)^^1 ftfoí.8 / al 25(4):681- 591. Also see ER, UU Patent Numbers 5 837 876: 5 750 336: 5 633 363; 5 459252: 5 401 836; 5 110 732 and 5 023 179. The root-preferential regulatory sequences of Arateopte italiana are disclosed in the document US20130117883. The promoters, with preference. seminal* include both promoters with seed specificity (those promoters: that are active during the development of these som®s$ such as promoters of seed storage proteins) and seed germination promoters (those promoters that are active during the seed germination). See, Thompson, et al. (1989) SfoEssays 10:106, incorporated herein by reference. Such seed-preferred promoters include, but are not limited to, Ciml (cytokinin-induced message): cZ19B1 (19 kDa zain from mate); and miips (nfio-inositol-l -fasfatg-slifia (see US Patent No. 6,225,529, incorporated herein by reference). Gamma-zain. and Glb-1 are promoters with endosperm specificity. For dicotites, the seed-specific promoters Include, but are not limited to, Kanitz trypsin inhibitor 3 (KTI3) (Joluku and Goldberg, (1989) P / ant Ce# 1:10791093), bean β-phase, hapin, P-conglcmin, wisteria 1 , soy teat, eruciferal, and the like For monocots, promoters with seed specificity include, but are not limited to, the 15 kDa corn zein, the 22 kEM tena, 27 kDa zain, la g-zein, waxy , shrunken 1, shrunken 2, globulin 1. ele See also document WO 2000'12733, which discloses seed-preferred promoters of the smN and enu'2 genes, incorporated herein by reference, In dícctííédónéás,. promoters with a preference for the seed include, but are not limited to, promoter ArabtepsiA seed coat, pBAN; and all déÁ.rabfeops / s„ p26, p63 and p63tr early seed promoters (US Patent Nos. 7,294,760 and 7,347,153). A promoter with an expression that is "preferential" for a particular tissue is expressed in that tissue to a greater degree than in at least one other tissue of the protein. Some promoters with tissue preference show expression almost exclusively in the particular tissue. When a low expression level is desired, weak promoters will be used. Generally, expression is a weak promoter, tai cams was used herein, refers to a promoter that lowers the expression of a coding sequence at a low level. A low level of expression is intended to refer to levels between about 1 / 1000 transcripts, to approximately 1 / 100,000 transcripts to approximately 1 / 500,000 transient. As an alternative, don't know what expression 'weak promoters' also encompasses promoters that 'fake expression only in some cells and not in others to obtain a low overall level of expression. When a promoter drives expression to unacceptably high levels, portions of the promoter sequence can be deleted or modified to reduce expression levels. These weak constitutive promoters include, for example, the core promoter of the Rsyn7 promoter (WO 1999 / 43838 and US Patent No. 6,072,300), the CaMV 35S core promoter, and the like. Other constitutive promoters include, for example, those disclosed in United States Patent No. 5,608049; 5,608,144: 5,604021; 5,569,597; 5,466,785; 5,399,680; 5,268,463; 5,608,142 and 6,177,611. incorporated herein by reference. The list of promoters above is not intended to be limiting. Any suitable promoter can be used in the embodiments. In general, the expression cassette will comprise a marker gene settable for screening transformed cells. Selectable marker genes are used to select for transformed cells or tissues. Merchant genes include genes encoding antibiotic resistance, such as those encoding neomycotic fetransferase II (NEO) and hygromycin 20 phosphotransferase (HPT), as well as genes that they confer resistance to herbicidal compounds such as glufosinate ammonium, hromexinii, imidazoylnones, and 2,4-dictorophenoxyacetete (2,4-D). Additional examples of suitable selection marker genes include, but are not limited to, genes encoding dcranfenicol resistance (Narrara Estrella. el a / .. (1963) EMBO J. 2:987-992); methotrexate (Herrera Estrella, (1983) Natura 303:209-213 and Meijer, &t a / ., (1991) Plañí Mol Ble!. 16:807-820); streptomycin (Jones, et a / .. (?987) Mol Gen. Géhet 210:86-91): spectinomio.na (Bretegne-Sagnard, ef 0996) Ltánsgenic Res, 5:131-137); bteomycin (Hille, ata / ,, (1990) Plañí Mol BM 7:171-176); sulfonamide ( Guerioeau, staL (1990) Pian? Mol Biol. 15:127-136 ); bronwinil (Stalker. ef (1988) Setenes 242:419-423 ); glyphosate (Show, yes a / ., (1986) Science 233:478-481 and US patent applications sene numbers 10 / 004,357 and 10 / 427,692); phosphinothricin (DeBlocfo et al (1987) EMBO 30 J. 0:2513-2518) See, generally. Yarranton, (1992) Curo Opin. Biotech. 3506-511; Chosiopherson, ef ai, (1992) Nati Aesd. SW*. USA 89:6314-6318; Yao, ef al„ (1992) Cali 71 :63-?2; Rezmkrsff, (1992) Mal. MfcroPM 6:2419-2422; Barkley, et al., (1980} in The Operan, pp. 177-220: Hu. al ai, (1987) C&U 48:555-566; Brown, et al., (1987) Bell49:603-612; Figge , etsl., (1988) Cali 52:713-722; Déuschte, uf al., (1989) Proc. Apad, USA 86:5400-5404; Fuerst ote / , (1989) Prec. HaS. AcaiT Scí USA 66:2549-2553; Deuscbíe, «, (1990) Setenes 248:480-483; Gossen, (1993) Ph.D. Thesis, University of Heidelberg: Queens, et at, (1993) Prec. Nati. Asad. Set. USA 90:1917-1921; Labow, el al, (1990) Mel. Cell. Blk 10:3343-3366; Zambretti, «4Μ, 0982) Prec. Nafo Apgrf. Seí USA 89:3952-396$ Baim, et a / ., (1991) Rrsc, Natt AcaÓ-Ser, USA 88:5072^5076; Wybpr'ski, yes,. (1991) Nudeic Acid Bes. 19:464732 4653; Hiienand-Wissmán, (1889) Tapies Mal. Strua. βίοι. 10:143-162; Degentólb, ef a / .. (1991) AntimÍGrah. Agent CtemofAer, 35:1591-1595; Kieinschnídt, ef yes, (4988) Bi&chemistfy 27:1094-1104; BonH (1893) Ph.D. Thesis, Uáiwsity of Heideiberg; Góssem et af., (1992) Proñ. NM AcM Sw, USA 89:5547-5551; Oliva, sta / .. (1992) Antimicreb. Agent Ch&malh&r. 36:913-919; Hlavka. etal, í 1985) Handbock af Exp&rim&nfei Pharrnac.ofogy,V^ 78 (Sprmger-Verlag. Berlin) and Gilí, eta¡. (1983) Nature 334:721-724. Such disclosures are incorporated herein by reference. The above list of selection marker genes is not intended to be limiting. Any detectable marker gene can be used in the embodiments. Those of skill in the art of obtaining transformed plants via AgroMcfem-mediated transformation methods that other Agro^cieifem strains may be used in addition to 2707S and that the choice of strain may depend on the identity of the host plant species to transform. The methods of these embodiments involve introducing a polypeptide or polynucleotide into a plant, "introducing", as used herein, refers to presenting the plant with the O polynucleotide; polypeptide in such a way that the sequence gains access to the interior of a human cell. The methods of these performed do not depend on a particular method of introducing a polynucleotide or pslipeptide into a plant, but only on whether the polynucleotide or polypeptide gains access to the Interior of: at least one of the plant, Methods for introducing pblinucfeotides or polypeptides into plants include, but are not limited to, stable transformation methods, transient transformation methods, and virus-mediated methods. 'Stable transformation, as used herein, means that the newpheotide construct introduced into a plant integrates into the plant's genome and can be inherited by offspring of the plant. Transient transformation, as used herein, means that a polynucleotide is introduced into the plant and does not integrate into its plant genome or that a polypeptide is introduced into a plant, Piante, as used in The present document refers to complete plants, plant organs (for example, leaves, stems, rates, etc.), seeds, plant cells, propagation ios. embryos and offspring. Plant cells can be differentiated to undifferentiated (eg, caites, cells in suspension culture, protopiasts, leaf cells, root cells, phloem cells, and pollen). The transformation protocols as well as the protocols for introducing nucleotide sequences into plants may vary depending on the type of plant or plant cell, ie, mentotyledonous or dicotyledonous, selected for transformation. Suitable methods of introduction of nucleotide sequences and subsequent insertion into the plant genome include microinjection (Crossway, et al., (1985) 3 / otecbfwques 4:320-334), ectropration (Riggs, ef al, (1986 ) Proa Nati Acad Sai USA 83:5502-5306). Agrubaotehám-mediated transformation (US Patent Numbers 5,563,055 and 5,981,840), direct gene transfer (Paszkowski M<, (1984 EMBO A 3:2717-2722) and ballistic particle acceleration (see, for example, US Patents from USA Numbers 4,946,050: 5,879,918;^ and 5,932,782; Tomes, al, (1995) in Plant Cali Tissue, and Qrgan ed. Gamborg and Phillips, (Springer-Vérfeg, Berlin) and McCabe, yes a / „ 0988) SfcWcÁrK:<tógy with Leol (documented WO 00 / 28056), For the fransformacrón of potatoes, see. Tu, ef sL (1998) AW Mofecufer ®ótogy37:829-838 and Chong, et al„ (2000) íransgcwc Fwarcfc 9:71-78, Additional treatment procedures can be found § én Wtessinger. et a / ., (1988) Arm, Rsk Genét 22:421-477; Sanford, yes, (1987) Particteafe Science and T&vhnalogy 5:27*37 (onion); Chnstou, et si. (1988) nanf Phy^ 87:671*674 {soybean); McCabe, eta / ., (1988) WTe^ncfógy 6:923-926 (soybean); Raer and McMufeft, (1991) / 0 W&b Ceh Dev. 27R175-182 (soybean); Singh, at a / ., (1993) T^eor. AppL Genet 96'319-324 (soybean): Daifa, &f&¡„ (1990) ^otecfinotogy 8:736-740 (rice); Klein, ef<, (1988) Rroc, Acad. USA 95:4305-4309 (corn); Klein, efa¿, 10 (1 §88) B / ofetemo / ogy 6:559-563 (matt); United States patents number 5,240,855; 5,322,783 and 5,324,646; Klein, I tied you up. (1988) F / anf PrtyW. §1:440-444 (maize^ ef (1990) S / otedw / ogy 8:633-839 (maize); HooyKaas-Van Stegteren. et a / „ (1984) Natore (London) 311:763-764; Patent de tes United States number 5,736,369 (cereals); Sytebter, et al, (1987) Proc. Nati, Adad. Set USA 84:53455349 (liliaceae); De Wet, et te,, (1965) in The Experimatete Afen^g / atten te Ovafe Tíssw, ad. Dhapman, Í5 s< ai. {Longman, New YórR). p. 197-209 (pollen); Kaeppter, te a / ,, (1990) P / ate CW 9:416« 418 and Kaeppier, ata / ., (1992) Theor. Apph Ger^t 84::560-566 (translormacton-mediated pair whiskers); D'Halluín, tete,, (1992) Plañí Ce« 4:1495-1505 (effect for): Lí, etaL, (1993) Píant Cali Repdris 12:250*265 and Christou and Ford, (1995) Amáfe te'Steány 75 :407*413 (arraz)í Osjoda, ef al., (1993) Wafute StotecbrMtógy 14:745-760 (corn by Agrsdacfenom fumef&sí&ns); all of which are incorporated herein 29 by reference. In specific disclosures, the sequences of the embodiments can be provided to a plant using various methods of transient transformation. Such transient transformation methods include, but are not limited to, the introduction of the ÍRDIG35583 polynucleotide or variants and fragments thereof directly into the plant or the introduction of the polypeptide transcript. IRDIG35563 on the floor. Such methods include, for example, microinjection or particle bombardment. See, for example, Ctesway, et al, (1936) ^o / Gen. Genet 202:179-185; Nomura, at a / ,, (1986) Plaet Sci. 44:53-53; Hspler, «f a¿, (1994) Ptpc. NM Acad, Ser 91:2176-2180 and Hush. cía / ·, (1994) Tés Journal of Ced Setenes 107:775-784, all of which are incorporated herein by reference. Alternatively, the IRDIG35S63 poinuepheotide can be transiently transformed in the plant using techniques in the viral vector system and precipitation of the poSnuGlectide in a manner that prevents post-release of the DNA. In this way, transcription can occur from the DNA bound to the particles, but the frequency with which it is released to integrate into the dwarf is greatly reduced. Such methods include the use of polyethylene (PEI) coated particles; Sigma η,° P3143). Methods for the directed insertion of a polyfracteotide to a specific location in the plant stem include Insertion of the polynucleotide into a desired germinal location and is accomplished using a site-specific nrambing system. See, for example, WÜ 1999 / 25821, W01999 / 25854, WO 1999 / 25845, WG1999 / 25855 and WO 1999 / 25853, all of which are incorporated herein by reference. Briefly, the polynuoleotide of these embodiments may be contained in a transfer cassette flanked by two non-identical recombination sites. The transfer cassette is introduced into a plant that has incorrectly incorporated into its genome a target site that is flanked by two non-identical reassortment sites that correspond to the sylphs of the transfer cassette. A suitable racombinase is provided and the transfer cassette is integrated into the target site. In this way, the polynucleotide of interest is integrated into a specific chromosomal position in the plant genome. LdS plant transformation vectors may be comprised of one or more DNA vectors necessary to achieve plant transformation including efe plant transformation vectors that are comprised of more than one contiguous DNA segment. These vectors are often referred to as binary vectors. Binary vectors, as well as vectors with helper piasmids, are most often used for Agrabasteríóm-mediated transformation, where the size and complexity of the DNA segments required to achieve efficient transformation is quite large and it is advantageous to separate the functions into separate DNA molecules. Binary vectors typically contain a plasmid vector containing the ds-acting sequences necessary for T-DNA transfer (such as the left border and right border), a selectable marker that is designed to be capable of expression in a plant cell and a gene of interest (a gene designed by genetic engineering to be capable of expression in a plant cell for which the generation of transgenic plants is desired). Also present in this plasmieto vector are the sequences necessary for bacterial replication. The action sequences in cie are arranged in such a way as to allow for efficient transfer into plant cells and expression in the plant cells themselves. For example, the selectable marker gene and the pesticidal gene are located between the left and right borders. Often a second plasmid vector contains ios. trans-acting factors mediating Agtobactefwm T-DNA transfer to vegetase cells. This plasmid often contains virutenoia functions (vir genes) that allow infection of plant cells by Agrabactenum and transfer of DNA by excision at boundary sequences and vir-mediated DNA transfer (Heliens and Muliineaux, (2000). ) in P / artf Science 5,446-451), Various types of Agroocfenum strains (eg, LBA4404, GV3101, EHATQ1, EHA105, etc.) can be used for the transformation of plants. The second plasma vector is not necessary to transform plants by other methods, such as microprojection. microinjection, electropofadon, polyethylengiicoi, etc. In general, plant transformation methods involve transferring heterologous DNA into target plant cells (eg, immature or mature embryos, suspension cultures, undifferentiated cells, protoplasts, ate.), followed by application of a maximum threshold level of da selection 3§ suitable (depending on the selection marker gene) to recover transformed plant cells from a pool of untransformed cell mass. After the integration of the exogenous hepherological DNA into the plant cells, an appropriate maximum selection threshold level is applied in the medium to eliminate the non-transformed cells and to separate and proliferate the putatively transformed cells that survive this selection treatment: by transferring a medium fresh. Through continuous passage and exposure to adequate selection, Céiutes that are transformed with the ptasmide vector can be identified and proliferate. Mojecular and biochemical methods can then be used to confirm the presence of the integrated heterogenic gene of interest in the genome of the transgemc plant. . Typically, explants are transferred to a fresh supply of the same medium and routinely cultured. Subsequently, transformed cells differentiate into shoots after placing supplemented regeneration medium to a maximum threshold level of . agent of: selection. Then, the shoots are transferred to a selective rooting medium to recover rooted shoots 18 or seedlings. The transgone seedling then grows into a mature plant and produces fertile seeds (for example, Híet, et &L (1994) The Plant Journal 8:271-282; Ishidá, et &1„ (1996) Nature Biotechnology 14;74S-76O), Typically, explants are transferred to a fresh supply of the same medium and cultured routinely. A general description of fecnfeas and methods for generating transganic plants can be found in Á^ss and Park, (1994) Cnfcaf Revfews ín Plant Scíeoc® 13:219-239 and 15 Bommineni and dpuhan (1997) Mayola 42:107-129, Since the transformed material contains many cells, there are presumed transformed cells as well as non-transformed cells in any part of the target callus or subjected tissue or group of cells. The ability to remove non-transformed cells and to allow proliferation of transformed cells results in cultures of transformed plants. The ability to remove non-transformed cells is often a limitation to the rapid recovery of transformed plant cells and the successful generation of cells. Transgenic plants. From these cells that have been transformed, plants can be obtained according to conventional methods. See, for example, McCormick, et al, (1986) Ptant Calí Reporta 5:81-84. These plants can be cultivated and subsequently pollinate with the same transformed strain or with different strains and the resulting hybrid can be identified that expresses constitutively or inducibly the 2S desired phenotypic trait. Two or more generations may be grown to ensure that the expression of the desired phenotypic trait is conserved and stably inherited, and then the seeds are collected to ensure that the desired phenotypic trait has been expressed. The nucleotide sequences of these embodiments can be provided to the plant by 30-day contact with a virus or video nucleic acids. Typically, such methods involve incorporating a nucleotide construct of interest into a viral DNA or RNA molecule. . It is recognized that the disclosed embodiments include IRDIG35563 polypeptides that are initially synthesized as part of a viral polyprotein, which can later be processed by vivo or vitro proteolysis to produce the final desired IRDIG35563 polypeptide product. Such a viral polyprotein is also recognized, comprising at least a portion of the amino acid sequence of an IRDIG35563 of embodiments. may have the desired pesticidal activity. Such viral proteins and the nuclear sequences encoding them are encompassed by embodiments. Methods of providing plants with nucleotide constructs and producing such encoded proteins in plants, involving DNA or video RNA molecules, are known in the art. See, for example. US Patent Numbers 5,889,191; 5,889,190: 5,866,785; 5,589,367 and 5,318,931, incorporated herein by reference. Methods for the transformation of cíórapíafecs can be found:, for example, in Svab, 5 ef M, (1990) Pk>c. NáíL Ac&d. Said. USA 87:8526-8538, Svan and Mátiga.. (1993) Proa, Nati Acád Scí, UGA 90:913-917; Svab and MaUga, (1 §93} EMSÜ J. 12:601-606. The method is based on the supply with a gun of DNA particles containing a selection marker and the targeting of the AON to the plastid ganome by means of recombination of In addition, pistid transformation can be achieved by transactivation of a plastid-borne silent transgene by tissue-preferential expression of a plastid-targeted nonolearly encoded RNA polymer©. )rw. MM-ACM Sai USA 91:7301-7305, The embodiments further refer to plant propagation material from a transformed plant of the embodiments including, but not limited to, seeds, tubers, corms, bulbs, leaves, and root and shoot cuttings. The embodiments can be used to transform any plant species, including, without limitation, monocots and dicots. Examples of plants of interest