Title - ISOLATED CRY1B VARIANT POLYPEPTIDE MOLECULE, POLYNUCLEOTIDE ENCODING IT, MODIFIED BACTERIAL CELL COMPRISING IT, DNA CONSTRUCT FOR ITS EXPRESSION, AND METHOD COMPRISING IT

Abstract

Nucleic acids and variants and fragments thereof, obtained from Bacillus thuringiensis strains that encode variant polypeptides with enhanced pesticidal activity against insect pests, including Lepidoptera and Coleoptera. The specific formulations provide isolated nucleic acids encoding pesticidal proteins, pesticidal compounds, DNA constructs, and transformed microorganisms and plants comprising a nucleic acid of the formulations. These formulations are useful in methods for controlling pests, especially plant pests.

Description

INSECTICIDAL POLYPEPTIDES HAVING AN IMPROVED SPECTRUM OF ACTIVITY AND THEIR USES REFERENCE TO ELECTRONICALLY SUBMITTED SEQUENCE LISTING A sequence listing having the file name “5409WOPCT_SequenceListing.txt” created on Thursday, September 24, 2015 and having a size of 267 kilobytes is archived in machine readable format together with the specification. The sequence listing is part of the specification and is incorporated herein by reference in its entirety. FIELD The present disclosure relates to recombinant nucleic acids encoding pesticidal polypeptides having insecticidal activity against earworm and / or armyworm and / or an improved spectrum of pesticidal activity against insect pests. The compositions and methods of the disclosure use the disclosed nucleic acids and their encoded pesticidal polypeptides to control pests in plants. BACKGROUND OF THE INVENTION Insect pests are one of the main factors in the loss of crops in world agriculture. For example, military caterpillar feeding, tracer worm damage, or European corn borer damage can be economically devastating to agricultural producers. Insect pest-related crop loss from European corn borer attacks on field and sweet corn alone has reached approximately $1 billion per year in damage and control costs. Traditionally, the primary method of affecting insect pest populations has been the application of broad-spectrum chemical insecticides. However, consumers, as well as government regulators alike, are increasingly concerned about the environmental risks associated with the production and use of synthetic chemical pesticides. Because of these concerns, regulators have banned or limited the use of some of the most dangerous pesticides. Thus, there is substantial interest in the development of alternative pesticides. Biological control of agriculturally important insect pests with the use of a microbial agent, such as fungi, bacteria, or other insect species, provides an ecologically and commercially attractive alternative to synthetic chemical pesticides. Generally speaking, the use of biopesticides presents a lower risk of contamination and environmental hazards, and biopesticides provide greater target specificity than is characteristic of traditional broad-spectrum chemical insecticides. In addition, biopesticides often cost less to produce and thus improve the economic performance of a wide variety of crops. Certain species of microorganisms of the genus Bacillus are known to have pesticidal activity against a wide variety of insect pests including Lepidoptera, Diptera, Coleoptera, Hemiptera, and others. Bacillus thuringiensis (Bt) and Bacillus papilliae are among the most successful biocontrol agents discovered to date. Insect pathogenicity has also been attributed to strains of B. larvae, B. lentimorbus, B. sphaericus (Harwook, ed., ((1989) B Bacillus (Plenum Press), 306), and B. cereus ( Patent No. WO 96 / 10083).Pesticidal activity appears to be concentrated in parasporal crystal protein inclusions, although pesticidal proteins have additionally been isolated from the vegetative growth stage of Bacillus.Several genes encoding have been isolated and characterized these pesticidal proteins (see, for example, US Patent Nos. 5,366,892 and 5,840,868). Microbial insecticides, particularly those derived from Bacillus strains, have played an important role in agriculture as alternatives to chemical pest control. Agricultural scientists have recently developed crop plants with improved resistance to insects, through genetic engineering, to produce pesticidal proteins from Bacillus. For example, maize and cotton plants have been genetically engineered to produce pesticidal proteins isolated from Bt strains (see, e.g., Aronson (2002) Ce / / Mol. Life Sci. 59(3): 417-425, Schnepf et al (1998) Microbiol Mol Biol Rev. 62(3):775806). These genetically engineered crops are widely used in American agriculture and have provided the farmer with an environmentally friendly alternative to traditional insect control methods. In addition, potatoes that have been genetically engineered to contain Cry pesticide toxins have been sold to the US farmer. Although they proved to be very successful commercially, these insect resistant, genetically modified crop plants provide resistance to only a limited variety of economically important insect