include, but not imitent, maize (Zea mays), Firassfca sp, (eg, β,. napas, B. rapa, B. jtmsaa), particularly those Bravatea species useful as sources seed oil, alfalfa (Afed / cago SédVé), rice (Oryza sáfete), rye (Sécate caréate). sorghum (Sorghum bicGfcp Stargbítm vulgar millet (for example, pearl millet ( / fenmstem gíaucum), proso millet (Pantoa? mtocewh), foxtail millet (Setens íte / áa), finger millet (Efeuaoe caracana)). sunflower ( Hatorf / ws anouus), safflower (Carthamus feíct'tes), wheat (Frir / cum a&sfivum), soybean (Gr / cina rrw^ tobacco (Nicatiami tabacum), potato (Mcoííana tabacam}, peanuts (Araehis hyp^aaa), cotton (Gossypru?nóarbád^^ Gosáyaum rtírafeúm), sweet potato (Ipomoea Patatos), casáva (MsmW' escótente), coffee (Cofeea spp,), coconut (Cocos mtófera), pineapple (Ananas comosus), citrus trees (Cifras spp,), cocoa (Theobroma cacao), tea (Csme.Ww&ws), banana (M« / sa spp,), avocado (Persians dfneréane), fig (Reos caslca), guava mango (Marígíf&a tefecs), olive (Otea ©«ropeeaj. papaya (Cañé® papaya), cashew (Awwflun·! occfteptáte), macadamia (>Macartete írttegnfof / a), almond (Prunus smygdateX remotaeha azucarera (Prnab^ amy^daliis), sugar cane (Sacteram spp.), oats, barley, ornamental and coniferous plants, Vegetables include tontate (Lyeepéreicorí eá^^ lettuce (for example, Lacróca sáfete), green beans (Phasécfe voigaré), broad beans (Rhaseofos toáoste), peas (Latbyms spp,) and members of the genus Cucumte such as cucumber (C, satmus), centaupe (C. canta / upensís j, and melon (C. ma / o). Omamsntafes plants include azalea (Rhodódenrfren spp.), hydrangea (Wacropéjrfte 35 rtydrangsa), hibiscus (H / bfecus rósasaoensísj, roses (Rosa spp.), tulips (Tú#a spp,), daffodils (ÍW&fssw ópp,), petunias (P^^ hyó^é), carnations (Díánt / ms éárye^by#úaK..p^bSétSé (EsrphortVe puichemma ) and chrysanthemum Conifers that can be used in the practice of the embodiments include, for example: pines, such as iaeda pine 3δ ponderese (Ríosponderosa), p>not ΙοφοροΙο. (Pinas conforta) and Monterey pine {Ww radfefaj; Dougias fir (Pseuduísuga wnz / esvfK^ from Canada (Tenga camsdens^^ white (Rtea glauca); sequoia (Sequoia aeinpervrrens); true firs, such as white abato (Abíes amabilis} and balsam fir (Abte ba / sawa) and cedars such as western red cedar (Thaja blioats) and Aláska yellow cedar (Chamáecypam oooíéatente). peanut, sorghum, wheat, millet, tobacco, etc.), lates such as corn and soybean plants. Grasses include, without limitation: annual pea (Pos aonuaj; annual ryegrass (Lnlium muOorum); Canada bluegrass (Poa csn^essa); red fescue (Festuca rubra}; tenuous bentgrass (Agrostís temas); stolonlfera agrestid (Agroatís pafástds ): desert pyrograss (Agrapyron desertorum), crested fescue (Agropyron cnsfaium), hard fescue (Kentucky grass fescue (Roa prafensis); grazed orchard (Dadyirs gtewata); perennial ryegrass (Lo / rum persone); red fescue (Festuca rubra); white agréshde (Agrosfis atea): common pea (Pos tdvisi^); lamb bread (Festuca ew?a); inert bromine (ñ / omus wró); tall feslucs (Festuca arundmapea): timothy of the swamps (Phfeum pratense); canine bentgrass (Agrosíis canina); Alkaline Tears Grass (Pucróei / ted^ Plain Grass (Agropyron smiO); Common Grass (Cynodoh spp,}*: St. Augustine Grass (Stenotepfoiím s^ Zoysia Grass (Zaysia app.); Babia Grass (Fáspatom netafem); Carpet Grass (Axonopus centipede grass (Bremaóhfós ^fouraates); Kikuyu grass (Paom'Sétum dámtesfounfy white chaplea (Paspalum vagtoafum); blue grass (Swfofoua giw / te): buffalo grass (&ucMa®'dac^fo^ banderea grass (ñoj<e / or "a curtipenriuia). Plants of interest include grain plants that provide seeds of interest, oilseed plants, and leguminous plants. Seeds of interest include cereal seeds such as mafe, wheat, barley, rice, sorghum, rye, millet, etc. Oil plants include cotton, soybean, safflower, sunflower, «rasste, corn, alfalfa, palm, coconut, flax, castor, olive, etc. Leguminous plants include beans and peas. Beans include guar, garrotín, fenugreek, sojai beans, china bean, paliar bean, babas, lentils, chickpeas, etc. Evaluation of the fratformaqídn of the introduction of the heterologous hexagon AON in plant cells, the transformation or integration of the hsterologP gene in the plant ganome is confirmed by various methods, such as nucleic acid analysis. proteins and metabolites associated with the integrated gene. PCR analysis is a rapid method to screen transformed cells, tissue, or shoots for the presence of the incorporated gene at an early stage before transplanting them into soil (Sambrook and Russell (2001) Molecular Cloning; A Laboratory Manual. Coid Spng Harbor Laboratory Press , Cold Spring Harbor, NY). PCR is carried out using oligonucleotide primers specific for the gene of interest or the origin of the AgrobacteAurn vector, etc. Plant transformation can be confirmed by Southern blot analysis of genomic AON (Sambreok and Russei!, (2001) supra). In general, total AON is extracted from the transformant, digested with the appropriate restriction enzymes, fractionated in a gal ds garose, and transferred to a mtroketelose-nylon membrane. The membrane or transient is subsequently probed with, for example, a 32P radiolabeled target DNA fragment to confirm the integration of the gene introduced into the plant genome according to conventional techniques (Sambrock and Russef!, (2001) amen arme quoted above). In Northern blot analysis, siRNA is isolated from specific tissues of the transformant, fractionated into a ge! of formaldehyde-agarose and transferred onto a rtaiton filter according to standard procedures which can be found in Sambrook and Russell. (2001} previously reviewed); The expression of RNA encoded by the pesticidal gene is tested after hybridizing the filter with a radioactive probe obtained from a pesticidal gene, by methods 1Q known in the art (Sambrock and Russell, (2001) discussed above). Western blots, biochemical assays and the like can be carried out on the transgenic plants to confirm the presence of the protein encoded by the pesticidal gene by conventional procedures (Sámbrook and Russell, (2001) supra) using antibodies that bind to one or more presser epitopes on the IREJIG35S6-8 polypeptide. Bioassays in insects of Árabidíwsis transcenioa. Transgenic Arabidops / s lines expressing modified IRDIG3SS63 proteins can be used to demonstrate activity against insect species in artificial diet overlap assays. Proteins extracted from transgenic and non-transgenic Arab / Dopsis lines can be quantified by appropriate methods® and sample volumes adjusted to normalize the protein concentration. Bioassays are then carried out on diet, artificial as described below. Non-transgenic Arabidopsis and / or. Swab and water should be included in tests as background check treatments. Transoceanic corn shipments. The bi-activity of IRDIG35563 toxins and vanants produced in plant cells can also be demonstrated by conventional bioassay methods (see, for example, Huang et al., 2006}, Effectiveness can be tested by feeding various plant tissues or derived tissue chips. from a 1RDIG35S63 toxin-producing plant to diarsa insects in a controlled feeding environment.Alternatively, protein extracts can be prepared from various plant tissues derived from a ÍROIG35563 toxin-producing plant and incorporated the extracted proteins into a bioassay of 1RDIG35563 toxin. It is to be understood that the results of these feeding assays are to be compared with hyoassays carried out in a similar manner using appropriate control tissues from these host plants that do not produce the IRDIG35363 protein or variants, or to other control samples. . Methods to introduce genome editing technology in plants. In some embodiments, the disclosed IRDIG35563 polynucleotide compositions can be introduced into the genome of a plant using editing technologies! genome or SRDIG35563 polynucieophids previously introduced into the genome of a plant can be edited using editing technologies! genome. For example, the disclosed polynucleotides can be introduced into a desired location in the genome of a ptenfa through the use of Dicaiengria cleavage technologies, such as TALEN, megahyctases, zinc finger nucleases, CRiSPR-Cas and the like. For example, these disclosed polynucleotides can be introduced into a desired location in a ganome using a CRiSPRCas system for the purpose of target-specific insertion. The desired location in a plant genome can be any desired target site for insertion, such as a genomic region amenable to plant breeding, or it can be a target site located in a genomic window with an existing trait of interest. Existing traits of interest may be an endogenous trait or a previously introduced trait. In some embodiments. Where the disclosed IRD1G35S63 polynucleotide has previously been introduced into a genome, genome editing technologies can be used to alter or modify the introduced polynucleotide sequence. Site-specific modifications that can be introduced into the disclosed IRDIG35563 polynucleotide compositions include those produced using any method for introducing a site-specific modification including, but not limited to, the use of gene repair oligonucleotides (eg, Publication dé EE. , deletion or substitution of nucleotides within the introduced polynucleotide. Alternatively, double-strand break technologies can be used to add additional nucleotide sequences to the introduced polynucleotide. Additional sequences that can be added include additional expression elements, such as enhancer and promoter sequences. In other ways, gene editing technologies can be used to place additional proteins with insecticidal activity in close proximity to the IRDIG35563 polynacleotide compositions implicated herein within a plant genome to generate molecular pools of proteins with insecticidal activity. An "altered target site", an "altered target sequence". A "modified target site" and a modified target sequence are used interchangeably herein and refer to a target sequence as disclosed herein that comprises less than one alteration when compared to a target sequence. not altered. Said "alterations" include, for example, (i) replacement of at least one nucleotide, (ii) a deletion of at least one nucleotide. (iii) an insertion of at least one nucleotide or (iv) any embedding of (i) - (ííí). Trait accumulation in tfansgenic plants. The transgenic plants may comprise an accumulation of one or more insecticidal polynucleotides disclosed herein with one or more additional polynucleotides that result in the production or deletion of multiple polypeptide sequences. Transgenic plants comprising pools of polynucleotide sequences can be obtained by traditional hybridization methods or by hybridization methods. 3S genetic engineering or by both. These methods include, but are not limited to, hybridization of individual lines each comprising a polynucleotide of interest, transformation of a transgenic plant that. comprises a gene disclosed herein with a subsequent gene and cotransfrmation of genes in a single Tai Plant cell as used herein, the term ''accumulated'' includes having multiple traits present in the same plant (i.e., they are incorporate: both traits in the nuclear gensma, one trait is incorporated in the nuclear genome and one trait is incorporated into the genome of a ptestid or both traits are incorporated into the yenuma of a plastid). In a non-limiting example, the "traits, cumulatives*" comprise a molecular cumulative where the 5 traits are physically adjacent to each other. A trait, as used herein, refers to the phenotype obtained from a particular sequence or groups of sequences. Gene conversion can be carried out using individual transformation vectors comprising multiple genes or gene-carriers. per separated in multiple vectors. If the sequences are accumulated by genetic transformation of plants, the δ polynucleotide sequences of interest can be combined at any time and in any order. Traits can be introduced simultaneously into a cotransformation protocol with the provided polynucleotides of interest using any combination of transformation cassettes. For example, in case two sequences are to be introduced, the two sequences may be contained in separate transformation cassettes (trans) or be contained in the same transformation cassette (cis). The expression of the sequences can be driven by the same promoter or by different promoters. In certain cases, it may be desirable to introduce a transformation cassette that suppresses expression of the polynucleotide of interest. This can be combined with any combination of other suppression cassettes or overexpression cassettes to generate the desired combination of plant traits. It is further recognized that polynucleotide sequences can be assembled at a desired genomic location using a site-specific recombination system. See, for example, WO 1999 / 25821, WO 1999 / 25354, WO 1999 / 25840, WO 1999 / 25855, and WO 1999 / 25853, all of which are incorporated herein by reference. In some embodiments, pota encoding the pteipéptide ίΚΟΙΟ35583 disclosed herein, alone or in combination with one or more additional insect resistance traits may be combined with one or more additional internal traits (eg, herbicide resistance, fungal resistance, virus resistance, stress tolerance, disease resistance, and the like) or external traits (eg, increased yield, modified starches, improved oil profile, balanced amino acids, increased amount of lysine or methaine, increased digestibility, improved fiber quality , drought resistance and the like). Therefore, the polynucleotide embodiments can be used to provide a complete agronomic package of improved crop quality with the ability to be flexible and cost effective for any number of agronomic pests. Useful transgenes for accumulation include, but are not limited to' t. Transgans that confer resistance to Insects or disease and that encode; (A) Plant disease resistance genes, plant defenses are normally activated by a specific interaction between the product of a disease resistance gene (R) in the plant and the product of an avirucence gene (Avr). ) corresponding in he pathogen. A variety of plants can be transformed with a cloned resistance gene to genetically engineer plants that are resistant to specific pathogenic strains. See, for example, Dones, eta / ., (1094) Scfence206:789 (cloning of the tomato CA9 gene for resistance to Cladosporfum fhiviim); Martin, et al, (19S3) Scfa^^ (Tomato Pto gene for resistance to tomato Ps&udomonas sydpgse pv. encoding a chymase protein); Mindrirtos, éí sí, (1 094) Cé / i 78:1089 (AfabÍdopsis RSP2 gene 5 for resistance to Peeodomorw symgae}, McDoweity Woffenden, (2003) Trefes Bi&techno!,. 21(4):178-83 and Tdyoda, et al, (2092) Res. 11(6):567-82. A disease resistant plant is one that is more resistant to a pathogen compared to the wild type plant. (B) Genes encoding a BaeMiis thuringiensis protein, a derivative thereof, or a synthetic polypeptide modeled therefrom. See, for example, Geiser, et al., (1986) Gene 481109, who disclose the dohacidh and nucleotide sequence of a BL deta-endotoxin gene. In addition, DNA sequences encoding deta-endotoxin genes can be purchased. in you Amanennos Type Culture Collection (80^^ Md ), for example, with ATCC reference numbers^40098,67136, 31995 and 31998, Other non-limiting examples of B&cittus fJwringiensis transgenes being genetically engineered are provided in the following patents and patent applications and are incorporated herein by reference for this purpose: United States Patent Numbers 5,188,960; 5,689,052; 5,880,275; 5,988,177; 6,023,013, 6,060,594, 6,063,597, 6,077,824, 6,620,988, 6,642,030. 6,713,259, 6,893,625, 7,105,332; 7,179,965, 7,208,474; 7,227,056, 7,288,843, 7,323,556, 7,329,736. 7,449,552,7,468,278, 7,510,878. 7,521,235, ? 544,882, 7,695,304, 7,696,412,7,629.504. 7,705,216, 7,772,465, 7,790,846, 7,858,849 and WQ 1991 / 14778; WO 1999 / 31248; WO 2001 / 12731; W01999 / 24581 and WO 1997. / 40162. Genes encoding ptegu¡c>das proteins can also be included, but not limited to: insecticidal proteins from Pscutomonas sp, such as PSEEN3174 (Monaíysin: (2011) PLoS Pathcgens 7:1-13); from Pseudórnonas protect» strain CHAO and Pf-5 (previously fluorescens) (Pechy-Tarr, (2008) Environmental Microbiology 10:2368-2366; NA reference from GenBank. EU4O0157); from Pseudqmonss lew (Liu. et al. (2010) J. Agríe, Food Chém., 58:1234312349) and from Pseudomonas pseudas / ca / rgenes (Zhang, et at, (2009) Aunáis of Microbiotegy 59:45-50 and Li, et al. (2007) Plant Cell Tiss. Organ Culi. 89:159-168); insecticidal proteins of PhoiorhsÉidífs sp, and XenorítaiMus sp. (Hinchíiffe, st al., (2010) The Open ToxÍCology Journal. 3:101-118 and Morgan, et al, (2001) Applied and Envír. Micro. 67:2062-2069); US Patent No. 6,048,838 and US Patent, NA 6,379.946; a PiP-1 polypeptide from US 9,688,730; an AIIP-1A and / or A0P-1B polypeptide from US9,475,847; a PIP-47 polypeptide from te US Publication NA US2016Q186204: an IPD045 polypeptide, an IPQ064 polypeptide, an IPO074 polypeptide. an iPDQ75 polypeptide and an IPD077 polypeptide from PCT Publication Number WO 2016 / 114973; a pteipeptide IPDO80 of the PCT Number of PCT / US17 / 5S5 Í7 series; an IPD078 polypeptide. an IPD084 polypeptide, a 1PD085 pmipeptide, an IPD086 polypeptide. an IPD087 polypeptide, an IPD066 polypeptide and an IPDQ89 polypeptide of Serial Number PCT / USI7 / 54160: the PlP-72 polypeptide of US Patent Publication Number 11820160366891; a PtiP-50 polypeptide and a PtlP-6S polypeptide of US Publication Number US20170168921: an IPDQ98 palipeptide, an FD059 pdipeptide, an IPD108 polypeptide, an IPD1G9 polypeptide from US Serial Number. 62 / 521084; a PtlP-83 polypeptide from US Publication. Number US2O1S0347799: a US Publication PtlP-96 polypeptide. Number U$20170233440; a polypeptide IPD879 of PCT Publication Number WO2017 / 23438: a polypeptide IPQ082 of PCT Publication S Number WO 2017 / 105987. an IPD090 polypeptide of Serial Number PQT / UST7 / 30602, an IPDG93 polypeptide of US Serial Number 62 / 434020; an IPD103 polypeptide of Serial Number PCT / US17 / 39376; an IPD101 polypeptide of US Sen. Number 62 / 438179; a US Serial Number 0121 polypeptide. 82 / 506,514; and iS-erteotexinac but not limited to, the classes Cryl, Cry2, Cry3, Gry4, Cry5, Cry6, Qry7, Cry8. CryO. CrylO, Gryll, Cryl2, Cry13, Gry14, CrylS, 10 Cry18, Cryl7, CrylS, Cry19, Cry2Ú, CryXl, Cry22. Cry23, Dry24sCrySS, CryM Cry27. Gry28, Cry2§, Cry30, Cry31, Cry32, Cry33, 0^34,0^35.0^36, Cry37(Cry3S, Ccy3S, Cry40, Gry41, Gry42, Cry43, Cry44, Cfy45, Cry46, Cry47, G.ry49, CrySO , Cry5t Cry52, Cry53, Cry§4, Cry55.Cry56, Cry57, CrySS, CryS9, Cry6Q> Cry61.Cry62, Gry63< G?y64:Cry65.Cry66, CrySZ, Cry68, Cry89, Cry70, Cry71 and Cry 72 polypeptides give δ-endotoxin and cough cytolytic genes cytl and cyt2 from 8. / ourinp / ens / s Some members of these 15 classes of S. teyfwfenste insecticidal proteins can be found in Crickmore» et al. ^acillus Óluríngteasis tóxiOom (2011), &nlitescí..:Sués®x..au.uto1tome / N^^ can be accessed on the Internet using the prefix Some examples of o-endotoxins also include but are not limited to the Qry1A proteins of US Patent Numbers 5,880,275, 7,858,849 and 8,878,607: a CrylAc mutant from US9,512,187; a DIG-3 or DIG-11 toxin (N-terminal deletion of α-helix 1 and / or α-helix 2 variants of cry proteins such as Cryl A. Cry3A) from US Patent Numbers 8,304,604, 6,304 ,695 and 8,476(226; Cryl8 of US Patent Scheduling Number 10 / 525,318, US Patent Application Publication Number US20160194364 and US Patent Numbers 9,404,121 and 8,772,577, the Cryl B variants of PCT Publication Number WO2816 / 61197 and Serial Number PCT / US17 / 27160: CrytC de fe US Patent, NT 6,033,874- te protein Cryl O deidocumente US2Q170233758; a CrylE protein from PCT Serial Number PCT / US17 / 53178; a Cryl F protein from US Patent Numbers 5,188,960 and 6,213,138; Cry WF chimeras of US Pat. Numbers 7,070,982: 6,962,705 and 6,713,063; a Cryl I protein from PCT Publication Number WQ 201770233759; an Oyl J variant of US Pubhcacton US20170240803: a Cry2 protein tetes 30 odriio the Cry2Ab protein from US Patent ΝΛ 7,064,249 and the Cry2A 127 protein from US 7208474; a Cry3Aqus protein includes but is not limited to an engineered hybrid insecticidal protein (eHIP) created by fusing unique combinations of variable regions and conserved blocs of at least two different Cry proteins (US Patent Application Publication Number 2016 / 0017914); a Cry4 protein; a Cry5 protein; a CryG protein; Cry8 proteins gives fes 65 US Patent Numbers 7,329,736, 7,449,552, 7,803,943,7,476,761, 7,105,332, 7,339,092, 7,373,499,7,482,760 and 9,593,345; A CryO protein lates as members of the Cry9A, CryGB, Cry9C, Cry9D families. CryQE and CrySF including the Cry9 protein from US Patent 9,000,261 and 6,802,933 and US Serial Number, WU 2017 / 132188; a Gry15 protein from Naimov, et al., (2008) Applied and Envíronméntai Mícrobtofogy, 74:7145-7151; a Crv14 protein from US Patent ΝΛ US8,933J99; a Cry22, a Cry34Abi protein from US Pat. Nos. 8,127,160. 8,824,145 and 6,340,593; a. truncated Cry34 protein from US Patent NA US8,816,157: a CryET33 and cryET'34 protein from US Patent Numbers 6,248,535, 6,326,351 6,399,330. 6,949,626, 7,385.107 and 7,504,229; a CryET33 and CryET34 homolog of the US Patent Publication. Number 2006 / 0191034, 2012 / 0278954, and te PCT Publication Number WO 2012 / 139004; a Cry35Ab1 protein from US Patent Numbers 6,083,499, 6,548,291 and 6,340,593; a Cry46 protein from US Pat. NA 9,403,881, a Cry 51 protein, a Cry binary laxin; a TIC901 or related toxin; TIC807 of te Patent Application Publication of US Patent Number 2008 / 0295207: TiC853 US8,513,493: ET29. ET37, TIC809, TIC810. TIC812. UC127, T1C128 of PCT US 2008 / 033867; AI-engineered hemipteran-toxic proteins US Patent Application Publication Number US2O160150795, US Patent AXMI-027, AXMI-036 and AXM1-038, NA 8,236,757; AXMMJ31, AXM1-039, AXMI-040, AXM1049 from US Patent NA 7,923,502; AXMI-018, AXMI-02Q and AXMI-021 of the WO document 2006 / 083691; AXMW1Q- from WO 2005 / 036032: AXMl-003· from WO 2005 / 021585; AXM1-008 of the US Patent Application Publication Number 2000250311: ΑΧΜΙ-0δ6 of the US Patent Application Publication Number 2004 / 0216188; AXMI-007 of te US Patent Application Publication Number 2004 / 0210965; AXMI-009 of te US Patent Application, Number 2004 / 0210964: ΑΧΜΙΌ^ of US Patent Application Publication Number: 2004 / 0197917: AXMI-004 of ia US Patent Application Publication Number 2004 / 0197916; AXMI-028 and AXMI-029 dsl documented WO 2006 / 119457; AXMI-007, AXMI-0O8, AXM!-0080rf2, AXMI-009, ΑΧΜΙΌ14 and AXMP004 of WO 2004 / 074452. AXMI-150 from ia US Patent NA 8,084,416; AXM1-205 of US Patent Application Publication Number 201170023184; AXMI011, AXMPQ'12, AXMW13, AXMPQ15, AXMI-01 θ, ΑΧΜΙ4344, AXMI-037, AXMI-043, AXMI-033, AXM1-Q34, AXMí-022, ΑΧΜΙ-023, AXMI-041, AXMI-063 and AXMl-064 of te Patent Application Publication of USA Number 2011 / 0263488; AXMIQ46, AXMI048, AXMI05O, AXMIQ51, AXMI052, AXMI053, AXMI054, AXMI055, AXMI056, AXMI057, AXMI0SB, AXMI059, AXMIO60, AXMI061, AXMI067, AXMI069, AXMI071, AXMI072; AXMI074. AXMIQ75,..AXMI087. AXMIO88, AXMI093, AXMI070, AXMI08Q, AXMJO81, AXMI0S2, AXMI09t AXMI092. ΑΧΜ|Ο96, / &Μ1897, AXMIO98, AXMTO AXMHOO, AXMU01, MMI102, AXMIW3, AXMim / WI107, AXMI108. AXMI109, AXMI110. AXMiHI, AXMI112, AXMI114, ΑΧΜΙ1Ί6, AXMI117, AXM1118, AXMI119, AXMI120, AXMI121, ΑΧΜΠ22, AXMH23, AXMI124. AXMU25, AXMI126, MMI127, AXMl^ AXMI161. AXMIW, AXMI183, AXMI132, AXMI137, AXMI138 of US Patent US8461421 and US8,461,422; AXMi-RI and related proteins from te US Patent Application Publication Number 2010 / 0197592; AXMI221Z, AXMI222Z, AXMI223Z, AXM!224z and AXMI225Z from WO 2011 / 103248; AXMI218, AXMI219, AXMt.220, AXMI226. AXMI227, ΑΧΜΙ228, AXW29, AXMÍ230 and ΑΧΜΙ23Ί of WO 2011 / 103247; ÁXMM15. AXMI-113, AXMN 005, AXMI-163 and AXMI-184 of US Patent No. c8,334,431; AXMI-001, AXMI-002, AXMI-030, AXMI4W and AXMI-045 gives US Patent Application Publication Number 2010 / 0298211; AXMI-066 and AXMW76 of US Patent Scientific Publication Number 2009 / 0144852;: AXMH2& AXMI139, AXMI13T, AXMI133, AXMI140, AXWM1, AXMH42, AXMH43, AXMlt44. AXMI14S, AXMI148, AXMim AXMH5Z AXMI153, AXMH54, ΑΧΜΙΤ55. ΑΧΜΙ^ AXMÍ155, ΑΧΜΠ68, AXMlW, AXMI168, AXMI1M AX^UM AXMI171, AXMI17& AXMI173, AXMI174, 5 AXMIÍ75, AXMH76, AXMÍ177, AXMI178, AXM|1 79, AXMI180, AXW81, AXMÍM1H, AXMÍM1H AXMI187, AXMIT88, ΑΧΜΠ89 of US Patent No. 8,318,900; AXMI079, AXMIOUS, AXMI081, AXMI082. AXMI091, AXMI092. AXMIOW, AXMIQS7, AXMI098, AXMI099, AXMI10D, AXMiTOl, AXMH02,. AXMI1Ó3, AXMI W4, AXMIW7, AXMI108, AXMI169, ÁXMIT10, ΛΧΜΙ116. AXMI117, AXMI118, AXMI11& ΑΧΜΙ120, ÁXMI121, AXMI122, AXW123, AXMI124, AXMI1257, TO AXM11268, AXMI127, AXMI129, ÁXMÍ164, AXMi'151, AXMÍ161, AXMÍ183. AXMI132, AXMU38, AXMI13? US Patent US8461421: US Patent AXMI192. USS^StAI S; AXMI281 of ia US Patent Application Publication Number- US20160177332; US Patent AXMI422, US Pat. a CrylAc, Cry2Aa and CrylGa toxin protein from 13 Sadi / us tOenngfensis strain VSTS 2528 of US Patent Solo Publication Number. 2011 / 0064710. The proteins Cry MPO ΜΡΏ51, MP088, MP06& MP07Q. MP091S. MP109S, MPT14, MP121, MP134S, MP183S, MP185S, MP186S, MPT95S, MP197S, MP208S, MP209S, MP212S, MP214S, MP217S, MP222S, MP234S, MP235S, MP237S, MP242S, MP243, MP248, MP249S, MP235S, MP251M MP287S, MP238S, MP295S, MP298S, MR287S, MP300S, MP304S, 20 MP306S, MP3WS. MP312S, AIP314S, MP319S, MP325S, MP328S, MP327S, MP328S, MP334S, MP337S, MP342S, MP340S, MP356S, MP359S, MP360S, MP437S, MP451S. MP452S, MP466S, MP468S, MP476S, MP482S, MP522S, MP520S, MPS48S, MP5S2S, MPÓ82S, MPS64S, MP566S, MP587S, MP569S, W573S, MP574S!;MP575S!MF581S, MP590, MP594S, MPS95, MPS05, MPS96S7, MP6 MP602S, MP604S, MP636S, MP629S, MP630S, MP63TS, MP632S, MP633S, MP634S, MP635S, MP830S, MP640S, MP644S, MPS4SS, MP651S, MP652S, MP653S, MP651S, MPS66S, MP672S, MPS96S, MP704S, MP724S, MP720S, MP73SS, MP755S, MP773S, MP799S, MPSQ0S, MP801S, MP8Q2S, MP8Ú3S, MP805S, MP809S, MP8T5S, MP828S, MP831& MP844S. MP852, MP8658, MP87SS, MP887S. MP891S, MP896S. MP898É MP935S. MP988, MP980, MP903, MP907, MP1049, MPW. MP1087, MP1O80. MP1081, MP1200. MP1206, MP1233, and MP1311 of the US Serial Number 62 / 607372. The insecticidal activity of the Ory proteins can be found for example in Frannkenhuyzen, (2000) J, invert. Path. 101:1-16), Ei use of Cry proteins as traits of transgenic plants and plants transgenic for Cry including but not limited to plants expressing CrylAo, CrylAc+Cry2Ab< CrytAb, Cry1A.TÜ5tCrylF, Cry1Fa2, CrylF+CrylAc, Cry2Ab, Cry3A, mCrySA, Cry38bi, Cry34Ab1, Cry35AbÍ, Víp3A, mCry3A, GryÓc and CSI-Sí have received regulatory approval (see, Sanahuja, (2011) Piant Blotech doumai 9:283-300 and CERA. (2010) GM Crop Database Genter for Environmental Risk Assessment (CERA), ILQI Research Foundation, Washington D.C. at Gera-gmc.org.'index,pbp?action~gm.qrop database where it can be accessed over the Internet using the prefix *www”). More than one pesticidal protein may also be expressed in plants such as Vip3Ab and CrylFa (US2012'0317682); CrylBE and Cry1F ( US201270311746 ); GrylCA and Gryl AB (US2&12 / Q311745); Cryl F and CryGa (document US2012 / 031768i x CrylOA and QrylSE (document US201^ and CfytFa:(dgqumento US2012 / 033158$); CrylAB and CrylBE (US2Q12 / 0324S06); CrylFa and Cry2Aa and Cryti and CrylE (document US2Q12 / 0324605); Cry34Ab / 35Ab and Cry6Aa (US20130187269); Cry34Ab / VCry35Ab and Cry3Aa ( US20130167268 ); CryIDa and GrylCa ( US 9709982 ); Cry3Aa and Cty6Aa (US 9798963): and CryM and CrylÁb or VjpSAa (US9,045,766). Pesticidal proteins also include insecticidal üpases. By killing lipid hydroases from US Patent No. 7,491,869 and cholesterol oxidases, such as from S&^pfomyces (Purea!; et al (1993) TO Biochem Biophys Res Uomnwn 15:14OB-1413), Pesticide proteins also include toxins VIP (Vegetative Insecticidal Proteins) of US Patent Numbers 5,877,012,6,167,279, 6,137,033, 7,244,820. 7,615,686 and 8,237,020 and the like. Other VIP proteins can be found at lifescí,sussex.ac,ιík / 'home / NeiL·Qrici>;more / Bt'vip.htm! ai which can be accessed on the Internet using the prefix www*. Pesticide proteins also include Cyt proteins including variants of Cyt! A 15 of the PCT document with serial number PCWS2017 / 000510; pesticidal proteins also include toxin complex (TC) proteins, obtainable from organisms such as Xenorhabdus, Photorbabdus, and Paenibacidtis (see US Patent Nos. 7,491,698 and 8,084,418). Some TC proteins have individual insecticidal activity and other TC proteins potentiate the activity of individual toxins produced by the same given organism. The toxicity of an individual TC protein (from Photorhabdus. X&norhabdus or Paenibacillitis, for example) can be enhanced by one or more TC protein enhancers derived from a source organism of a different genus. There are three main types of TC proteins. As cited herein, the ctese A proteins (Protein A) are individual toxins. Class B proteins (Protein B) and class C proteins (Protein C) potentiate the toxicity of class A proteins. Examples of class A proteins are TebA. TcdÁ, XptAI and XpiA2. Examples of class B proteins are TcaG, TcdS, XpiBIXb and XptCIWí. Examples of class C proteins are TccC, XptGIXb and XptBIWi. Pesticide proteins also include proteins from the venom of spiders, snakes, and sscorpions. Examples of peptides from! venom from spider mites include, but are not limited to, icotoxin peptides and mutants thereof (US Patent No. 8,334,366), (C) A polynudeot that encodes an insect-specific hormone or ferum, such as an eedMterctose and juvenile hormone, a variant thereof, a mimetic based thereon, or an antagonist or agonist thereof. See, for example, the disclosure by Hammoek, ef aL, (1990) blattira 344:458, of baculovirus expression of cloned juvenile hormone esterase, a juvenile hormone inactivator. (D) A nucleotide polyptide encoding an insect-specific peptide that, upon expression, alters the phystotagy of the affected pest. For example, see these disclosures by Regen, (1994) J. Bio!. Ch&tn. 269:9 (expression cloning yjekieUNA ceding fer insect diuretic hormone receptor); Pratt. ata / ., (i989} Bic^bam. BibphySi P&a. Cbmm. 183:1243 (án allostetió is Idént^ed in punfata); Ctiattopadhyay. eíál, (2004) GnWc® / Refews fe Mfcrc>btofc^:3{X^ (2004) J WIW 67(2):300-3 i 0: Cartini and GrossWe-Sa, (2002) Toxican 40(11):1515-1630: Ussuf, et al, (2001) Curr Sal. 80(7):847-853 and Vasconcelos y Olíveles, (2004) Fox / con 44(4):365-403. Refer also to US Patent No. 5,266,317 to Tomalski, etfe which discloses genes encoding insect-specific toxins. (E) A polynucleotide that encoded an enzyme responsible for a hyperacum Litation of a menoterpene, a sesquiterpem. an asteroid, tudroxamic acid, a phenylpropanoid derivative or another non-protein molecule with insecticidal activity. d-i A protein that encodes an enzyme involved in the modification, including post-fraduction modification, of a biologically active molecule: for example, a glycoprotein enzyme, a pmtebite enzyme, a lipoprotein enzyme, an olease, a cyclase, a transaminase, an esterase, a hydrolase, a fesphatase, a dnase, a phosphoritese, a polywase, an elastase, a chitinase and a glucanase, whether natural or synthetic. See PCT Application WO 1993 / 02197 in the name of Scott et al, which discloses the sequence wclestidica fe^ Molecules of DNAs containing chitinase coding sequences can be obtained, for example, from ATCC® under reference numbers 39637 and 67152. See also, Kramer, et al. (1 §93) / nsect &ochafn. Mofee, Βκ& 23:^1, who teach the nucleotide sequence of an nDNA encoding tobacco hookworm chitinase and KawaSecK et^.. (1993) P / aéf Mofee. 8fe 21:673, who provide the nucleotide sequence of the parsley poiiubiquitin ubi4-2 gene and US Pat. Nos. 6,563,020; 7,145^0 and 7,087.810, (G) A polynucleotide encoding a molecule that stimulates signal transduction. For example, see the disclosure by Botella, et fe (1994) Plañí Motee. Biol 24:757, from nucleotide sequences of fecalm^^ cDNA donors and Gness, et ák. (1994) Plañí Phystel 104:1467, who provide the nucleotide sequence of a maize caimodulin cDNA clone. (H) A uccleotid polypeptide encoding a hydrophobic momentum peptide. See PCT Application W0 1995 / 16776 and US Patent No. 5,580,852 (disclosure of tachyplesin peptide derivatives that inhibit fungal plant pathogens) and PCT Application WC 1995 / 15855 and US Patent No. 5,607,914 (shows peptides : antimicrObic drugs that confer resistance to the disease). (I) A pofinnucleotide encoding a membrane permease, a channel blocker. For example, see disclosure by Jaynes, alai. U993i PlañíSel 89:43. give heterologous expression of a lytic peptide ó® CBrcopine-beta analogue to render transgenic tobacco plants resistant to Ps&ue'a^onas ^anac&anim. (3) A gene encoding an invasive viral protein or a complex toxin derived therefrom. For example, the accumulation of viral envelope proteins in transformed plant cells confers resistance to viral infections and / or the development of diseases caused by the virus from which the envelope protein gene is derived, as well as by related viruses. See, Beachy, et al, (1990) Ann. Rev. Phytap&thnl. 28:451. Coat protein-mediated resistance has been conferred on transformed plants against alfalfa mosaic virus, cucumber mosaic virus, tobacco streak virus, potato tea virus X, potato tea virus ¥ , the tobacco etch virus, the tobacco rattle virus and the tobacco mosaic virus. H § (K) A gene encoding an insect-specific antibody or an immunotoxin derived therefrom. Therefore, an antibody directed at a critical metabolic function in the insect's gut inactivates an affected enzyme, killing the insect. See Tayfer, ata / ,, Abstract n,e497< SEVENTH INTL SYMPOSIUM ON MOLECULAR PLAHT-MICRQ8E INXERACTIONS (Edinburgh, Scotland. 199 +} (enzymatic inactivation in transganibus tobacco by production of 10-chain antibody fragments). (L) A gene encoding a virus-specific antiderp. See, for example, Tavíádoraki, etaL, (1993) 366'469, who show that transgenic tapirs expressing recombinant antibody genes are protected from virus attack. (M) A pninucleotide encoding a developmental arrest protein produced in nature by a pathogen or parasite. Therefore, the tonic ando-alpha-'β4 -D-poiigalacturonases facilitate fungal colonization and release of plant nutrients by solubilizing homo-alpha-1,4-D-galacturonase from the plant cell wall. See, Lamb, et al, (1992) Bía / Teahnoíagy 10:1436. The detection and characterization of a gene encoding a bean endopolygalacturQnase inhibitor protein is described by Tóubarí, ef ai, (1992) Plañí J. 2:367. (N) A polynucleotide encoding a growth arrest protein produced in nature by a plant. For example. Logemann, yes? a / ,, (1992) Biü / 7ecM^'ogy 16:365, have shown that transgenic plants expressing the barley ribosome-inactivating gene have increased resistance to fungal disease. (O) Genes involved in the acquired systemic resistance response (SAR) and / or the genes involved in pathogenesis, Bfiggs, (1995) Ctmní BMogy 5(2), Pieterse and Van Loen. (2004) Cum Qpih. P / ani Βίΰ. 7(4):466-64 and Somssich, (2603) Caí / ' 113(7):815-6. (P) Antifungal genes {Qornelissen and Melchers, (1993) Pl PhysKd. 101:709-712 and Parijs, stat, (1991) P / ánta 183:258-264 and Bushneli, et al, (1998) Cae J. of Plañí Paíh 20(2):137-149. See also US Patent Applications Serial No. 09 / 950,933; 11 / 619,645; 11 / 657,710; 11 / 748,994; )1 / 774,121 and U.S. Patent Number 6,891,085 and 7,306,946. LysM receptor-like kinases for the perception of chitin fragments as a first step in the defense response of plants against fungal pathogens (document: US 2012 / 6110696). (Q) Defoxifying genes, such as fumpmsin, beauvericin. mgnWormina and zearalenone and its 35 structurally retarded derivatives. See, for example, US Patents 5,716,820; 5,792,931; 5,798,255; 5,846,612; 6,083,736; 6,538,177; 6,388,171 and 6,812,380. (R) A polynucleotide encoding a cystatin and cysteine ​​proteinase inhibitors. See Humerus United States Cough Powerful 7,205,453. (S) Genes Je Feñsta. See WO 2803 / 008863 and US Patents ndmem 6411,377; 6,853,865; 6,777.592 and 7..238,781. (T) Galles that confer resistance to namatedos. See, for example, PCT Application WO 1996 / 30517; PCT Application W0 1993 / 19181, WO 2003 / 033651 and Urwin, etaí, (1998) 5 Planta 204:472-479, Wfemson. (1999) CurrÓpió Pieot Bio, 2(4):327-31; fes US Patent Numbers 6,284,948 and 7,301,069 and mR164 genes (WO 2012 / 058266). (U) Genes that provide resistance to Phytephthora root rot, such as Rps 1, Rps 1-a, Rps 1-b, Rps 1-c, Rps 1-d, Rps 1-e, Rps 1 genes -k, Rps 2, Rps 3-a, Rps 3-b, Rps 3-C, Rps 4, Rps S, Rps 6, Rps 7 and other Rps genes. See, for example, Shoemaker, ef at, Phyiophih&ra T0 Roof Roi R&& / stance Gene Mappmg m Soybean, Plant Geneme IV Conference, San Diego, Calrf. (1995), (Vj Genes that confer resistance to brown stem rot, such as those described in US Patent No. 5,689,035 and incorporated by reference for this purpose, (W) Genes that confer resistance to Coiletotnchum, such as ios described in and incorporated by reference for this purpose in United States Patent Application US 2009 / 0035765, Publication 15. This includes Rcg loeus, which can be used as conversion of a sote locus, 2, Transgems that confer resistance to a herbicide, for example: (A) A polynucleotide encoding resistance to a herbicide that inhibits the growth point or meristem, such as an imidazolidinons or a sUfonylurea. Exemplary genes in this category encode the AIS enzyme and mutant AHAS .