pests. Consequently, there remains a need for new Bt toxins with an improved spectrum of insecticidal activity against insect pests, e.g. eg, toxins with enhanced activity against insects of the order Lepidoptera and / or Coleoptera. Furthermore, there remains a need for biopesticides with activity against various insect pests and biopesticides with improved insecticidal activity. SUMMARY OF THE INVENTION Compositions and methods for affecting insect pests are provided. More specifically, the embodiments of the present disclosure relate to methods of infecting insects that use nucleotide sequences encoding insecticidal peptides to produce transformed microorganisms and plants expressing an insecticidal polypeptide of the embodiments. In some embodiments, the nucleotide sequences encode polypeptides that are pesticidal to at least one insect belonging to the order Lepidoptera. In some aspects, nucleic acid molecules and fragments and variants thereof are provided which encode polypeptides having pesticidal activity against insect pests (eg, sec. id. no.: 4, sec. no. of ¡dent: 6, section with ident: 8, section with ident: 10, section with ident: 12, section with ¡no dent: 14, sec with ident no: 16, sec with ident no: 18, sec with ident no: 20, sec with ident no. : 22, section with id no.: 24, section with ident no.: 26, section with ident no.: 28, section with ident no.: 30, sec. with ident no.: 32, section with ident no.: 34, section with ident no.: 36, section with ident no.. 38, section with ident no. : 40, SEQ ID NO: 42, SEQ ID NO: 44, and SEQ ID NO: 46, and encoding the polypeptide of SEQ ID NO: .: 3, section with ident no.: 5, section with ident no.: 7, section with ident no.: 9, section with ident no. : 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 23, sec. with no. of ident.: 25, sec. with no. from ident: 27, sec. with no. of ident.: 29, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. of ident.: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with num. of ident.: 45, respectively). The wild-type (eg, naturally occurring) nucleotide sequence of the embodiments derived from Bt encodes an insecticidal peptide. The embodiments further provide fragments and variants of the disclosed nucleotide sequence that encode biologically active (eg, insecticidal) polypeptides. In another aspect, variant Cry1 B polypeptides are provided, encoded by a modified (eg, mutagenized or engineered) nucleic acid molecule of the embodiments. In specific examples, pesticidal proteins of the modalities include protein fragments and full-length polypeptides produced from mutagenized nucleic acids designed to introduce particular amino acid sequences into the polypeptides of the modalities. In particular embodiments, the polypeptides have enhanced pesticidal activity relative to the activity of the naturally occurring polypeptide from which they are derived. In another embodiment, the nucleic acids of the embodiments can be further used to produce transgenic (eg, transformed) monocot or dicot plants characterized by genomes comprising at least one stably incorporated nucleotide construct comprising a coding sequence for the embodiments operably linked to a promoter that drives expression of the encoded pesticidal polypeptide. Accordingly, transformed plant cells, plant tissues, plants, and seeds thereof are further provided. In another aspect, a transformed plant can be produced using a nucleic acid that has been optimized for higher expression in a host plant. For example, one of the pesticidal polypeptides of the embodiments can be reverse translated to produce a nucleic acid comprising codons optimized for expression in a ί i I ί j particular host, for example, a crop plant such as a maize plant (Zea mays). Expression of a coding sequence by said transformed plant (eg, dicot or monocot) will produce a pesticidal polypeptide and confer give the plant greater resistance against insects Some embodiments provide transgenic plants that express pesticidal polypeptides useful in methods intended to affect various insect pests. In another aspect, pesticidal or insecticidal compositions containing the variant Cry1B polypeptides of the embodiments are provided, and the composition may optionally comprise other insecticidal peptides. The embodiments encompass the application of said compositions to the environment of insect pests to affect those insect pests. insect pests. BRIEF DESCRIPTION OF THE FIGURES Figures 1a-1g show an amino acid sequence alignment, using the ALIGNX ® module of the Vector NTI ® integrated package, from CrylBd (sec. ident no.: 1), IP1B-B1 (sec. ident. no. No.: 3), IP1B-B21 (part with ident. no.: 5), IP1B-B22 (part with ident. no.: 7), IP1B-B23 (part with ident. no. .: 9), IP1B-B24 (part with ident. no.: 11), IP1B-B25 (part with ident. no.: 13), IP1B-B26 (part with ident. no.: 15), IP1B-B27 (Section ID No.: 17), IP1B-B28 (Section ID No.: 19), IP1B-B29 (Section ID No.: 21) , IP1B-B31 (Section ID No.: 23), IP1B-B32 (Section ID No.: 25), IP1B-B33 (Section ID No.: 27), IP1B- B34 (Section ID No.: 29), IP1B-B40 (Section ID No.: 31), IP1B-B41 (Section ID No.: 33), IP1B-B42 ( sec. with ident. no.: 35), IP1B-B43 (sec. with ident. no.: 37), IP1B-B44 (sec. with ident. no.: 39), IP1B-B45 (sec. with ID no.: 41), IP1B-B46 (section with ID no. : ,í c 43), IP1B-B47 (Section ID No.: 45), MP258 (Section ID No.: 47), and GS060 (Section ID No.: 49). Amino acid sequence diversity among Cry1B polypeptides is highlighted. Figures 2a-2e show the amino acid sequence of MP258 with the leader region (*), Domain I (#), Domain II (&), and Domain III (!) indicated below the sequence. Figure 3 shows an alignment of amino acid sequences, using the ALIGNX® module of the Vector NTI® integrated package, of Domain I type Cry 1 Be of CrylBe (amino acids 35-276 of sec. ident. no.: 58) and the CrylBe-like Domain I of MP258 (amino acids 36-276 of SEQ ID NO: 47). Amino acid sequence diversity between domains I of Cry1B polypeptides is highlighted. Figure 4 shows an alignment of amino acid sequences, using the ALIGNX® module of the Vector NTI® integrated package, of Domain III of CrylAh (sec. with ID NO: 61), CrylBd, CrylBh (SEQ ID NO: 52), CryIBi (SEQ ID NO: 54), and MP258 (SEQ ID NO: 54). :47). Amino acid sequence diversity among Domain III Cry1B polypeptides is highlighted. Figures 5a-5c show an amino acid sequence alignment, using the ALIGNX ® module of the Vector NTI ® integrated package, of Domain I and Domain II of MP258 (SEQ ID NO: 47), CrylBe (sec. ident. no.: 58), CryIBi (sec. ident. no.: 54), CrylBg (sec. ident. no.: 60), CrylBf (sec. ident. no.: .: 59), CrylBa (sec. ident. no.: 55), CrylBh (sec. ident. no.: 52), CrylBd (sec. ident. no.: 1), CrylBb (sec. . with ident. no.: 56), and CrylBe (sec. with ident. no.: 57). Amino acid sequence diversity between Domain I and Domain II of the Cry1B polypeptides is highlighted. DETAILED DESCRIPTION The embodiments of the disclosure are directed to compositions and methods for affecting insect pests, particularly, plant pests. More specifically, the nucleic acid isolated from the modalities and fragments and variants thereof comprise nucleotide sequences encoding pesticidal polypeptides (eg, proteins). The described pesticidal proteins are biologically active (eg, pesticides) against insect pests such as, but not limited to, insect pests of the order Lepidoptera and / or Coleoptera. Compositions of the modalities comprise isolated nucleic acids and fragments and variants thereof encoding pesticidal polypeptides, expression cassettes comprising nucleotide sequences of the modalities, isolated pesticidal proteins, and pesticidal compositions. Some embodiments provide modified pesticidal polypeptides that have insecticidal activity against insects of the order Lepidoptera relative to the pesticidal activity of the corresponding wild-type protein. The embodiments further provide plants and microorganisms transformed with these novel nucleic acids and methods involving the use of such nucleic acids, pesticidal compositions, transformed organisms and products thereof to affect insect pests. The nucleic acids and nucleotide sequences of the embodiments can be used to transform any organism to produce the encoded pesticidal proteins. Methods involving the use of such transformed organisms to affect or control pests on plants are provided. The nucleic acids and nucleotide sequences of the embodiments can additionally be used to transform organelles, such c as chloroplasts (McBride et al. (1995) Biotechnology 13: 362-365; and Kota et al. (1999) Proc. Nati. Acad. Sci. USA 96: 1840-1845). The modalities further relate to the identification of fragments and variants of the naturally occurring coding sequence that encode biologically active pesticidal proteins. The nucleotide sequences of the embodiments can be used directly in methods to affect pests, particularly, insect pests, such as pests of the order Lepidoptera. Accordingly, the embodiments provide novel methods of affecting insect pests that do not rely on the use of traditional synthetic chemical insecticides. The modalities involve the discovery of naturally occurring biodegradable pesticides and the genes that encode them. The embodiments further provide fragments and variants of the naturally occurring coding sequence that additionally encode biologically active polypeptides (eg, pesticides). Nucleic acids of the embodiments encompass nucleic acid or nucleotide sequences that have been optimized for expression by the cells of a particular organism, for example, nucleic acid sequences that have been reverse translated (i.e., backtranslated) with the use of plant-preferred codons based on the amino acid sequence of a polypeptide having enhanced pesticidal activity. The modalities further provide mutations that confer improved or altered properties to the polypeptides of the modalities. See, for example, US patent no. 7,462,760. In the following description, various terms are widely used. The following definitions are provided to facilitate understanding of the modalities. Units, prefixes and symbols may be represented in their accepted SI