- as described, for example, by Lee, et al. (1988) EAfSO J, 7:1241 and Mita, ©fal, (1990) neor. Appl, Gerset 80:449, respectively. See also US Patent Numbers 5,605,011: 5,013,659; 5,141,870-5,767,361; 5,731,180; 5,304.732, 4,761,373: 5.331107: 5,928,937 and 5,378,824. United States Patent Application Serial Number 11 / 683,737 and International Publication WO 1996 / 33270. (B) A polynucleotide encoding a protein for resistance to glyphosate (resistance imparted by 5renolpifWiL3·^ synthase (EPSP) and araA mutant genes, respectively) and other phenotype compounds, such as glufosinate (phosphinetridne aoetlj transferase (PAT) genes). , selectable marker of Sfreptomyoes coe / ico / or (A3) (DSM-2) and of iosphinocin acetyl transferase from Streptomycas hygrvscopicus (bar)) and pyridinoxy or ferioxy propionic acids and cyclohexones (genes encoding the ACGase inhibitor). See, for example, US Patent Number 4,940,835 to Shah, et al., which disclose the nucleotide sequence of an EPSPS toana that can confer glyphosate resistance. US Patent Number 5,827,061 to Barry. etet, also describes genes encoding EPSPS enzymes. See also, US Patent Numbers 6,566,587; 5,338,961; 6,248,876; 6,040,497; 5,804,425; 5,633,435; 5,145,783:4,971,908: 5,312,910; 5,188,642; 5,094,945, 4,940,835; 5,866,775; 6,225,114; 6,130,366; 5.31066?; 4,535,080; 4,789.061: 5,633,448; 5,510,471; Rs. 36,449; RE 37,287 E and 6,491,288 and International Publications EP 1173580: WO 2001 / 68704; EP 1173581 and EP 1173582, which are incorporated herein by reference for this purpose. The response to glyphosate is also conferred on plants that express a gene encoding a glyphosate oxido-reductase enzyme, as described in more detail in US Patent Nos. 5,776,769 and 5,463,175. incorporated herein by reference for this purpose. In addition, resistance can be imparted to! gfiphosate to plants by ia overexpression of genes encoding glyphosate N-acelyltransterase. See, for example, United States Patent Numbers § 7,462,481: 7,405,074 and United States Patent Application Publication Number US 2008 / 0234130. A DNA molecule that modifies a mutant areA gene can be obtained under ATCC® reference number 39256, and the nupheotide sequence of the mutant gene is disclosed in US Pat. No. 4,769,061 to Comal. EP Application Number 033 033 to Kumada, M, and US Patent Number 4,975,374 to Goodman, ei a / ., disclose de-gudeotide sequences of glutamine sinetase genes that confer resistance to herbicides such as LlosSnotrcina. The hucteotide sequence of a fosShdMch-acebl-toanferase gene is provided in EP Application Numbers 0 242 246 and 6 242 236 to Lsemans, ei ai.; De Greef, yes af., (1989) BiaiTeGhnoiogy 7:6, describe the production of transgenic plants expressing: chimeric bar genes encoding phosphin tricin sestile transferase activity, See also US Patent No. 5,969,213; 5,489.520, 5,550.318; 5,874,265; 5,919,675; 5,581,236; 5,648,477; 5,646,024; 6,177,616 and 5,879,903. which are incorporated herein by reference for this purpose. The document US 2011 / 0107455 discloses the DSM-2 gene and the gene product dpi sequences as well as its use in plants resistant to the herbicide ghtosinata. Exemplary genes that confer resistance to fsnoxy propionic acids and etethohexones, such as sefoxidlma and haioxyfop, are the Acc1-S1 genes. Acc1-S2 and Accl20 S3 described by Marshall, eí (1992) Tbeor. appi. Gene!, 83:435, (C) A polynucleotide encoding a protein for resistance to a herbicide that inhibits photosynthesis, such as a thazine (psbA and gs·:· genes) and a benzonitrih (Ceminiase gene), Przibüla . ei ai., (1991) Plañí Qeíl 3:169, describe the transformation of CMamyd&rfionas with plasmids encoding mutant psbA genes. The nucleotide sequences for hitlase genes are disclosed in US Patent Number 4,810,648 to Stalker and DNA molecules containing these genes are available under ATCC Reference Numbers* 53435, 67441 and 67442. Cloning and the expression of DNA encoding a glutethione S-transferase is described by Hayos. etal (1992) Yesoehem. J 285:173. (D) An oolinuclétide encoding a piar protein with resistance to Acetohydroxyacid synthase, which has been discovered, what? renders plants expressing this enzyme resistant to multiple types of herbicides, it has been introduced into a variety of plants (see, for example, Hation, si al, 1995) JWo / Gen Genet. 246:419). Other genes that confer resistance to herbicides include: a gene encoding a rat cytochrome P45Q7A1 chimeric protein and yeast NADPH-cytochrome P4S0 oxidoreductase (Shióta, ei aL (1994) Plañí Physiol 196:17). genes for ghtathione reducase and superoxide dismutase (Aoho, yes ai.. (1995) Pl&rít Cell PhysiGi 36:1687) and genes for various phosphotrensferases (Dada, et al. (1992) Plañí Mol Blol 20:619), (E ) a polynucleotide that encodes resistance to a herbicide that is. targets ta protoporphyrinogen oxidase (protox) which. It is essential for the production of chlorophyll, the protox enzyme serves as a target for a series of herbicidal compounds. These herbicides also inhibit the growth of all the different plant species present, causing their total destruction. The development of plants containing Altered prctox activity that are resistant to these herbicides was described in the Patents: of the United States number 6,288,306: 6,282.83 and 5,767,373 and in the International Publication WO 5 2001 / 12825. (F) The aad-1 gene (originating from Spírtgbó / ton hen^ / óvo7a«s) encodes prolein aritoalkanoateO'didxigenase (AAD-1). The trait confers tolerance to 2,4-dichlorophenoxyacetic acid and ariioxlfenpxypropionate herbicides (commonly cited as *fop* herbicides such as quizatofop). The aad^1 gene, soto, for herbicide tolerance in plants was originally disclosed in WO2005 / 107437 (see also US 2009 / 00S3366 ). The aad-12 gene, denvacu from DeWa actoowans, encoding the protein aryloxyalkanoate dioxygenase (AAD-12) that confers tolerance to 2,4-dicphorophenoxyacetic acid and pyrldyloxyacelate herbicides by inactivating several herbicides with an aritoxyalkanoate moiety, including phenoxy auxin (eg 2,4-D, MGPA), as well as pyridyloxy auxins {eg fluroxypyr, trichopyr). (G) A polynucleotide encoding a herbicide resistant dicamba monooxygnase disclosed in United States Patent Application Publication 2003 / 0135879 for cdniferlr tolerance to dicamba; (H) A polyfoucteotide molecule encoding bramoxynylnitrilase: (Bxn) disclosed in US Patent No. 4,810,648 for conferring tolerance to bromoxynil: (!) A polynucleotide molecule encoding phytoeng (crti) described in Mísawa, st a / ., (1983) Piad J, 4:833-840 and in Misaba, al., (1 §94} Plañí J. 8:481 -4.89 for tolerance to North America. 3. Transganes that confer or contribute to an altered glano characteristic; 4. Genes that control male sterility; 5. Genes that create a site for site-specific DNA integration; 6. Genes that affect resistance to abtotic stress; 7, Genes conferring increased performance: and / or 8, Genes that confer digestibility of the plant, 9. Gene silencing. In some embodiments, the accumulated trait may be in the form of silencing one or more polynucleotides of Interest resulting in the suppression of one or more polypeptides of the target pest. In some realizations. silencing is achieved using a deletion DNA construct. In some reactions, one or more polynucleotides encoding IRDIG3S563 polypeptides or fragments or variants thereof may accumulate with one or more polynucleotides encoding one or more polypeptides having Insecticidal activity or agronomic traits as discussed above and opioinally may further include one or more pejinuoleotide that provide genetic location of one or more target pcyllinucleotides, as described below. A “DNA construct of. Deletion is a recombinant DNA construct that when transformed or integrated in a systematic way into the plant genome, results in the detection of a target gene in the plant. The .daily gene may be endogenous or transgenic to the plant. "Suppression", as used herein with respect to the target gene, generally refers to the suppression of the levels of mRNA or protein / snzyme expressed by the target gene and / or the level of enzyme activity or the protein functionality. The term suppression includes down-reducing, declining, diminishing, inhibiting, eliminating and preventing» ''Gene silencing,'' does not specify the mechanism and is inclusive of, and not limited to, antisense strategies, co-suppression, viral suppression, hairpin suppression , jRNA-based stem-loop* suppression, and small RNA-based strategies. Some embodiments relate to the downregulation of target gene expression in insect pest species by interfering ribonucleic acid (RNA) molecules. PCT Publication WO 2007 / 074405 describes methods for inhibiting daily gene expression in invertebrate pests including the Colorado potato tea beetle, PCT Publication WO 2005 / 110088 describes methods for inhibiting the expression of target genes in invertebrate pests including the western bush raphe worm to control insect infestation. In addition, PCT Publication WO 2009 / 091864 describes compositions and methods for the suppression of target genes from insect pest species, including insect pests of the genus ARN-inclusive nucleic acid molecules for targeting the H subunit of ATPase vacuotar , dilles to control a population and infestation of Coleoptera pests, as described in US Patent Application Publication 2012 / 019558, PCT Publication WO 2012 / 055982 describes ribonucleic acid (RNA or double-stranded RNA) what inhibits or downregulates the expression of a target gene what encodes: an insect ribosomal protein such as ribosomal protein 1.19, the L40 ribosomal protein, or the S2?A ribosomal protein: a sublimity of the insect proteasome such as the RpnS protein te protein Pros 25. the protein Rpn2, te protein of the beta subunit 1 of the protease or the protein Pros bata 2; a β-coatomer of vesicle insect COPI, the y-coatomer of vesicle COR, the protein O'-coatomer or the ξ-ccatomer of vosicute COR; an insect Tetraspanin 2A protein which is a puta transmsmbrane domain protein; an insect protein belonging to the actin family such as Actin 5C; an insect ubiquitin-SE protein; an insect protein Sec23 which is a GTPase activator involved in intracellular protein transport; an insect crinkled protein that is a non-conventional myosin that is involved in motor activity; an insect crooked neck protein that is involved in the regulation of nuclear mRNA alternative splicing; an insect H*-ATPase vacuoter G subunit protein and an insect Tbp-1 such as the Tal-binding protein ds PCT publication WO 2097 / 035550 describes a ribonucleic acid (RNA or double-stranded RNA) that inhibits or downregulates the expression of a target gene encoding SnfT, US Patent Application Publication 2011 / 0054007 describes RPS10-targeted polynucleotide targeting elements.US Patent Application Publications 2014 / 0275208 and US2015 / 02573B9 describes polynucleotide silencing elements that target RyanR and PAT3 PCT Patent Application publication WO2016 / 138106 describes polynucleotide silencing elements that target the afe or gamma coatomaner The cough Patent Application Publications United States 2012 / 029750, US 20120297501 and 2012 / 0322660 describe interfering ribonucleic acids (RNA or double-stranded RNA) that work after ingestion by a species insect pest for downregulating the expression of a target gene in said insect pest, wherein the RNA comprises at hand a silencing element wherein the Silencing Somanth is a region of double-stranded RNA comprising hybridized complementary strands, one strand of which comprises or consists of a nucleotide sequence that is at least partially complementary to a target nucleotide sequence within! target gene. US Patent Application Publication 2012 / 0164205 describes potential targets for interfering double-strand ribonucleic acids to inhibit invertebrate pests including: a Chd3 homologous sequence, a beta-tubuin homologous sequence, a V homologous sequence -40 XDa ATPase, a homologous sequence of EF1 a, a homologous sequence of the ρ2β subunit of the 26S proteasome, a homologous sequence of the juvenile hormone epoxide hydrolase, a homologous sequence of the can-ai protein of Chloride-dependent inflammation, a homogeneous sequence of a glucose protein Mosphate l-Cteshydrogenase,. a homologous sequence of the Act42A protein, a homologous sequence of ADP-inhibition factor 1, a homologous sequence of the transcription factor I!B protein, homologous sequences of chitináSá, a homologous sequence of the ubiquitin corygator enzyme, a homologous sequence to gltoeraldehyde-3-phosphate dehydrogenase, a ubiquitin B homolog, a juvenile hormone esterase homolog, and an alpha tuhulin homolog. Use in pest control dyes, General methods for employing strains comprising a nucleic acid sequence of the embodiments or a variant thereof in the pest control plant or in the genetic engineering of Other organisms as pesticidal agents are known in the art. . Host microorganisms known to occupy the lithosphere (phylloplane, phyllosphere, rhizosphere, and / or rhizoptane) of one or more cultures of interest can be selected. These microorganisms are selected so as to be able to compete successfully in the particular environment with naturally occurring microorganisms, provide stable expression and maintenance of the gene expressing the IRDIG35563 polypeptide, and desirably provide better protection of the pesticide against deactivation and degradation m&dtoambiehtates, Alternately, the IRDIG3S563 polypeptide was produced by introducing a heterologous gene into a host cell. Expression of the heterologous gene results, directly or indirectly, in the intracsiary production and maintenance of the pesticide. These cells are then treated under conditions that prolong the activity of the toxin produced in the cell when the cell is applied to the environment of the target pest(s). The resulting product retains the toxicity of thuxin. These naturally encapsulated IRPIG35563 polypeptides can then be formulated according to standard techniques for their environment in which a target pest is hosted, for example, often. follow and ef foliage of plants. See, for example, EPA 0192319 and references cited therein. Spray applications are another example and are also known in the art. The subject proteins can be formulated appropriately for the desired end use: and then sprayed (or otherwise applied) on or around the plant or in the vicinity of the plant to be protected before an infestation is discovered. , after I know target insects are discovered, both before and after and the like. For example, bait pellets can also be used, and are known in the art. Pesticide gompositones. In some embodiments, the active ingredients can be applied in the form of compositions and can be applied to the growing area or the plant to be treated, simultaneously or in succession, with other compounds. These compounds can be fertilizers, herbicides, cryoprotectants, surfactants, detergents, pesticide soaps, sleeping oils, polymers and / or timed release or biodegradable vehicle formulations that allow long-term dosing of a target area after a single application of the formulation. They can also be selective herbicides. chemical insecticides, virucides, microbicides, pesticides, fungicides, basferiocides. Nematics, molluscicides » Mixtures of several of these preparations, if desired, together with additional agriculturally acceptable vehicles, surfactants or adjuvants that promote application can be used in the formulation. Suitable vehicles and adjuvants can be solid or liquid and correspond to substances commonly used in formulation technology, for example, natural or regenerated mineral substances, solvents, dispersants, wetting agents, adhesives, binders or fertilizers. Likewise, the formulations can be prepared into edible baits or shaped into pest traps to allow feeding or ingestion by a target pest of the pesticide formulation. Methods for applying an active ingredient or biochemical composition containing at least one of the 1RDK335563 pdlpeptidgs produced by the bacterial strains include foliar application, seed coating, and soil application. The number of applications and application rate depend on the intensity of infestation by the corresponding pest. The composition can be formulated as a pofvOj powder, mphomagranules, granules, spray, emulsion, colloid, solution or the like and can be prepared by conventional methods, such as drying, lygphilization. homogenization, extraction, filtration, centrifugation, sedimentation or concentration of a culture of polypeptide-containing polypeptide. 99% by weight. Lepidopteran, Dipteran, Heteropteran, Nematode, Hempteran, or Coleopteran pests may be eliminated or reduced in number in each area by the methods of the disclosure or may be applied prophylactically to an environmental zone to prevent infestation by a susceptible pest. Preferably, the pest ingests or is contacted with a peasing effective amount of the polypeptide. Pesticidally effective amount, as used herein, refers to an amount of the pesticide that can cause the death of at least one pest or significantly reduce the growth, feeding, or normal physiological development of the pest. This amount will vary depending on factors such as, for example, the specific target pest to be controlled, the specific environment, location, plant, crop, or agricultural site to be treated, environmental conditions, and method. The rate, concentration, stability, and amount of application of the pesticidally effective polypeptide composition. Formulations may also vary with respect to climatic conditions, environmental considerations, and / or frequency of application and / or or the severity of the pest infestation. The described pesticidal compositions can be produced by formulating the bacterial cell, crystal and / or spore suspension or isolated protein component with the desired agriculturally acceptable vehicle. The compositions may be formulated prior to administration in an appropriate medium, such as freeze-dried, freeze-dried, dried, or in a suitable aqueous vehicle, medium, or diluent, such as saline or other buffer. The formulated compositions may be in the form of a powdered or granular material or a suspension in oil (vegetable or mineral) or water or oil / water emulsions or as a wettable powder or in combination with any other carrier material suitable for agricultural application. Suitable agricultural carriers can be solid or liquid. The expression vehicle acceptable from e| from an agricultural point of view” covers all adjuvants, inerts, dispersants, surfactants, thickeners, binders etc, which are normally used in pesticide formulation technology: these are well known to those skilled in pesticide formulation, such formulations may mixed with one or more solid or liquid adjuvants and prepared by various means, for example, homogeneously mixing, compounding and / or grinding the pesticidal composition with suitable adjuvants, using conventional formulation techniques. Suitable formulations and methods of application are described in US Patent No. 8,468,523, incorporated herein by reference. Plants may also be treated with one or more chemical compositions including one or more herbicides, insecticides, or fungicides. Exemplary chemical compositions include: Fruit / Vegetable Herbicides: Atrazine. Bromacífo, Diurún,. Glifasato, Linurón, Metribuzina, Simazina. Tafluralirsa, Ruazifop, Glufosinate, Halosulfuron Gown, Paraquat, Propizamide, Setoxydim, Butafertecito, Hafesulfuron, Indáziftem; Insecticides for fruits / vegetables: Aldicarb, Bacm'us thuriengiensis, Carbaryl, Carbofuran, C-terpyrifos, Cipermethnna. Deltamethrin, Diazinone, Malafion, Abactin, Cifiúirina / bsta-cifiutnna. Esfenvaleratc, L»bdacihalofona, ACéquínucíl, BifenaZato, Metaxífenózida, Novaíurón, Chromafenozida, Tiacloprid,. Dlnofefurqn, FluaCripirim, Tolfenpyrad, Clothianidin, Espirad iotofém Gammactnalofona Espiramcsiten uspmosud Rlnaxí^r, Cíazipir, Espinoteram, Triflumurón, Espirotetramat. Imidacteprid, Fiubandiamide, Thiodicarb, Metaflumizone, Srilfoxafior, Clflumethofen, Cyanopyrafen, irmdacfoprid, Clothianidin, Tiarnefoxam, Spinothoram, Thiodicarb. Flonicamid, Methiocarb, emamectin benzoate, Indoxacarb, Fortiazato, Femamifas, Cadusafos, Pyriproxylen, fenbutatine oxide, Hextíazox, Metemite, 4-n(6-Cíorpyridin-3fomethylM2,2-diflUórótiÓamíno1furan-3í5H)-one:: Fungicides for fratasfoortális: Carbendazim:, Chlorothalonil, EBDCs, Sulfur, Thiophanate-meHo. Azoxysyrobin, Cymoxanil, Fluazinam, Fosetii, Iprodione, Kresoximmethyl, Metalaxli / mefenoxam, Trifioxfestrobin, Etaboxam, ipfcvaBca^. Trifloxíestrobw, Fenhexamide, Oxpóconszófe fumerate, Ciazófamíd, FehamídOné, Zoxámida,. RGdXíestrobi^ Piracfostrobina, Giflufenamid, Bescsiid; Herbicides for cereals: Isaproturbn, BronwWt tocml, Fenoxls, Clorsulíuron, Cícdiftaíop, Dictotep, Diflufenicén, Fenoxáprop, Rorasulam, Flueroxypyr, Metsulfurón, Tríasulfurán, Fiucarbázona, iodesulfuran, Própóxícarbazóna. Picohnafen, MesQsuffurbn, Bsflübutamid, Pinoxadén, Amidosulfuróm Trfensulfyrón metiio, Tnbenuran. Flupyrsulfuron, SulfosuW Pirasulfotol, Piroxsutem, Floffenácfet,TtalkóXidim.,;Rrd^ for cereals; Carbendazim. Clcrotalonil, Azsxfestrobin, Giproconazole, Ciprodinil, Fenpropimorph, Epoxiconazot Krescxim-metiio. Quinexifém Tebucenazol, Trifloxystrobin, Simeconaze!, Picxystrobin, Pifactestrubin. Dimoxysirobin, Prctioconazole. FUoxastrobma, insecticides for cereals: Dimetoatc, Lambda-cshaltrina, Deitarnetnna, alpharolpermethrin, p-ciñutrin, Bifenthrin, Imidacloprid, Ciotiánidlna, Tíameípxam, Tiaclopnd, Acetamiprid, Dineiofurán, Chlorphinfos, Methamidofos, Oxídemeton-methiium, Pirimicarb, Methiocarb; the matte: Atrazine, Alacicr, Sromoxinii, Acetoctor. Dicamba, Cfopiraiid, (S-)Dimethenamid, Glufosinato, Glífosata, ísaxafeiK (S-JMetolaCior, Mesotríona, Nfcoscifmcm Prímtsb^urán, Rlmsulfurpn, Suicotrkmá, Fsramsuifurón, Topramezona, Septentricmai, Safiufenacil. Carbofuran, Clomirifabs, Blenthrin, Fipronil, Imidacloprid, Lambda-Cythothrin, Tefluthrin, Terbufos, Thiamethoxam, Glottianidin, Spiromesifen, Flubendiamide, Trifiamuron, Rmaxipir, Deltametrin, Thiedicarb, β-Ciflüthrin, Ctpermethnna, Bifecttma, Lafenuron, Triftamoron, Triftamoron Etiproi, Cíazipir, Tíadbprid, Acetarnipnd, Dmetofurán, Avermecfin, Metíoearb, Spirodiciofen, Spirotetramat: Fungicides for maize: Fenitropan, Tiram, Protlcccnazole, Tebuconazole, Trifloxystrobin, Herbicides for rice: Butaclor, Propanii, Azimsutfurón, Sensulfurón, M^ Cibalurén, op Féntrazámlda, Imazssul^ Mefenacet, Oxazictomef&na, Píro^ Piributicarb, Qütnclorac, Tsobencarb, indanotan, Flufenacet, Fenlrazarmda, Hatosu ifurón, Oxazlciomefbna, Berizebicie-ίάπ, Rrifialtd, Penoxsutem, Sispidbac, Oxadiargil, EWsutíurón, Pretiiacior, Mesdrinna, Tefunltríona, Qxadíazocá, Fetwaprop, Pirímisulfan: Insecticides for rice: Dtazinon. Fenitration, Fenebucarb, Monodotophos. Benfuracarb, Buprofszín, Dinoteturán, Flpronlí, Irgbadopdd, Isoprocarb, Tiactoprid, Chromaphenazide, Thiaclopnd, Knotefurán. Clothianidin, Etipral, Flubendiamide, Rinaxipir, Dsltamethrin, Acetamide, Thiamethoxam, dazlpir, Spinosad. Spinotoram, Emamecta-Senzoaro, Cypermethrin, Cartap. Metamidophos. Etofónprox, Tdazofos, 4*{((6-Cl&roiridimM^ difluoroethyljam^pona, Carbofuran. Benfuracarb: Fungicides for rice: Thieanate-methyl, AzQxlsstrcbine, Carpropamid, Edifenfos, Ferimzona, iprobenfos, isoprothioian, Pencicuron, Probenazol, Pyroquilón, Triciclazístro Tbírnazole , Dicíocimst, Fenoxanií, Simeconazoi, Tiadiníi: Herbicidas para el aiggdón: Diurón, Fluometurón, MSMA, Oxífluorfén, Prometrina, Trifluralina, Carfentrazona, Cíetodim, Fluazitcproutilo, Gíñósaw, Ncrflufazón, Pendimetalm. Plñbobác-sodio, Tnflóxísulfurón, Tepráioxidim, Giufosinsto, Fiurnfoxaz- na, f idiazuron; insecticides for cotton: Acephalous Aidicarb, Chlorpyrifcs, Cypermethrin, Deltameirin, Malathion, Monocrotophos, Abamectin, Aqelamsprid, Emamectin Benzoate, Imldadopnd, indoxacarb, Lambda-Cihetatana, Espumad, Thiodicarb, Gamma-Cíhatolnba, Spirolmesifénba , FlonicamKl. Flubeodiamide. Tnfiumuron. Rmaxipir, 8eta«Ctflutnna. Spiroletramat, Clotiartidiha, Thiamethoxam, Tiadopnd, Dinetofuran, Flubendlarnide, Gi azipír, Spinosas, Spinótoram, gamma Cihaiotrina, 4-i[(6-Clorpiadin-3niimetfi](2,2foifiuor<4.ti)amir^ Thiodicarb, Awnec'm, Ftónicamíd, Piridajil, Espircmesílen, SylfoxaSpr, Proferidos, Tnazpfós, Endosuifám Fungicides for him S cotton: Etrkiiazoh 'Metatox^ Qulntozene; Soybean herbicides. Aiador, Bentazone, Tdfluralfn, Chlorimuron-ethyl, Cioransulam-Metiio, Fenoxaprop, Fomesafen. Fluazifop, Glyphosate, Imazamox, Imazaqutn, Imázétapír, (S-)Métolador, Matribyzfn. PentSmetallih, Tepraloxydim, Glufosinatg; insecticides for the saja: Lambda-cyhaiothrin, Metomil, Parando, Tiocarb. Imidaclopnd, Cíoüanidtna, Thiamethoxam, Thiacloprid, Aceiatnlpríd, Dmetofurán, Flubendiamide, Rinaxipir. Cyazipir, Spinosad, Spiriptoram, Emamectin-Bénzo^ Etiprole, fieltamethrin, 8-Cyfluihna, gamma and lambda Cyhaiotrin, 44((6CiQrpyridin-S-ÍiJmetiiXXZ-difiupretiiJamíno Spirotétramát, Espmodiclofen, Triflumuron, Flon icamid, Tíódicarb, beta-C iflotrina: Fungicides for Ja sóia: Azoxystrobin, Ciproconazoi, Epoxiconazole, Flstriáfol, Píracbeslrobína, Tebuconazg!, Trifloxiestrobina, Protíoconazoí, Tetraconazcí; Sugar beet herbicides: Cioridazón, Desm&dííam. Ethofumesate, Fenmedipham, Triaiató. Ciopyraiid, Fluazifop, Lenacil, Metamitron, Qumnwac, Cicíoxidim, Triflusulfuron, Tepraloxidirn, Quizaiofóp; sugar beet insecticides: imidadopríd, cyothianidin, thiamethoxam, thiacloprid, aeelamiprid, dinethofuran, deftamethrin, β-GÍflufnna, gammafiambda gihátethrin, 4-[[(6-C}grpindm-3il)med|K2,2-difiuóréti1jamino]forar^ TeMrin®, Rinaxipir, Ciaxlpir, Rpronito, Garbofuran·: Herbicides for the top»; Ctepiralid, Dicloíop, Fluazífop, Glufosinafo. Giifosate, M&iazaelop TriHuralin Etamat Sulfuron, Quinmarac, Quizalofbp, Ctetodim. Theoraioxydim; Fungicides for rapeseed: Azoxysstrobina, Carbendasim, Fludioxoníi, iprcdiona, Procloraz, Vindozolm; Insecticides for rapeseed: Carbofuranp organophosphates, pyrefroids, Thiacíoprid, Geltametriaa, imidadqprid, Glotíánidiria, Tíamaioxam, Aceiamiprid. Dinetofuran, β-CiSutnna, gamma and lambda Gihafotrind, tsu-F|üváler^ Etiprole, Spinosad, Espinoforam, Flubendiamide, Rínaxipír, Ciazipir, 4-[K.6-Cloφiridin-3-íl)methyl](2!2.foífiuoretíl )8m:ínojfuran*2(6:H)-Oi^s, In some embodiments, the herbicide is Afrazir®, Bromadl, Diuron, Qtorosulfürdn, Mateulfurom Thifensulfuron Methyl, Tribenuron, Acetochlor, Dicamba, Isuxaflutole, Nícosuifuron, Rimsuffuron, Pidtiobaodium. Rurmoxazine, C torimurón-Etiío, Mstrlbuzín, Quizalcfop, S-m&tolacior, Hexadin® or combinations thereof. In some embodiments, the insecticide is Esfenvaterate, Cíorarttraniliproi. Methomil, Indoxacarb, 30 Oxamil or combinations thereof, Oiaouicidal and insecticidal activity. Pest1* includes, but is not limited to, insects, fungi, bacteria, nematodes, mites, fleas, and the like. Insect pests include insects selected from the orders Coleoptera, Diptera, Hymenoptera, Lepidoptera, Malophagous, Homoptera, Hemiptera, Orthoptera, Thysanoptera, Dermaptera, Isoptera, Anpplurcs, Siphonaptera, Trichoptera, etc., in particular, 35 Lepidoptera and Coleoptera. The. compounds of the embodiments exhibit activity against insect pests, which may include ecornomically important agronomic, forestry, greenhouse, viwo, orhamean plant, food and fiber, animal and public health related, structural pests domestic and commercial, household and stored products. The larvae of the order Lepidoptera include, but are not limited to, heartworms, cutworms, caterpillars, and helictnos of the family Noctuidau, Spodoptera fegzperda ÜE Smith (maize armyworm); & meager Hübner (cogoltaro de la remoiarha); $. Jifera Fabricius (tobacco singing worm, drug of bunches); Mámesfra confines her Walker (cogolterabortha); M. toassfeaa Linnaeus (cabbage moth); Agrotis ipsifen Hufnagel (black cutworm); A. orthogon® Morris» (western cutworm); A subterranean Fabricius (granular cutworm); Afaóama árgfeeáa Hübner (cotton leafworm); Trichopíusia ni Hübner (cabbage caterpillar); Pseudopíusia includens Walker (W soybean caterpillar); Anticarsia gemmatalis Hübner (velvet bean caterpillar): Hypena saabra Fabricius (green clover worm); Heliothis wrescens Fabricius (tobacco fruit worm); Pseudaiptia unipunda Hawrth (heart); Atfieés mM&ra Bames and Mcdunnoygh (rough-skinned cutworm); Euxoa massoda Harris (dark-sided cutworm); Barias fesuiapa Boisduval (spiny caterpillar); E. vi'tiafia Fabricius (speckled caterpillar): Hetieaverpa armigera Hübner (American caterpillar); H, Boddie zea (cotton caterpillar), Mefanchra beta Harris (zebra caterpillar); Egíra (Xytomygas) cüríaíis Grate (citrus cutworm): borers, moths, shoot worms, pinnae worms and asgueletizers of the family Píralidae Osfeda nubítatís Hübner (European corn borer); Amyeipi& traesífeHa Walker (orange ship worm); Anegaste ku&hnidfe Zélter (Mediterranean flour moth); Cadra badelfe Walker (almond pin); Cbife suppressafe Walker (rice stem borer); C. partete, (sorghum borer); Comyra oeph<rt» / ea Stainton (rice moth); Crambas caí / ginosete Qiemens (maize shoot worm); C. teterrete Zíncken (forage grass shoot worm); Cnapha / ocrocíS medmafs Guenée (rice leafroller); Desmía feaerafís Hübner (grape leaf folder); Dfaphánia hyatete Linnaeus (melon worm); D. nfódaf&Stoll (decomposer worm): D / alr&&& grandiose / fe Dyar (southwestern corn borer), D. sáccharaZte Fabricius (sugarcane borer): Eoreuma fcW Dyar (Mexican rice borer); Ephesí / a eluteilta Hübner (tobacco (cocoa) moth): Gaitería metíondia Linnáéus (greater wax moth); Herpategramma W^ker (grass shoot worm); Hamo&osoma Hulst (sunflower moth): Sasmopa / pus égnosste (lesser corn thalium borer); Gray Acteofe Fabricius (lesser wax moth) Loxostege sfibiicabs Linnaeus (beet sprout worm); Orthaga íhyrisaüs Walker (tea tree bud poHla); Ajaraca fesfu / afe Geyer (bean pod borer); Plodia interpunctelia Hübner (Indian moth of the Hanna); Scbp&phaga mGertfeas Walkér (yellow stem borer); Weewé^iífo Gusnée (celery defohader); and leafrollers, fruit worms, seed worms, and treat worms of the family Tortactaae, Aoferd gfoverana Walsingham (Western black-headed fruit worm); A váfíapa Femald (oriental red-headed fruit worm); Arcrt / ps argyrosp / fe Walker (leaf wrapper of fruit trees); TO. rosana Linnaeus (European leafroller); and other Ardiips species. Adoxophyas arana Fischer ven Rossierstamm (tortricid stick bears fruit in summer); Cócriy / ís paspes Walsing (banded sunflower moth); Cydfe iátiferr&ana Walsingham (hazelnut tea worm); C, / xwflwWa Unnaeus (mwiana moth); Pfofynote testes Ciemens (coiled or leaf-vanegated); P. tetona Walsingham (omnivorous leafroller); tebesfe bofwa Genis and Schlffermüller (European moth of fes vines); Spteota oceífana Genis and Schiffermüííer (moth with eyespots); Endopw v / team? Cíemeos (grape moth);: jEppoecW ambiguefíe Hübner (vine moth); Bonsgota sa / udricófe Meyrlck (Brazilian apple leafroller): Grapnoííla molesta Busck (Oriental fruit moth); Stema ñstetMna Riley (sunflower moth); Afgyrotaérda spp spp,; and Cbonstoneura spp. Other selected agronomic pests from the order Lepidoptera include, but are not limited to. A / sopW ροηταίρφ Hante (autumn looper); ffoeste / fe Zeíier (borer of the méídc&lón remitas); Anísate senator J.E. Smith (orange-striped rubte worm): Anteeréea pemyí Guérin^Méneville (Chinese oak Tussah chick); Sombyx mori Linnaeus (silkworm); Buceafafrix fiarbsrieíÍa Busck (cotton leaf borer); Cote emytoeme Boisduvaí (alfalfa caterpillar); Batana / ntagerríma Grate and Robinson (walnut caterpillar); btertórotous $$&&&$ Tschetwedkov (Siberian silk moth), ©momos would remedy Hübmr (elm worm); Erarte Waría Harria (caterpillar 1S of linden); Eaprctobs teysortoo (mamen-tailed moth); Harrisina americana Guérin-Ménevife (grape leaf skeletonizing worm): Henjferaa oiMae Cocktail (range caterpillar); HyphMtria cunea prury (retia worm); Kaitena iycnp&fsiceiia Waisingham (tomato pinworm); Lambdim teeSada testefo Hüíst (Caterpillar d^ Eastern Hemlock!); £, fseelfeda the western deuta); Walleye Unnaeus (satin moth): Lymantn'a dispar Unnaeus (gypsy moth); Manduca gdfogúemacidata Haworth (five-spotted falcon poiilfe, tomato hornbill); M. sexta Hawórth (tomato shoot, tobacco shoot); Opefophteta temafa Línnaéus (winter moth-; Páfeacdtá tapate Peck (spring looper); Papr / fo crespñonfes Cramer (giant swallowtail, orange dog): Ph^gante traWfte Packard (oaiifornianQ oakworm)^ afretta Stainton ( Citrus leafminer), Phyllonorycter biancardeffa Fabricius (spotted leafminer); Pieria bmssicae Unnaeus (large white butterfly); P. rapae Unnaeus (small white butterfly); P. napí Unnaeus (green-veined white butterfly); P / afypte cardííídactyla Rifey (poííüa plume de afcachofa); Pñde / la xyteteiía Unnaeus (diamond back moth); P&ctinaphara gossypíslfa Saunders (rasada caterpillar); Porfea protodtee Bbisduval and Leoohté (southern coi worm); Sabulúd&s asgrofata Guanee (omnivorous caterpillar ); Sch / zura concinaa J E. Smith (red-bump caterpillar): 3Q catéate^ Olivier (poíitla del grano Angoumo>s); Thaiim&tapoaa p / iyocampa Sehifferrnuiter (pine pracesipwia caterpillar); Tmo / a bisse / i / afia Hummel (polilia dé fe rapa forming networks); Fúta absó / ute Méyrlck (tomato miner); yponomeafa pade / the Unnaeus (ermine moth); Heáotñís subways Guenée; Ma / acospms spp. and Qfyyia spp. Urves and adults are of interest! order of Coleoptera including weevils of the families Anthribldae, Bruchidae, and Curcultonidae (including, but not limited to: Aníbonomi fS grand / s Sóhemap (weevil); Ü$5Orncjpí<us oryzopñte Kuschei (rice water weevil); Sírbpbte :^ Unnaeus (grain weevil); S, oryzse Linúaous (rice weevil); Bypsra punctata Fabnoius (cloverleaf weevil); Cylífídrocapíuru& adspérsus LaConté (sunflower thallium weevil); Smfcranyx fu / vué LéConte ( sunflower seed weevil); S. sorc&fes LeConte (gray sunflower seed weevil); Spfte.napáoras r^^^ (corn stingj); flea beetles, cucumber beetles, root maggots, beetles leaf beetles, potato beetles, and leafminers of the family Chrysomelididae (including, but not limited to, Sáy (Colorado potato beetle); D / ebmtfca virgífera virgifera LeConta (western corn beetle) ;0. Barben Smith and Lawrence (aKiterlSo Worm); 0, ufKtecfápupetate bcwsrd / Barber (doradilla); CMatocnenta .eu / fca^ Melshsimer (corn flea beetle); Phyltotr&ta cruciferas Goeze (cruciferous flea beetle); Phyllo^&ta stríaiaia (striped flea beetle), Co / aspfe brurmea Fabrícíus (grape tailspls); Outema melanopus Linnaeus (cereal flea beetle); Zygugramma ®xc / amafmis Fabrico (sunflower beetle)); beetles of the family Coccinellidae (including, but not limited to, Epilachna varivestis Mulsant (Mexican bean beetle)); rodent beetles and other beetles of the family Scarabeeidae (including, but not limited to: PapiHia japonica Newmae (Japanese beetle); Gycfócepriate fáweabs Arrow (northern masked squash, white thorn); C. ímmapulate Olivier (southern masked squawk , thorsalo white): Wzotrogas majafís RazQumgwsky (European chafar); PhyiÍcphágá crirtffa Burmeister {térsale· blanco); Ügyrus gibbo^us De Geer (carrot beetle)); carpet beetles of the family Dermestidae; wireworms of the family Baterida®, E / eodes spp., H^anotus spp; Gonoderws spp; Morw& spp; Cracks spp Cteblcers spp.; Aebius spp.; bark beetles of the family Seóiytidae and beetles of the family Tenébríonidae. Of interest are adults and immature larvae of Diptera, which include leafminers Agromyza parvícomís Loew (corn rot miner); midges (including, but not limited to: Cantarmia sorghicoia Coquilteit (sorghum midge); Mayetieía destructor Say (Hessian fly): íbMípte (trígq midge); Neotas / optera mürtfefátiaa& Felt, (sunflower seed midge)) ; fruit flies (TephtWae),-Oscinalfa frit Linnaeus (Fruit flies 25 you fruit); larvae (including, but not limited to; Delta pistura Meigen (corn larvae); D. Fallen coaretáta (wheat top fly) and other Oé / fa spp., Weromyza americana Rteh (wheat thalium larva); Mltscá domestica Linnaeus (houseflies); PaPnia canicularís Linnaeus, F. femoralis Stein (small houseflies); Sirwpuxys-cafc / trans Linnaeus (stable flies)); face flies, horn flies, sucking flies, Chrysomya spp.; Pbormia spp. and other pests of museoid flies, horse flies, Horseflies spp., Gástroptuiss botflies spp.; G&sÍrus spp,; larvae of cattle Hypód&tma spp.; deer flies Chrysops spp.; W&tópbagus pvws Uhnaeus (keds) and other Braebycera, Aedes spp, mosquitoes; Apopifé / es spp.: Cutex spp.; black flies Prwmu / ium spp,; Simdiutn spp; biting mosquitoes, sand flies, sciurids and other rifemafocers. Insects of interest include adults and three nymphs of the orders Hemiptera and Homdptera, such as, but not limited to, adelgids of the Adelgidae family, plant bugs of the Miridae family, cycads of the Cicádida® family, leafhoppers, Empoasca spp.; of the Cicadelllldaé family, pipacélids of the CixúdaR families. Ratíriae, Fülg&oidea, Issidae and Délphacidae, treehoppers of the family Membratádag, psyllids of the family Ps^lidae, whiteflies of the family Aleyrodidae, aphids of the family Aphldidae, phylloxera of the family PhyílQxeridáe, weevils of the family Pseudococcidae, mealybugs of the families Asterolecanidae, Cocddae. Dactyiopiidae, Diaspididae, Enocoecteae, Qrthezlidae Phgenioaooucídae and Marganxfidae, lace biohosts of the family Tlngidae, stink bugs of the lamellae Pentatomidae, stink bugs, Bfesus spp., and other seed bugs of the family Lygaeidae, ceroopoids of the family Cercopidae, squash bugs of the family Coreídae and red bugs and cotton stains of the family Pyrrhocpridae. Agronomically important members of the order Homoptera include, but are not limited to: AsyrfhÍSfphon pisum Harás (pea aphid); Apñís cracervora Koeh (cowpea aphid); A. fabaa Scopoli (black bean aphid); A. gosaypii Giover (cotton aphid, melon aphid): A. madfradGis Forbes (corn root aphid); A. poml De Geer (apple aphid); A. pascóte Patch (aphid apirea); Atteortom (digital aphid); Chaptos / pocn fragaeMu Cocieres (strawberry aphid); Dtáraphtá natáa KurdjumovfMordvito (pink fig aphid); Dysaphis pl&nteginea Paaserini (pink apple aphid); Erroxoma iatwgmum Hausmann (woolly apple aphid); Srewcoryrre brésafcae Linnaeus (cabbage aphid); Hyátápl&ñi& pn / ní Geofiroy (mealy plum aphid); Lípapds érysimí Kaítenbach (turnip aphid); Wfopofophium dirrhorfum Wáíker (cereal aphid): MacfOSfpfwm auphorbtáe Thomas (aphid: potato); Myzus p&rstáaa Sulzer (peach-potato aphid, green peach aphid); Alásonowa diÍsdgri Mostey (lettuce aphid); Pemp / ugas spp. (root aphids and caecidian aphids); Rhopalosipham kill Fltch (Corn Leaf Aphid): R pad / 2S Ljnnaeus (aphid of cherry smooth and oats); Schízaphfe grammym Rondan! (wheat aphid); Srpña f / ava Forbes (yellow sugarcane aphid); Sítobto Avenas Fabricius (English grain aphid); Thertáaphis máatáata Bucktoa (alfalfa spotted aphid); Toxoptera aurantg Boyar de Fonsoclombe (black citrus aphid) and T. Gtátátáa Ktrkákíy (brown citrus aphid); Ade / ges spp. (thin skinny); Páy / toxera devastar,Ά Pergande (phylloxera of the pecan tree); Bemis / a tabací Gennadius (tobacco whitefly, sweet potato whitefly); B. atgenUfolñ Beliows and Perring (silverleaf whitefly); citri Ashmead (white citrus moss); Triataurodas abatitánsus (band-wing fly) and T. vaporartánim WesfwoGd (greenhouse whitefly); E / npoasca Harfis (potato hopper); Lapd&lphax sf / tádltás Fallen (smaller brown fuigorammfo^ Ma&btástás gbadri / ífíeaítís Forbes (aster leafhopper); NepftiJíítáb: ctáftáeps Uhlsr (green clcadelid); M n / gfbptátbs Stáí (rice oicadélldo); Oapanrafa tágans Stál (brown leafhopper); Peregr / nus maídís Ashmead (corn cycad); SogafeAs Mera Hcrvath (redneck-backed warmbird). Rope all orwóo / a Muir (delfácído déi árózj; TypfiÍabyba ointment McAtee (white apple cicada); &yíhroñeoura spp. (grape cicada); Magictáada saplsridec / m Unnaeus (periodic cicada): táerya pumhasi Maskell (ribbed mealybug); Quadraspídípfus permc / os^^ (San José mealybug); Rfanpcoccwe dfn Risss (citrus weevil); Pseudocaocus spp. (ob© weevil complex); Cacapsy / / a pyoco / a Foerstér (pear psyfla.); FríQzéd / ospyrr.AShm^ khaki), The species; Agronomically important of interest in the order Hemiptera include, but are not limited to:. Acr&stémím hilara Say (green thumbtack); Anasa fhsttá De Geer (pumpkin bug); Sfesus teucapisn / s feteopfems Say (bug); C^ryfáuóa gossyp / i Fabñpíus (cotton lace bug); Gydopellís modesta Dsstani (tomato bug); .Pysdereys swfwefcs HerríoteScháffer (cotton stainer); Euschfctus servas Say (brown stink bug). E. variotanus Palisot de Beauvois (single-spotted green bug); GrepiQst&lhus spp. (seed bug complex); § coreolas Say (Amencaha bug of the puffies): ¿ygus línsolafís Palisot de BeauvOíS (common meadow bug); L Hesperas Kmght (Higas bug}; L. pratea^s Linnaeus (Western meadow bug); L n^til^ehpís Pdppius (European lygus bug); Lygoeoris pabuiinus Linnaeus (Common green capsid insect}: Nexara viridula Linnaeus (bug southern green stink bug); Oe&atas pugnax Fabritaus (atrocious stink bug); Qppppeltvs fasdatus Dallas (large Mtoeed stink bug); Pssudafomosoefe serratas Reufer (jumping cotton flea). Furthermore, the embodiments may be effective against Hemiptera. tetes like, Calocoris norvegícus Gmelín (strawberry bug); Odhpps eampestris Flames; Plesiocoris tugict^a Fallen (apple capsid bug); Cyrtopoltis mod&stus Distant (tomato bug); Qyrtopeffis notalas Distant (sucking fly); Spamgomcus afoofescfetas Reuter (white-marked jumping flea); Diaphfioceris 1S ehlorioriÍs Say (bug of the three-spined acacia plant)· Labopídícela there; Knight (onion plant bug); PseudaiomoscoUs sedatus Rcuter (cotton jumping flea), Adefpbocons fast Say (fast plant bug!: Boeeitocanstís iin&atus Fabricius (four-lined plant bug): Mys / us encaé Schiliing (false bug) í^tó r&phanús Howarú (false stink bug); Atezara vírídula Linnaeus (southern green stink bug); ñvygaster spp., Coreóte spp, Pyrrhocoridw spp., Ttaítfae spp.; B / ostorn&lidae spp.: PeduA / dae spp. and CMidae spp. Also included are adults and larvae of the order Acarí (acara) such as Aceña fosich&fl& Keífer (rice curl áoarq); Pefmbía / atens Müller (brown mite of wheat); spider mites and red steels in the family Tetranychidag. Paíioflycte almi Kóch (European red bird); Arctic tatranychas. Koch (colon spider mite); (T. medanieli McGregor (McDamel's mite); T. airmabarinus Bolsduvaí (carmine spider mite); 7, (ur^ianZ Ugarov and Nikolski (strawberry spider mite); flat mites of the family Tenuipa!pidae (Brévípaipus lewisi McGrégor (mite mites of the citrus fruit); shoot mites and rusts of the Eriophyidae family and other foliar-feeding acers and steels important for human and animal health, that is, dust mites of the Epidormopidae family, mites of the follicles of | a family Demodicidae, grain mites in the family Glycíphagidae, fleas in the order Ixodidae, tedas seapufáris Say (deer tick), L holopyolus Nettmann (Australian paralysis tick), Permacenta·'· νόηοόΦδ Say (amertaana dog tick) ; Ámó / yómma amsncanom Linnaeus (lone star tick) and scabiotic mites of the families Psoroptidae, Pyémotidae and Sarcoptidae, Insect pests of interest include the superfamlfe of bed bugs and other related stink insects including, but not limited to, species belonging to the family Pent&tomidae (Negara viridula. Haiyarñorpba halys, Pfezodaru& gulldini. Eusdhistüs sem / s,. Aardstemom pilare, Easpfiisius Peros, Eusefrisfás Acf&sternum hitare, píchelops furcatí / s, Qíph&tpps m& / aaaftflu.is and Sagrada Ma^is (Sacred bug;}. la family Ptafasptaae (M&g&cGpts sibrada - globular stink) and family Cyó / VOss (Scs^ - root stink) and species of Lepidoptera, including, but not limited to plastron: diamond-backed poiiia, eg, Het / coverpa zea Bbddie: soybean caterpillar, for example, Rsetfoopteá mc / urferfe Wafker and caterpillar of the eg, Anticarsia g&mmataíis Hübner. Methods for measuring pesticidal activity include, for example, Caspia and Lang. (1990}J. .um. entorfío}. 