form. Unless otherwise indicated, nucleic acids are written from left to right in the 5' to 3' orientation; amino acid sequences are written from left to right in the amino to carboxy orientation, respectively. Numeric ranges include the numbers that define the range. Amino acids may be indicated herein by their known three-letter symbols or by the one-letter symbols that are recommended by the IUPAC-IUB Biochemical Nomenclature Commission. In addition, nucleotides may be indicated by their generally accepted single letter codes. The terms listed above are more fully defined with reference to the specification in its entirety. As used herein, "nucleic acid" includes reference to a single- or double-stranded ribonucleotide or deoxyribonucleotide polymer and, unless otherwise limited, encompasses known analogs (eg, peptide nucleic acids). ) that have the essential nature of naturally occurring nucleotides in that they hybridize to single-stranded nucleic acids in a similar manner to naturally occurring nucleotides. As used herein, the terms "encoding" or "encoded", when used in the context of a specific nucleic acid, mean that the nucleic acid comprises the information necessary to direct translation of the nucleotide sequence into a specified protein. The information by which a protein is encoded is specified by the usage of codons. A nucleic acid encoding a protein may comprise untranslated sequences (eg, introns) c within translated regions of the nucleic acid or may lack such untranslated sequences (eg, as in cDNA). As used herein, "full-length sequence" in reference to a specified polynucleotide or its encoded protein means that it has the complete nucleic acid sequence or complete amino acid sequence of a native (non-synthetic) endogenous sequence. A full length polynucleotide encodes the full length catalytically active form of the specified protein. As used herein, the term "noncoding," used in the context of the orientation of a nucleotide sequence, refers to a double-stranded polynucleotide sequence operably linked to a promoter in an orientation in which it is not transcribed. no coding string. The non-coding strand is sufficiently complementary to an endogenous transcript so that translation of the endogenous transcript is often inhibited. Therefore, when the term "non-coding" is used in the context of a particular nucleotide sequence, the term refers to the complementary strand of the reference transcription product. The terms "polypeptide", "peptide" and "protein" are used interchangeably in the present description to refer to a polymer of amino acid residues. The terms apply to amino acid polymers, where one or more amino acid residues are an artificial chemical analogue of a corresponding naturally occurring amino acid, as well as naturally occurring amino acid polymers. The terms "residue" or "amino acid residue" or "amino acid" are used interchangeably herein to refer to an amino acid that is incorporated into a protein, polypeptide, or peptide (collectively "protein"). The amino acid can be a naturally occurring amino acid and, unless otherwise limited, can encompass known analogs of naturally occurring amino acids that can function similarly to naturally occurring amino acids. Polypeptides of the embodiments can be produced from a nucleic acid described herein or by use of standard molecular biology techniques. For example, a protein of the modalities can be produced by expression of a recombinant nucleic acid of the modalities in a suitable host cell or, alternatively, by a combination of ex vivo methods. As used herein, the terms "isolated" and "purified" are used interchangeably to refer to nucleic acids or polypeptides or biologically active portions thereof that are substantially or essentially free of components that normally accompany or interact with nucleic acid. or polypeptide as found in its natural environment. Thus, an isolated or purified nucleic acid or polypeptide is substantially free of other cellular material or culture medium when produced by recombinant techniques or substantially free of chemical precursors or other chemicals when chemically synthesized. An "isolated" nucleic acid is generally free of sequences (such as, for example, protein-coding sequences) that naturally flank the nucleic acid (ie, sequences located at the 5' and 3' ends of the nucleic acid) in the DNA. genomics of the organism from which the nucleic acid is derived. For example, in various embodiments, the isolated nucleic acids may contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb, or 0.1 kb of nucleotide sequences that naturally flank the nucleic acids. in the genomic DNA of the cell from which the nucleic acid is derived. As used herein, the terms "isolated" or "purified", with reference to a polypeptide of the embodiments, mean that the isolated protein is substantially free of cellular material and includes protein preparations having less than about 30% , 20%, 10% or 5% (by dry weight) of contaminating protein. When the protein of the forms or biologically active portion thereof is