83:2480-2485: Andrés, yes a / ., (1988) Bioch&m; J. 252199-206: Marrona, et al., (1985) ¿of£coriom / o Enromad US Patent No. 5,743,477, all quats are incorporated herein by reference in their entirety. In general, protein is mixed and laughed at feeding trials. See, for example, Marróse, et al, (1985) J. ©rancié. 78:290-293. Such tests may include contacting the plants with one or more pests and determining the ability of the plant to survive and / or kill the pest. Nematodes include parasitic nematodes, such as root-knot, cyst and lesion nematodes, including Reterodefa spp., Me / oidogyne spp. and G / obodera spp.; in particular, members of the cystic nematodes, including, but not limited to, Heterodera g / ycwes (soybean cyst nematode); Heférodera xchschd / (sugar beet cyst nematode); Heirloom oats (n^ of 15 cereal cysts) and Gfeóodera rostocfeensfe and Giododera-paffida (potato cyst nematodes). Lesion nematodes include Prafyfencbus spp. Seed treatment. To protect and empower! production yield and trait technologies, seed treatment options can provide additional flexibility to the breeding plan and cost-effective control against insects, weeds and diseases. Seed material can be treated, typically surface treated, with a composition comprising combinations of chemical or biological herbicides, herbicide savers, insecticides, fungicides, germination inhibitors and enhancers, nutrients, plant growth regulators and activators, bactericides , nematicides, avicides and / or moiu:sqi.iicides. Typically, these compounds are formulated together with carriers. additional surfactants or application promoting adjuvants used in the formulation. Coatings can be applied by impregnating the spreading mat with a liquid formulation or by coating with a wet or dry combination formulation. Examples of the various types of compounds that can be used as seed treatments are given in The Pesticsdé Manual: A World Compendium, C.D S. Tomlin Ed., Published by the British Crop Production Council, which is incorporated herein by reference, Some seed treatments that may be used on crop seeds include, but are not limited to, one or more of abscisic acid, acylbenzoic-S-mephipho, avermectin, amitroi, azaconazole, azospirilum, azadirachtin, azoxystrobioa, Sacilius spp. (including one or more of the bristle, firm, megaienum, pumife, sphaeñcus, subtilis and / or thunngiensis species), bradyrhizoolum spp. (which includes one more g of betas, canariense, elkanii, iríomotense, japonteum, ííaonigense, pachyrhizi and or yuanmíngense). captan, carbcxrns, chitosan, dothianidin, copper, ciazipír, WemeaneZdl, etidiazot, ílpronll, fiudíoxoml, fluóxastroblna, fiuquinoonazd, Ourazol. fiuxofenim, hairpin protein, imazalil, imidadoprid, ipconazd, isonavenaides, lipo-quitopligcsaccharide, manganese, maneo, mofenoxam, metalaxyl, metconazole, miclsbutanit PCN8, penflufen, peniciiiium, pentiopyrad, permethrins, picoxystrobin, 2G protitóGórazol, pyractostrobin, rinaxipir, S-metoaelor, sapanin, sedaxane, TCMTB, tebuconazole, thiabendazole tianwwn, tiocarb, tirara, talc.lofos-methyl, tnadtarengl, trichoderma, Wi&xtastrote triéconazole and / or zinc. PCNB seed coating refers to EPA tea registration number 00293500419, it contains quintozen and terrazzo!. TCMTB refers to s 2-(tfecyanomet¡tau; benzoüazol. Seed varieties and seeds with specific transgenic traits can be tested to determine what seed treatment options and application rates can complement such transgenic varieties and traits to improve yield. For example, a variety with good yield potential but susceptible to head blight may benefit from the use of a seed treatment that provides protection against head blight, a variety with good yield potential but susceptibility to nematodes qtastlcbs may benefit from the use of a seed treatment that provides protection against cyst nematodes and so on. Conversely, a variety embracing a transgenic trait conferring resistance to insects may benefit from the second mode of action conferred by seed treatment, a variety embracing a transgenic trait conferring herbicide resistance may benefit from a seed treatment. seeds with an insurer that enhances lá. plant resistance to that herbicide, etc. In addition, good root establishment and early emergence will result from proper use of a treatment: for seeds it can result in more efficient use of nitrogen, better ability to withstand drought, and an overall increase in potential. yields a variety or varieties containing a particular trait when combined with a seed treatment. Methods for Killing an Insect Pest and Insect Co-Population In some embodiments, methods for killing an insect pest are provided, comprising contacting the insect pest, either simultaneously or sequentially, with an insecticidally effective amount of a recombinant IRDIG35563 polypeptide of the disclosure. In some embodiments, methods of killing an insect pest are provided, comprising contacting the Insect pest with an insecticidally effective amount of a recombinant protein of SEQ ID NO: 2 or a variant thereof. In some embodiments, methods of contracting an insect pest population are provided, comprising contacting the insect pest population, simultaneously or sequentially, with an insecticidally effective amount of a recombinant 1RDIG35563 polypeptide of the disclosure, In some embodiments. Methods of controlling an insect pest population are provided, comprising contacting the insect pest population with an insecticidally effective amount of a recombinant IRD1G35563 polypeptide of SEQ ID NO: 2 or a variant thereof. As used herein, to control a pest population “to control a pest*” refers to any effect on a pest that results in the limitation of the damage caused by the pest. Control an inflicted pest, stop without limitation, eliminate the pest, inhibit the development of the pest, alter the fertility or growth of the pest in such a way that the pest causes less damage to the plant, reduce the number of offspring produced, producing fewer healthy pests, producing pests more susceptible to attack by predators, or preventing pests from feeding on the plant. In some embodiments, methods of controlling an insect pest population resistant to a pesticidal protein are provided, comprising contacting the insect pest population, either sinultaneously or sequeóciálraenl®, with an insecticidally effective amount of a recombinant IRBIG3S563 polypeptide. of disclosure. In some embodiments, methods of controlling an insect pest population resistant to a pesticidal protein are provided, comprising contacting the insect pest population with an insecticidally effective amount of a combinant íRD!G35563 polypeptide of SEQ. ID NO: 2 or an «arlante: of the same. In some embodiments, methods of protecting a plant from an insect pest are provided, comprising expressing in the plant or cell thereof at least one recombinant polynucleotide encoding an IRD1G35563 polypeptide. In some embodiments, methods of protecting a plant from insect pests are provided. an insect pest, comprising expressing in the plant or cell thereof a recombinant polynucleotide encoding a 1RDIG35563 polypeptide of SEQ ID NO: 2 or variants thereof. Strategies for pest resistance of insects ÜRy). The expression of δ-endotoxins gives β. tetmégfens / s in transgenic maize plants has been shown to be an effective means of controlling agriculturally important insect pests (Periak, efaL, 1990; 1993). However, insects have been evoke that are resistant to S-endotoxins from β. Ihuringí'ensfs expressed in transgenic plants. Said resistance, in case it were disseminated, would clearly limit the commercial value of the germplasm that contained said S-andotoxins of 8 One way of increasing the efficacy of GM insecticides against target pests while reducing the development of insecticide-resistant pests is to use non-GM refugia (ie. non-insecticidal protein) (a crop / non-insecticidal mafe section) for use on transgenic crops that produce a single insecticidal protein active against target pests. The United States Environmental Protection Agency jjomjrafi<sj^ where it can be accessed using the prefix www) publishes requirements for use with transgenic crops that produce a single Bt protein 30 active against target pests. In addition, the National Cora Growers Association, on its website: dofids can be accessed using the prefix "iww) also provides similar guidance regarding shelter requirements. Due to losses to Insects within the refuge area, larger refuges may reduce overall performance. Another way to increase the efficacy of transgenic insecticides against target pests while reducing the development of insecticide-resistant pests would be to have a repository of insecticidal genes that are effective against groups of insect pests and that manifest their effects through different modes of action. . 6S The expression in one plant of two or more insecticidal compositions toxic to the same species of insect, expressing each insecticidally at effective levels, could be another way of achieving control of the development of resistance. This is based on the principle that the evolution of resistance against two separate modes of action is much more unlikely than one. Roush, for example, § exposes strategies of two toxins, also called ''pyramid formation or accumulation for the management of insecticidal iransganic crops. (The Royal Society. Phil Trens. R. Soc. Lond. B. (1998} 353:1777-1786). The accumulation or pyramiding of two different proteins, each effective against target pests and with little or no resistance The US Environmental Protection Agency requires that 10 significantly less structured shelters (generally 5%) of non-Bt corn be planted than for single-trait products ( gweralnren^ 20%).There are several ways to provide the IRM effects of a refuge, including various geometric planting patterns in fields and in bagged seed mixes, as described in more detail by Roush, In some embodiments, the IRDIG3S563 polypeptides of the disclosure are useful as a strategy for managing insect resistance in combination (ie, forming a pyramid) with other pesticidal proteins including, but not limited to, Bt toxins, insecticidal proteins of Xenonhabdus sp. or PMoi'haMtJS sp,, other proteins with insecticidal activity and the like. Methods for controlling infestations by lepidopteran and / or coleopteran insects in a transgemc plant are provided that promote insect resistance management comprising expressing in the plant at least two different insecticidal proteins having different modes of action. In some embodiments, methods for controlling lepidopteran and / or coleopteran insect infestation in a transgenic plant and promoting insect resistance management comprise the presentation of. at least one of the insecticidal proteins of the IRDIG35563 polypeptide to insects of the order Lepidoptera and / or Coleoptera, In some embodiments, methods for controlling tepidopteran and / or coleopteran infestation in a transgenic plant and promoting insect resistance management comprise presenting at least one of the IRDIG35563 polypeptides of SEQ ID NO: 2 or variants of cough themselves, insecticides for insects of the order Lepidoptera and / or Coleoptera. In some embodiments, the methods for controlling infestation by lepidopteran and / or coleopteran insects in a transgenic plant and promoting the management of insect resistance comprise expressing in the transgenic plant an IRDIG35563 polypellid and a protein Cry or will hear protein insecticide for insects of the order of the Lepidoptera and / or Coleoptera that have different modes of action. In some embodiments, methods for controlling infestation by lepidopteran and / or coleopteran insects in a transgenic plant and promoting insect resistance management comprise expression in the transgenic plant of a polypeptKÍn IRDIG35S63 of SEQ ID ÑQ. 2 or variants thereof and a Cry protein or another insecticidal protein for insects of the order Lepidoptera and / or Coleoptera, where the RDIG35^3 eípoiípeptido and Cry protein have different modes of action. Methods are also proposed to reduce the likelihood of the emergence of resistance in lepidopteran and / or coleopteran insects to transgenic plants expressing insecticidal proteins to control insect species, comprising expression of an insecticidal IRD1G35563 polypeptide for the insect species. in combination with a? second insecticidal protein for the species of ins^o, which have different modes of action. Also provided are means for effective management of resistance in lepidopteran and / or coleopteran insects from transgenic plants, comprising co-expressing at high levels in the plants two or more insecticidal proteins toxic to lepidopteran and / or coleopteran insects, but displaying each a different way of firing its killing activity, where the two or more insecticidal proteins comprise an IRDIG35563 polypeptide and a Cry protein. Means for effective management of lepidopteran and / or coleopteran insect resistance to trmsgénicae plants are also provided. which comprise co-expressing at high levels in plants one or more insecticidal proteins toxic to lepidopteran and / or coleopteran insects but each showing a different way to carry out its killing activity, wherein the two or more insecticidal proteins comprise a IRDIG35563 polypeptide from SEQ ID NO: 2 or variants of fes themselves and a Cry u protein; another protein with insecticidal activity. In addition, methods are provided for obtaining approval from regulatory agencies for the planting or commercialization of plants expressing inseetfeid proteins for insects of the order Lepidoptera and / or Coleoptera, comprising the step of referring to. refer to or rely on data from insect binding assays showing that the IRD1G35563 polypeptide does not compete for binding sites for Cry proteins in insects. In addition, methods are provided for obtaining regulatory agency approval for planting or marketing plants expressing insecticidal proteins for insects of the order Lepidoptera and / or Coleoptera comprising the step of referring to, submitting or relying on. data from insect binding assays demonstrating that the IRD.IGW&3 polypeptide of SEQ ID NO: 2 or variants thereof do not compete for binding sites for Cry proteins in said insects. Methods to increase the yield of plants. The cure methods involve providing a plant or plant cell expressing a pplinucieotid that encodes the pesticidal polypeptide sequence disclosed herein and cultivating the plant or a seed thereof in a field infested by a pest against which the polypeptide has activity. pesticide. In some embodiments, the polypeptide has pesticidal activity against a lepidopteran pest, Coleoptera; Diptera, Hemiptera or Nematodes and the field is infested by a Lepidoptera, Hemiptera, Coleoptera, Diptera or Nematode swarm. As defined herein, "plant yield" refers to the quality and / or quantity of biomass produced by the plant. ‘’Slomasa*', as used herein, refers to any plant product measured. An increase in the biomass production is any improvement in the yield of the measured plant product. The increase in the yield of the plant has various applications. commercial. For example, the increase in foliar biomass of silver can increase ¢7 the yield of foliar vegetables for human or animal consumption. In addition: the increase in foliar biomass can be used to increase the production of pharmaceutical products or derived industries. floors. An increase of| re.ndim tempted may include any statistically significant increase including, but not limited to, an increase of at least 1%, an increase of at least 3%, a S increase of at least S%, an increase of at least 10%, an increase of at least 20%, an increase of at least 50%, at least 75%, at least 100% or greater in performance compared to a plant that does not express the pesticidal sequence. In specific methods, plant yield is increased as a result of improved pest resistance of a plant expressing an IRDIG35563 polypeptide disclosed herein. Expression of the ÍRDIG35563 polypeptide results in the reduced ability of a pest to infest or feed on the plant, thereby improving plant performance. Processing methods. Further provided are methods for processing a plant, plant part, or seed to obtain a plant, plant part, or seed food or food product comprising an IRQIG3S563 polynucleotide. The provided plants, plant parts, or seeds herein they can be processed to produce oil, protein products and / or by-products that are derivatives obtained through processing that have commercial value. Non-limiting examples include transgenic seeds comprising a nucleic acid molecule encoding an IRDIG35563 polypeptide that can be processed to produce soybean oil, soybean products and Z© soybean by-products, Trocasam lenta refers to any physical or chemical method used to obtain any product from soybeans and includes, but is not limited to, heat conditioning, flaking and milling, extrusion, solvent extraction or aqueous soaking, and extraction of whole seeds or partial, When an insect comes into contact with and ingests an effective amount of toxin delivered through the expression of transgenic plants. formulated protest composition(s), whether sprayed protein compositions, a bait matrix, or other qommtsiration system, the results are typically insect death, or the insects fail to feed on the source making the toxins available to the insects. insects. With suitable microbial hosts, eg, Fseudomonas, the microbes can be applied to the pest environment, where they will proliferate and be ingested. The result is the pest control. Alternatively, the microbe harboring the toxin gene can be treated under conditions that prolong the activity of the toxin and stabilize the cell. The treated cell, which retains toxic activity, can then be applied in the environment of the target pest, examples EXAMPLE 1 Construction of plasmids of the insecticidal toxin |RDt|G3SS6g and axmesin in bacterial hosnadonas. Conventional donation methods were used in the 6S construct of Rseudomoftas ffworwens (PO) expression plasmics engineered to produce IRDIG3S563 proteins encoded by plant-optimized coding regions. Restriction endonucleases and T4 DNA Ligase were obtained from New Engiand BioLabs (NEB. Ipswích, MA) for restriction digestion and DNA ligation, respectively. Piasmid S preparations were made using the NucteoSpin ® 1 Piasmid Kit (Machérey-Nagél Irte, Bethlshem, PA) following the suppliers' instructions for purification of low copy plasmids. DNA fragments were purified using a Kft QlAqüich® Gol Extraction Kit (Qisgen, Vento, Umburg) after elactrophoresis on Tris-acetate agarose gel. The basic cloning strategy involved subcloning the toxin coding sequence (CUS) IRDIG35693 (SEQ ID NO:1) into pDOWTWO into the Sp&l and Saft résíriéióh sites so that it is placed under the expression control of the Pt&c promoter and the rrnBT1T2 terminator da! plasmid pKK223-3 (PL Pharmacia. Milwaukee, W). pDOW1 169 is a medium copy plasmid with the RSF101Q origin, a pyrF gene, and a ribosome binding site preceding restriction enzyme recognition sites into which DNA fragments containing coding regions can be introduced. of protein (US Application 20080193974). The expression piásmldo, designated pDOW1169. was transformed by electroporation into DC454 (a strain of R fluaiGsccns close to wild type that has deftapyrF and IsgOlaeR mutations), or its derivatives, recovered on Soy Hydrogen medium and plated on selective medium (M9 glucose agar which lacks uracite). , Sambraok et al., supra). Details of these microbological manipulations are available in Squires $íai, (2004), US Patent Application. 20060003877, US Patent Application 20038193974 and US Patent Application 20060068262, incorporated herein by reference. Colonies were first screened by restriction digest of miniprep plasmid DNA. The plasmid AON from the selected clones containing the IRDIG35563 toxin were digested with four restriction enzymes and sequence verified to further validate the presence of the insert. EXAMPLE 2 Cg analysis and expression in shake flasks. Production of IRDIG35S63 toxin for characterization and bioassay in insects was achieved by P. teroscens strains grown in shake flasks harboring expression constructs (pDOW11S9). A culture glycerol stock solution of IRDIG35563 (0 S ml) was inoculated into 5 ml of production medium defined with 9.5% glycerel (Teknova Catalog No. 3D7426, Hellister, CA). Expression of the IROIG35563 toxin gene through the Ptsc promoter was induced by the addition of isopropyl-g-D-ltiogalactopyrsnosyl (IPTG) after an initial incubation of 24 hours at 38”C with shaking. Cultures were sampled at the time of induction and at various times after induction. Cell density was measured by optical density at 600 nm (OD®»). Other culture media suitable for the growth of Peectdomonas fk / oreacens can also be used. for example, as described in US Patent Application 20060068877, EXAMPLE 3 Ambacterium transformation. Standard cloning methods were used in the construction of binary plant expression and transformation plasmids. Restriction endonucleases and T4 DNA Ligase were obtained from New England Sidabs. Plasmid preparations were made using the NucteoSpin® Rasmid Kit. Preparation or the NucleoBond* AX Xlra Midi kit (both from Mácherey-Nagel, Duren, Germany), following the manufacturers' instructions. DNA fragments were purified using the QIAquick® PCR Purification Kit or the QIAEX Ü® Gel Extraditen Kit (both from Qiágen Venta, Ümburg) after isolation in gal. Electro-competent cells of Agrobacienym totetec / ems strain Z707S (a streptomycin-resistant derivative of 2707: Hepbum et al. 1985) were prepared and transformed using TO eteotroporation (Wé'gel and Glázebrook, 2002}. After effectroporation, 1 ml Peptone Yeast Extract Broth (VER, English Yeast Extract! Peptone) (yeast extract 10 g / l, peptone 10 g / |, and 5 g / L NaCl) was added to the cuvette and the YEP-cell suspension was transferred to a 15 ml culture tube for incubation at 28°C in a constantly shaking water bath for 4 hours. Strained on YEP plus agar (25 g / l) with spectinomphein (200 pg / m!) and streptomycin (250 pg / ml) and these plates were incubated for 2-4 days at 28 C> Separate single colonies into wells they were selected and streaked on fresh YEP* agar plates with e^éc^niMhtaine and streptomycin as described above and incubated at 28°C for 1-3 days. The presence of the genta IRDIG35563 insert in the binary plant transformation vector was determined by PCR analysis using vector-specific primers with template ptasmidic DNA prepared from selected Agmbactewn colonies. Cell pellets from a 4 ml aliquot of a 15 ml overnight culture grown in YEP with spectinomycin and streptomycin as above were extracted using Mini Preps Spin® from Qiagen (Venio, Hamburg, The Netherlands) performed according to the instructions of the maker. Plasmid DNA from the binary vector used in the Agropactenum electroporactan transformation was included as a control, the PCR reaction was completed using Taq DNA polymerase from Invitrogen (Cartsbad, CA) according to the manufacturer's instructions at 0.5X concentrations. PCR reactions were carried out in an MJ Research Peltier Thermocyctor under the following conditions; Step 1) 94 *C for 3 minutes; Stage 2) 94”C for 45 seconds; Step, 3) 55 “C for 30 seconds; Step 4) 72 *0 for 1 minute per kb expected product length' Step 5) 29 times to Step 2; Step 6) 72 Ό for 10 minutes. The reaction was kept at 4 *C after cycling. Amplification products were analyzed by agarose gel electrophoresis (0.7% to 1% w / v agarose by e / empt) and visualized by ethyl bromide staining. . A ketonia whose PCR product was identical to the control plasmid was fecotanated. EXAMPLE 4 Purification of IRPIG35563. Harvested Pf cells containing IRDIG35563 were sonicated in phthisis buffer consisting of 50 mM Tris (pH 8 0), 10% NaC11, ghcerol, and 2 mM EDTA with 50 µl protease buffer cocktail (Sigma -Aldrich. St. Louis. MO) by 25 ml of buffer. The extract was centrifuged at 20,000 x g for 40 minutes. The soluble protein in the supernatant was precipitated with 50% déramohio sulfate and centrifuged at 20,000 x g for: 30 minutes. The pellet was resuspended in 50 mM Tris (pH 8.0) and centrifuged at 20,000 x or for 20 minutes to pellet any mane! soluble. The supernatant containing IR&IG35563 was purified by abionic exchange chromatography using a 5 ml HiTrapwQ HP column with an ANTA Purifier chromatography system (GE Healthcare, UK). The column was equilibrated in 50 mM Tris (pH 8.0) and these 5 proteins were eluted with a stepwise gradient into 1 M NaGJ. Fractions containing proteins were pooled and concentrated using Amicon® Ultra-Centrifuge Filter Devices. 15 with a 30K MWCO (EMD Miliipore, Burlington, MA). The ÍRDÍG35563 protein sample was dialyzed overnight with 50 mM Tris (pH 8.) and the total protein concentrations were measured with the NanoDrop 200QC Spectrophotometer ('ITiermc Scientific, Wattham., MA), using the ASM method. EXAMPLE 5 Effectrophresis in qel. SDS-PAGE analysis was performed using NuP AGE® Novex® 4-12% Bis-Trís Preteíh skins (Thermo Scientific, Waitnam, MA). Proteins were diluted 4X in NuPAGE® LOS sample buffer (Thermo Scientific, Waíthám, MA) containing 100 mM TCEP before loading into it. Ten pL of Noves® Sharp Pro-Stained Protein Standard were loaded into one lane of each. gel. The 15 gal were run in NuPAGE® MES SDS running buffer according to manufacturer's recommendations and stained with SlmplyBlue™ SafeStain (Thermo Science, Walthám, MA), then destained in water and imaged on a glass scanner. flat bed. Fine preparation! of protein showed a single band of migrating protein at an apparent molecular weight of approximately 88 Wa. EXAMPLE 6 Preparation of samples and bioassays. Purified preparations of IRDIG35563 were appropriately diluted in 50 mM Tris, pH 8, and all bioassays contained a control treatment consisting of buffer buffer, which served as a background check for mortality and / or growth inhibition. Protein concentrations in the bioassay buffer were estimated with the NanoOrup 2000C Spectrophotometer (Thermo Setenóla, Wallham, MA), using the A280 method. The purified proteins were tested for their insecticidal activity in bioassays carried out with 1-2 day old neonatal lepidopteran larvae on artificial insect diet. BAW, SAW, FAW, rFÁW, CEW, TBW, SBL, VBC, and CBW larvae hatched from eggs obtained from a colony maintained by a commercial insectary (Benzón Research loc,tCurtiste, PA). rFAW larvae hatched from eggs harvested from owner colonies (Dow AgroSciences LLC, Indianapolis, IN). Bioassays were carried out in 128-well plastic trays specifically designed for insect bioassays (C-U International Ritman, NJ). Each well contained 2.0 ml of multi-speded Lepidoptera diet (Southland Products, Late Village, AR). A 40 pl 35 aliquot of the protein sample was pipetted onto the surface of the 2.0 er diet of each well (20 pi / cm'). Diet concentrations were calculated as the amount {ngj of IRDIG35563 protein per square centimeter (μH) of surface area in the well. Sa used a 9-dose concentration range of 9,000 to 3 ng / cm? with IB larvae tested per dose. The biases: from Hé / femterpa arm / géra used ? different concentrations of purified proteins, with a buffer-only control. Mortality and te arrest were evaluated after 7 days at 25 *0 with 16:8 temperature conditions. The treated trays were kept in a fume hood until liquid on the surface of the diet had evaporated or been absorbed into the diet. Within 24-48 hours of hatching, three individual larvae were picked up with a moistened camel's hair brush and deposited on the treated diet, one larva per well. Infested wells were then sealed with clear plastic cling sheets and vented to allow gas exchange (C-0 International, Ritman. NJj. Bioassay trays were maintained under controlled environmental conditions (28'C, -60% relative humidity, 16:8 íLuzíQsourldad]) for 5 days, after which the total number of insects exposed to each protein sample, the number of dead insects, and the weight of surviving insects were recorded. The Glsc was determined to be the concentration of IRDIG35563 protein in the diet in which the Gl value was 50%. The 60% lethal concentration (LCss) was recorded as the concentration of IRDIG35563 protein in the diet in which 50% of the insects were killed. Growth inhibition-concentration response curves were determined using a 3-parameter non-linear logistic using JMP Pro software, version 9.0.3 (SAS Instituí© lnc„ Cary, N€). The lethal concentration response curve was analyzed by .Probit analysis (Finney. 1971) of the mortality data and carried out using POLO-PC (LeGra Software). Table 2 shows the effectiveness of IROIG35563 against multiple insect species tested in an artificial diet overlay-(ng / Cms) bioassay. Table 2 dyad insect ............................. N % mortality (3000 ng / crn2) ~ ΐδο I Practical mortality (3000 ngtem2 ) t....................... 100.0.................. ....... C8W 16 100.0 100.0 CEW 46 21.7 J 65.2 ECB 16 6.3 J 12.5 FAW 32 93.8 ¡ 100 rFAW (resistant to Cry1F) 32 87.5 i 100 —— | 100.0 SAW 32 100.0 SSL ..................... 32 16 40.6 37A 1 50.0 j 50.0 ~~~~~~ 100.0 vsc EXAMPLE ? Production of insecticidal proteins IRDIG35563 and variants in dicotyledonous plants. Transformation into Arabidapsis. Arabnlapsis thahana Col-01 was transformed using the thyural immersion method (Weigei and Glazebíwk. 2002). The selected Agrobacíenum colony was used to inoculate 1 to 16 ml of the YEP broth culture containing appropriate antibiotics for selection. The culture was incubated overnight at 28 ®C with constant shaking at 220 rpm. Each: culture: was used to inoculate two caves of 500 ml of VER broth that contained appropriate antibiotics for the selection and the new ones: culture® were incubated at 28 ”C with constant agitation. Cells were pelleted at approximately 8700 x g for 10 minutes at room temperature and the resulting supernatant discarded. The cell pellet was carefully resuspended in 580 ml infiltration medium containing: 1^x Murashige and Skoog salts (Sygma-Aldrich) Gamherg Mamines 85 (Gdd BioTechnology, St Loeis, MOL 10 % sucrose (w / y ), 0.044 pM benclaminopurine (10 pi / l of 1 mg / ml stock solution in DMSü) v Silwet L-77 300 pW Plants of approximately 1 month of age were immersed in the medium for 15 seconds, taking care to ensure Dipping the newest inflorescence Plants are left on their sides and covered (transparent or opaque) for 24 hours, washed with water and placed face up Plants are grown at 22°C with a photoperiod Darkness 16:8 Approximately 4 weeks after submergence the seeds were collected. Arab / dapsM growth and selection Freshly harvested TI seed was allowed to dry for at least 7 days at room temperature in the presence of desiccant. The seed was suspended in a 0.1% agar / water solution (Sigma.Aidnoh) and then stratified at 4°C for 2 days. To prepare for planting, Sunshine Mix LP5 (Sun Gro Horticulture lnc.:>Béllevué, WA) in 26.6 cm x 53.3 cm 00.5 in x 21 in germination trays (T O. Plástic® inc,, Cleanváter , MM) was covered with fine vermioulite, sub-imged with Hoagland's solution (Hoagland and Arnon, 1950) until wet, then allowed to drain for 24 hours. The stratified seed was planted in the vermiculite and covered with humidity domes (KORD Products, Ramstea, Ontario, Canada) for 7 days. Seeds were germinated and plants were grown in a Gonviron (Models GMP4030 OCMP3244: Controlfed Environments Limited, Winnipeg. Manitoba, Canada) under long day conditions (photoperiod 16:8 light.dark) at a: fez intensity of 128 -150 pmal / mte at constant temperature (22 *C) and humidity (40-50%). The plants were initially irrigated with Hoagland's solution and subsequently irrigated with deionized water to keep the soil moist but not wet. The domes were removed 5-5 days after sowing and the plants were sprayed with a chemical setting agent to remove untransformed seed germinates. For example, if the plant-expressible detectable marker gene provided by the paired plant-transformation dn vector is a pair or bar gene (Wehrmann et al, 1906), transformed plants can be selected by spraying with Finate WOQX solution ( 6.78% glufosinate ammonium, Faroam Companies Inc., Phoenix, AZ.), Two subsequent sprays will be made at 5-7 day intervals. Survivors (actively growing plants) were identified 7-10 days after the final spray and transplanted into pots prepared with Sunshme Mix LP5. Transplanted plants were covered with a moisture dome for 3-4 days and placed in a Conviran: under the conditions of creeimtentq mentioned above.. Those skilled in the art of transformation in dicotyledonous plants will understand that other methods of selection for transformed plants are available when using other selectable marker genes expressed in plants (eg, herbicide tolerance genes). Table 3 shows the results (mean score (SEM)) of the TI bioassay of Arabidopsis against S GEW-i FAW, SAW, TBW and SBL. Five events were generated for each corislTUOtion and S® recorded the average leaf damage score (5 leaf punches / event, 5 days after infestation) 5 weeks after germination. The construction design and numbering are reported in Table 4. Table 3 Protein Construction CEW FAW SAW TBW SBL pDABI34633 0.46 (9.22) 0.42(0.19) | 0.35(0.15) 0.45 (0.21) 0.40(0.19) IRDIG35563 pDABI 34634 0.1 (0) 0.1 (0) i 0.1 (0) 0.11 (0.01) 0.1 (0) pDA8134635 0.1 (0) 0.1(0) i 0.1( 0) 0.30 (0.03) 0.1 (0) PDAB134636 0.1 (0) 0.1 (0) i 0.1 (0) 0.11 (0.01) 0.1 (0) Vip3Ab1 Control pos 0.11 (0.01) 0.1(0) | 074(0.06) 0.1 (0) 0.1 (0) Coi-0 Control neg 1 (0) 0.62 {0.07) i 0.61(0.06) 0.93 (0.04) 0.95 (0.03) Table 4 i Agro Vector with AtUbilO :: IRD1G35563.2 :: AtUbí W + 2C21 + CsVMV :: DSM2 :: pDA8134633 i i Orfl ' pD^rÜ634T Agre Ven cen ^Agra Vector with GmCAB ........ pDABI 34636 l prfl ; —....... ·.-..-----------------———-—--------------- --—- —— -——-———---------------—— EdAMPLE.6 Ten to 20 To transagenic &y&fi& plants harboring the expression vectors for these nucleic acids comprising SRDIG35563 are generated, for example, by Agmbactem / m-mediated transformation. Maxi mature soybeans (G / ycme) are sterilized overnight with chlorine gas for sixteen hours. After chlorine gas sterilization, the seeds are placed in an open container in a LAMINARA flow hood to dissipate the chlorine gas. The sterilized seeds are then inhibited with HsO for at least sixteen hours in the dark using a black box at 24 *C. Preparation of split soybeans. The split soybean protocol comprising a portion of an embryonic axis requires the preparation of soybean material that is cut lengthwise, using a #10 cpchilia attached to a scalpel, along the seed string to separate and to remove ia seed coat, and to divide ia hemife into two cotyledon sections. Careful attention is paid to parotelmerte the embryonic axis, where approximately 1 / 2 -1 / 3 of the embryonic axis remains attached to the nodal end of the couledor. inoculation . Divided sacs comprising a partial portion of the embonic sage are then immersed for about 30 minutes in a solution of Agrobactemjm iu / nefaciens (eg strain EHA 101 or EHA 105) containing binary plasmids comprising IRDIG35563. The Agrobacterium tuméfacfees solution is diluted to a final concentration of λ=δ.6 DOsse before immersing the cotyledons that comprise the embryonic axis. üo-cultiye. After incubation, split soybean semi-life is allowed to co-cultivate with the Agmbacterium fume / actens strain for 5 days in Mang, Kan co-cultivation medium. Agrobactento Profoeofe. 2.1. Roe Jersey: Humana Press» 2006, Print.) in a Petri dish covered with a piece of filter paper. shoot induction. After 5 days of co-culture, the split soybeans are washed in liquid Shoot induction (SL) medium consisting of B5 salts: B5 vitamins, Ferrous 28 mg / l, NazEOTA 33 mg / l , sucrose 30 gd, MES 0.6 g / l, BAP 1.11 mg / l, ΤΙΜΕΝΤΙΝΪ?Λ100 mg / l, cefotexime 200 mg / l and vancomlcin 50 mg4 (pH 5.7). The divided soybean seeds are then grown in sprout induction medium I (SI i) consisting of B5 salts, vitamins 85, Nobte agar 7 g / |, Ferrous 2§ mg / l, Na?EDTA 38 sucrose 30 g / i, MES 0.6 g / L BAP i .11 mg / l, TIMENTiN^ 50 mg / l, cefotaxim 200 mg / l, vancomyclna 50 mg / l (pH 5.7b with the flat side of the cotifedon up and the nodal end of the cotyledon embedded in the medium After 2 weeks of culture, the expiateles of the transformed split soybean are transferred to sprout induction medium II (Si II) containing medium SI I supplemented with glufosilate 6 mg / l (LIBERTY ®), Shoot elongation. After 2 weeks of culture in Si II medium, the cotyledons are removed from the buds and a flush bud pad containing the embryonic axes is excised by making a cut at the base of the cotyledon. Shoot aimohadilia isolated from the cotyledon is transferred to Shoot Elongation (SE) medium. SE medium consists of MS salts, Ferrous 28 mg / l, Na^ mg / l. sucrose 30 g / LyMES0.6g / l, asparagine SO mgd, L~ ptroglutafnic acid 160 mg / l. IAA 0.1 mg / l, GA3 0.5 mg / L, zeatine riboside 1 mg / L, TIMENTIN™ 50 mg / L, Cefotaxime 200 mg / L, Vancomycin 50 mg / L, Glufosinate 6 mg / L, Noble Agar 7 g / |, (pH 5.7). Cultures are transferred to fresh SE medium every 2 weeks. Cultures are grown in a COWIRONwa growth chamber at 24 *C with a photoperiod of 18 h at a light intensity of 80-90 pmoi / m^. entertainment The elongate shoots that developed from the cotyledon shoot aimohadilia are isolated by cutting the elongate shoot at the base of the cotyledon bud pad and immersing the elongate shoot in IBA (indoi 3-butyric acid) 1 mg / l for 1-3 minutes to promote rooting, then the elongated shoots are transferred to rooting medium (MS salts, vitamins B5rFerrous 20 mg / l, NazEDTA 38 mg / l, sucrose 20 gd and MES 0.59 g / l , asparaginq 50 mg / l, l.-p«ogfulamic acid 100 mg / l, Noble agar 7 g / l, pH 5.6) in phyla trays. Crop. After cultivation in a CONVIRONnia 24 C growth chamber, 18 h photoperiod. For 1-2 weeks, shoots that have developed roots are transferred to a soil mix in a covered ice cream cup and placed in a CONViRQN™ growth chamber (models CMP4030 and CMF3244, Controlled Environments Limited, Winnipeg, Manitoba, Canada). in oondictonee 5 long day (16 hours of light / 8 hours of darkness) at a light intensity of 120-150 pmoi / mfo at constant temperature (22 *C) and humidity: 40--50%) for acclimatization of the seedlings. Rooted seedlings are hardened in ice cream sundaes for several weeks before they are transferred to the greenhouse for further hardening and breeding of robust transgenic soybean plants. The development and morphological characteristics of the three transgenic lines are compared with 10 non-transformed plants. Root, shoot, foliage and reproductive characteristics of plants are compared, i. The characteristics of the brete delas plates such as height, numbers and sizes of leaves, time of flowering, size time! and appearance are recorded. In general, there are no observable morphological differences between transgenic lines and those without the expression of DIG proteins when grown in wiro and in soil in the greenhouse. EXAMPLE 9 ^tognsaygs.TO· Five duck soybean events were generated each coóStruGcióri and the average foliar damage rate (5 leaf punches / event, 5 days after infestation) was recorded 5 weeks after germination. The construction and numbering are reported in Table 4. Table 5 shows the results of the soybean TO bioassay against CEW, FAW, SAW, TBW and SBL. The fodder damage grading scale uses a scoring system from 1 to 9 with 1 representing 88-100% damage. Deregulated transgenic soybean, Conkesta, was used as a positive control. A non-transgenic soybean line was used as a negative control. The results for those events for which the protein was objectionable are presented in Table 5. Other test events produced inconsistent results, thought to be due to environmental conditions experienced during transport. Table 6 presents the scale of damage represented in Table 5. Table 5 Event Characteristic (RE) BCW CBW CEW SBL η··*............ TBW VBC FAW SAW Negative control Negative 1 3 1 Ϊ 1 1 1 1 Negative control Negative 1 5 1 : 1 1 1 1 1 Negative Control Negative 1 5 Ϊ 1 5 2 1 1 Negative Control Negative 1 9 1 1 3 l 1 2 Positive Control Pcsrtiva 1 to 8 9 7 9 1 9 9 Positive Control Positive 1 9 9 9 8 9 9 9 Positive Control Pcsihva 3 9 9 9 8 9 9 9 Positive Control Postova 3 9 9 9 9 9 1 9 9 134635(8)-254 AlActte 7 9 7 9 9 9 1 9 134833(9)-209 AtUbrtO 8 to 9 9 8 9 9 9 es 134633(10)-224 TW33(W'j-¿'l2 L 8 Ί 5 I 7 9 9 I 9 I 4 8 t § I 8 | 8 9 | 6.2 I 9 : 5 8 Table 6 Damage scale Percentage of damage 9 0 8 12.5 7 25 δ. 2 35 5 50 4 62.5 3 75 ______ 1 100 EXAMPLE 10 IRQ production IG35563 Ag / Obacterium-mediated transformation of maize. Seeds of the Higo Ti or B-104 Fi cross (Armstrong et al. 1991) were planted in 18.9 liter (5 gallon) jars containing a mixture of Métro-Mix 360 ai 95% soilless growing medium (Sun Gro Horticulture , Béllevue, WA) and 5% clay / manga soil. Plants were grown in a greenhouse using a combination of high pressure metal halide and sodium lamps with a 16 8 h photoperiod in light-darkness. To obtain Fa Immature embryos for transformation, controlled suh-pcfeizactones were performed. Immature embryos were isolated 8-10 days post-pollination when the embryos were approximately 1.0 to 2.0 mm in size, Infection and infection The surface of corn ears was sterilized by rubbing with liquid soap, immersing in 70% ethanol for 2 minutes, and then immersing in 20% commercial tissue (6.1% sodium hypoctene) for 30 minutes before rinsing. with sterile water. A suspension of Agrobactenum cells containing a superbinary vector was prepared by transferring 1-2 loops of bacteria grown in solid YEP medium containing 100 mg specimomycin, 10 mL tetracycline, and 250 mg / i streptomycin at 28'C for 2-3 days in 5 days. ml of liquid infection medium (Measure Basa! LS (Linsmaler and Skó&g, 1965). Vitamins Νδ (Chu at al., 1975}, 2,4-didorophenoxyacetic acid (2.44)) 1.5 mg / l, sucrose 63, 5 g, glucose 36.0 g / l, L-proim 6 mM < pH 5.2) containing 100 µM acetosyringone. The solution was vertexed until a uniform suspension was achieved and the concentration adjusted to a final density of approximately 200 Kiett units, using a Ktett-Summerson colorimeter with a purple filter, or an optical density ds approximately 0.4 at 550 nm. The immature embryos were isolated directly in a microcentrifuge tube containing 2 ml of the infection medium. The medium was removed and replaced by 1 ml of the AgrGbaaf&mim solution with a density of 200 Kletf units and Ag.mtoaeteffÍW splution and incubated for 5 minutes at room temperature and then transferred to the culture medium (Medium Basai LS (containing vitamins N6< 2,4-D 1.5 mg / l, sucrose 30.0 g / ζ L-proline 6 mM< AgNOa 0.85 mg / l, acetosyrmgone 100 pM and gamma galana 3.0 g / l {PhyteJechnotegy Laboratories.. Lenexa, KS), pH 5.8) for 5 days at 25°C in the dark. After culture, the embryos were transferred to selective medium whereupon transformed Oslados were obtained over the course of approximately 8 weeks. For the selection of maize tissues transformed with a superbinary plasmid containing a plant-expressible paf or bar marker gene, an LS-based medium was used (LS basal medium, with IX vitamins N6,2,4-D 1,5 mg / l, MES (2-(N~mórfólÍrto)efanosui^ acid^ monohydrate; T^ytoTechnotogy Laboratories., Lenexa, KS) 0.5 g / í, sucrose 30.0 g / ί, L-jxüSna 6 mM, AgNOa 1 0 mg / l, cefotaxime 250 mg / l, gallant gum 2.5 g / l, pH 5.7) with Bialatós (Gold BioTechnoíogy. SI. Louss, MO). Embryos were transferred to selection media containing 3 mg / l Bialatós until embryogamous isolates were obtained. Recovered isolates were pooled by transferring them to fresh selection medium at 2-week intervals for regeneration and additional analysis. Those skilled in the art of maize transformation will understand that other methods of selecting transformed plants are available when using other selectable marker genes. expressed in plants (for example, herbicide tolerance genes). Three IRDIG35563 constructs contained in plasmids pDAB134672, pDAS 134673 and pDAB 134674 were transformed into maize (Table 7). TO plants were regenerated and tested for their ability to control target ihsect pests. Table 7 plasmid; Description: pDAS134672 ZmUbH:4RD!G35563.3-S(Pinll. ZCi8. ZmUtel-AAD 1-ZmLip pDAB134673 ZmCAB-ÍRDiG35563.3-StPinll, ZC18, ZmUbil-AADI-ZmUp pDABI 34674 OsUbi1-IRDIG35563.3-O1sUbil , Zm Ubi 1-AAD 1-ZmLip A leaf section of 6.4 X 3.22 square centimeters (10 X 0.5 inch flat) was taken in duplicate from the V3 or V4 leaf of transgenic V5 Ts plants. For each test, leaf tissues from the wild-type plant were sampled to avoid cross-contamination by Bt toxins at leaf edges, followed by transformed plants. In each bioassay tray well (32-well trays and lids, CD International, Pitman, NJ), i leaf cutting was placed on 2% water^agar (Flsher Scientific, Fair Lawn, NJ) and this was replicated 2 times. by Insect species, by event and by construction. Each well was infested with ten FAW hatchlings (24-48 h of age) and sealed with a perforated plastic lid to allow air exchange. The trays were placed at 285C (18:8 h light.dark. 40% RH) and after 3 days graded for percentage leaf damage. The leaf damage data in percentage were analyzed with ANOVA and mean separations with the Tukéy-Kramer test when the variations were homogeneous using Pro 9.8.1 (2019 SAS Institute Inc.. Cáry, NC). The results of foliar damage by FAW in maize TO <¿s expresses IDIG35563 are presented in Table 8. Boards, j Construction i Events Mean (Dafid average) Standard error I pDABt 34672 1 11 36.3 14.8 1 pDA8t34673 | 25 58 6.08 pDAB134674 17 8.48 5.38 ¡ BW4 i 9 99.2 0.59 § Hercuiex 9 22.2 4.65 EXAMPLE 11 For regeneration, cultures were transferred to induction medium 28 (MS salts and vitamins, 30 gfi sucrose, 0.25 mg / l benzyaminopurlna 5 mg / 1,2,4-0, 3 mgfi Bialaphos, 25Q mg / 1 cefotaxim , gum galana 2.5 g.'L pH 5J) for 1 week under low light conditions (14 pEm^r1) then 1 week under high light conditions (approximately 89 pEm^r1). Tissues are subsequently transferred to 36'* regeneration medium (same as ihduWsn medium except lacking plant growth regulators). Seedlings 3-5 em in length are transferred to glass culture tubes containing SHGA medium (Schenk and Hildebrandf salts and vitamins (1972); PóyfaWihnoíagy^^ Lenexá. KS)« m / o-inosíioí 1.0 g / l , 10 g / l sucrose and 2.0 g / l gum gallan, pH 5.8) to allow further growth and development of shoots and roots. Plants are transplanted into the same soil mix as described above and grow to flower in the greenhouse Controlled pollination is carried out for the production of seeds, EXAMPLE 12 Design of a version opumízáda for plants of the coding sequence for IRDIQ^fg, A sequence of DNA that biases of cedon of plants was designed and synthesized to produce the protein IRD1G35583 in transgenic monocotyledonous and dicotyledonous plants. A codon usage table for maize (Zea maya L.) was calculated from 705 protein coding sequences (CDs) obtained from sequences deposited in GenBank, Codon usage tables for tobacco (Nícotíam tebacwh 1268 CD), canola (Drass / ca napas, 530 CD), cotton {Gossypftan h / rsuium, 197 CD) and soybean (Glyetob max; ca. 1000 CD) were downloaded from the data on the web sylph nttp7Aww.kaxusa,cr,jp / eodpn / , A set of skewed endons comprising highly used camouflage ndecodons for both maize and dicot datasets, in appropriate average weighted relative amounts, was calculated after omitting any redundant ncdons used in less than about 10% of total codon usages. for that amino acid in any type of plant. To derive a plant-optimized sequence encoding the IRDIG35563 protein, codon substitutions were made to the experimentally determined IRDIG35563 DNA sequence such that the resulting DNA sequence had the overall codon composition from the Codon Optimized Traits table. for plants. Additional refinements to the sequence were made to eliminate undesirable restriction enzyme recognition sites, potential plant intron splice sites, long A / T or C / G subtraction runs, and other reasons that could interfere with stability. , RNA transcription and translation of the coding region in plant cells. Other changes were made to introduce the desired restriction enzyme recognition sites and to remove long internal open reading frames (frames other than +1 ). < These changes were all carried out with the constraints of retaining the biased codon composition of plants. Synthesis of the designed sequence was performed by a commercial vendor (DNA2A Monte Park. CA). Additional guidance regarding the production of synthetic genes can be found, for example, in WQ 97 / 13402 and US Patent ia .n? 0380831. A maize optimized high GC AON sequence encoding lRD1G358S3 is given in SEQ ID NO:3. An optimized DNA sequence for dlcptífedonas encoding full-length IRD1G35563 is disclosed in SEQ 10 NO:4. Hybridization of AON immobilized on Southern blots with radioactively labeled gene-specific probes can be performed by standard methods (Sambrook et al., sapra ). Radioactive isotopes used to label pciinucleotide probes can include 32P, 38P, 14C, or 3H. Incorporation of radioactive isotopes into hairy nucleotide probe molecules can be accomplished by any of a number of methods well known to those skilled in the field of m&t biology (see, for e / emp / o. Samhrook eta / ., supra.); In general, hybridization and subsequent washes can be carried out under stringent conditions that allow detection of target sequences with homology to the claimed toxin-encoding genes. For these double-stranded DNA panic probes. hybridization can be carried out overnight at 20X to 25X below hybrid DNA Tmdd in 6X SSPE, 5X Denhardt SDS ai 01% solution, 0.1 mg / ml skimmed DNA (20X SSPE is 3M NaCl, 0.2 M NaHPQx and 0.02 M EDTA (sodium salt of etitenediamine ptetraacetic acid), tOOX Denhardt's solution is Pqlivinylpyrrolidone 20 g / l, Rcoll type 400 20 g / l Rcoll and 8SA 20 g / l (fraction V)]. Washes can typically be carried out as follows: to. Twice at room temperature for 15 minutes in IX SSPE, 0.1% SDS (low stringency wash). b. Once at 20X below da temperature Tm for 15 min in 0.2X SSPE, 0.1% SOS (moderate stringency wash). For oligonucleotide probes, hybridization can be carried out overnight at 10*C to 20*C below hybrid T® in EX SSPE, &X Denhardi's solution, 0.1% SDS, 0.1 mg / ml denatured DNA . The T>» era for cligonucleotide probes can be determined by the following formula (Suggs et al., 1981), 'T^C) “ 2(number of base pairs T / A) + 4 (number of base pairs G / C ) Washes can typically be carried out as argue: either. Tw» times at room temperature for 15 minutes IX SSPE, SDS ai 0.1 (low stringency wash), d. Once at hybridization temperature for TS minutes in i X SSPE, 0.1% SDS ai (moderate stringency wash). Probe molecules for hybridization and hybrid molecules formed between probes and target molecules can be rendered objectionable by means other than labeling / radioactive. Such alternative methods claim to be within! scope of this invention, EXAMPLE 13 Transformation of additional crop species; Cotton is transformed with IRDIG35563 (with or without a chloroplast transit peptide) to provide control of insect pests using a method known to those skilled in the art, substantially the same techniques previously described in Example 14 of the US Patent USA, 7..838,733 © e| Example 12 of International Patent Publication NT WQ 2007 / 053482., Although the present disclosure may be susceptible to various modifications and alternative forms, specific embodiments have been described by way of example in detail herein. However, it should be understood that this disclosure is not intended to be limited to the particular forms disclosed. Rather, the present disclosure is intended to cover all modifications, equivalents, and alternatives that fall within! scope of the present disclosure as defined by the following appended claims and their legal equivalents. bibltoaraphy Beliz, GA, Jacobs, K. A,, Eickbush, T. H., Cberbas, P. T, Kafatos, F. C, (1983) isolation of multigene families and determination of homologies by filter hybridization methods, In Wu, RL, Groseman, L, Mokievé. K. (eds.) Methods of Enzymology, Voi. 1.00 Academic Press, New York pp, 266*285, Crickmpre, N., Baum, J., Bravo, A,, Leredua, D- Narva, K,, Ssmpson, K., Schnepf, E„ Sun, M, and Zeigler, D.R. Sscflilts fhumgiensis.tokin nomenclature' (2Q16) http: / / www.bto Huang, F,^ Rógers, L. B.< Rhett, G. H< (2006) Comparative susceptibility of European coro borer, southwestern com borer, and sugarcane borer (Lepidoptera: Crambidae) te Cryl Ab protein in a commsroial hybrid, J. Econ. EntomoL 99:194-202, Lee, eff. al, (2003) The Mode of Action of the £aq$us ihuringiensfa Vegetative Insecticide! Proteio VípSÁ Differsfrom That af Cryf Ab 5«Endotoxin. App! Foviron, Microbe!. yol. 69 #8 4648-4657 Sambrook, J„ Fritsch, E. F,. Manistis, T. (1989) Mototer Cfentog: A Laboratory Manda / (2nd ed„ Cold Spring Harbor Laboratory Press, Pteinview, N.V.) Tijssen, P. (1993) Laboratory Technique© in Btochemistry and Molecular Bioiogy Hybridization with Nudefe Asid Probas, Part i. Chapter 2. P, C. van der Vlset (ed.), (Elsevter, N.Y.) Wbng, Kan, Agrdhactemm Prafoso / s. 2. 1. New Jersey: Humana Press, 2006. Print Weigel, D., Glazebrook, J. (eds.) (2002) Arabídaps / s: A Laboratory Manual Ccld Spring Harbor Press, Cpld Spring Harbor, NY, 354 pages. Yu, C. G„ Mullins, M.A., Warren, G.W., Kozie!, M.G. Y Estruch, J. J. 0S97) The Badilas thuririgfensis vegelahve insecticide! protein Vip3A íyses rnidgut epitheüum celis of susceptible insect. Appi, Environ. Miei'obiol.. February 1897; 63:2 532-6,

Claims

Claims:

1. A recombinant nucleic acid construct comprising one or more heterogeneous regulatory elements that direct the expression of a nucleic acid sequence encoding a polypeptide having at least 95% sequence identity with the polypeptide sequence of the SEQ ID NO:

2.

2. The construction of claim 1 wherein the nucleic acid sequence is chosen from the group consisting of SEQ ID NO:1, SEQ ID NO:3 and SEQ ID NO:

4.

3. An insecticidal chimeric toxin comprising residues 1 to 789 of SEQ ID NQ;2. W 4. An insecticidal chimeric toxin of claim 3 consisting of ia SEQ ID ND:2 5. A plant or part of a plant comprising a nucleic acid construct of claim 1.

6. A plant or part of a plant comprising a nucleic acid construct of claim 2. 15 7. The plant part of claim 5 wherein the plant is a seed, 8. The plant part of claim 6 wherein the plant is a seed 9. The plant or part of the plant of claim 5, wherein the nucleic acid construct encodes a chimeric toxin having insecticidal activity against one or more selected insects of Spodeptera exigua (gardama, BAW), Spodeptera meridional. SAW), 20 Spodoptera frugíperda (fruit tree cutter, FAW), Spodoptera frugíperda resistencia (fruit tree cutter, FAW), Wfccvtepa zea (corn worm, C'EW^ Rseudop / uste wtoderíá (soybean looper, SSL), Anífcarsra gemmafafe (bean caterpillar, VBQ), EeSathls virescens (tobacco caterpillar, TBW) and He / fcowpa armígera (cotton caterpillar, C8W).

16. A plant or part of a plant of claim 6 wherein the nucleic acid construct 25 encodes a chimeric toxin having insecticidal activity against one or more insects selected from Spodoptera exigua (planthopper, SAW), Spodoptera eridanra (southern bean worm, SAW), Spodoptera fragíperda (corn weevil, FAW), resistant Spodopfem (corn weevil.rFAW), / -lefieaveipa zea (corn worm, CEW), Pseudopiusía mz / udens (soybean looper, SBL). Anjeareis gemmaíafc (legume caterpillar, VBC), Heliotñis Wssrws (tobacco worm, 30 TBW) and Htfíeov&rpa armígera (cotton caterpillar, CBW i.

11. A method for controlling susceptible insects comprising bringing the insect into contact with an effective amount of a toxin of claim 3.

12. The method of claim 11 wherein the toxin is SEQ ID NO:

2.

13. A method for controlling an insect pest population comprising bringing said pest population into contact with an insecticidal amount of a toxin of claim 3. <4, The method of claim 13 wherein the insect pest population is selected from Spodoptera mergu® (planthopper, BAW), Spodoptera mergu® (southern corn earworm, SAW), Spodoptera frtigipeda (corn borer, FAW), Spodoptera frtigipeda resistant to CrylF, Heliceovea zea (corn borer, CEW), Pseudomonas arborvitae (stalk looper, SBL), and Amphicarsia gemmaiis (bean caterpillar, VBC).H&ÍÍQthis vir&s&efís (tobacco worm, TBW) and Heiícovsspa armígera (cotton caterpillar, CBW), 5 15, A method for producing an insect-resistant or insect-tolerant plant comprising crossing a non-transgenic plant with a transgenic plant comprising a construct of claim 1 stably incorporated into the plant genome and selecting the progeny containing the DNA construct of claim 1.