recombinantly produced, the culture medium represents less than about 30, 20, 10, or 5% (by dry weight) of chemical precursors or chemicals without the protein of interest. As used herein, a "recombinant" nucleic acid (or DNA) molecule refers to a nucleic acid (or DNA) sequence that is in a recombinant bacterial or plant host cell. In some embodiments, an "isolated" or "recombinant" nucleic acid is free of sequences (preferably protein-coding sequences) that naturally flank the nucleic acid (ie, the sequences located at the 5' and 3' ends). of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For the purposes of the present description, when "isolated" or "recombinant" is used to refer to nucleic acid molecules it excludes isolated chromosomes. As used herein, a "non-genomic nucleic acid sequence" or a "non-genomic nucleic acid molecule" refers to a nucleic acid molecule that has one or more changes in nucleic acid sequence compared to a native or genomic nucleic acid sequence. In some embodiments, the change to a native or genomic nucleic acid molecule includes, but is not limited to: changes in the nucleic acid sequence due to degeneracy of the genetic code; nucleic acid sequence optimization per codon for 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; removal of one or more introns associated with the genomic nucleic acid sequence; insertion of one or more heterologous introns; deletion of one or more upstream or downstream regulatory regions associated with the genomic nucleic acid sequence; insertion of one or more heterologous upstream or downstream regulatory regions; deletion of a 5' and / or 3' untranslated region associated with the genomic nucleic acid sequence; insertion of a heterologous 5' and / or 3' untranslated region; and modification of a polyadenylation site. In some embodiments, the non-genomic nucleic acid molecule is a cDNA. In some embodiments, the non-genomic nucleic acid molecule is a synthetic nucleic acid sequence. Throughout the specification, the expression "comprising", or its variants, such as "comprising" or "comprising", shall be understood to imply the inclusion of an element, integer, stage, or group of elements, integers or stages. mentioned, but does not exclude any other element, integer or stage, or group of elements, integer or stage. As used herein, the phrase "affecting insect pests" refers to making changes to the feeding, growth, and / or behavior of insects at any stage of development including, but not limited to: killing the insect insect; retard growth; impede reproductive capacity; anti-feeding activity; and the like. As used in the present description, the terms "pesticidal activity" and "insecticidal activity" are used synonymously to refer to to the activity of an organism or substance (such as, for example, a protein) that can be determined by, but not limited to, pest mortality, pest weight loss, pest repellency, and other changes physical and behavioral characteristics of a pest after feeding and exposure for an appropriate period of time. Thus, an organism or substance that has pesticidal activity adversely affects at least one measurable parameter of pest fitness. For example, "pesticidal proteins" are proteins that exhibit pesticidal activity by themselves or in combination with other proteins. As used herein, the term "pesticidally effective amount" refers to an amount of a substance or organism that has pesticidal activity when present in a pest environment. For each substance or organism, the amount effective as a pesticide is determined empirically for each affected pest in a specific environment. Similarly, "an insecticidally effective amount" can be used to refer to a "pesticidally effective amount" when the pest is an insect pest. As used herein, the terms "recombinant engineered" or "engineered" mean the use of genetic engineering to introduce (eg, engineer) a change in the structure of the protein based on understanding the mechanism of action of the protein and consideration of the amino acids that are introduced, deleted, or substituted. As used herein, the terms "mutant nucleotide sequence" or "mutation" or "mutagenized nucleotide sequence" refer to a nucleotide sequence that has been mutagenized or altered such that it contains one or more nucleotide residues ( eg, base pairs) not present in the corresponding wild type sequence. Said mutagenesis or alteration consists of one or more additions, deletions or substitutions or replacements of nucleic acid residues. When mutations are made by addition, deletion, or replacement of an amino acid from a proteolytic site, such addition, deletion, or replacement may be within or adjacent to the proteolytic site motif, as long as the target of the mutation is achieved (i.e., in so much that proteolysis is modified at the site). A mutant nucleotide sequence may encode a mutant insecticidal toxin that exhibits increased or decreased insecticidal activity or an amino acid sequence that confers increased or decreased insecticidal activity on a polypeptide containing it. As used herein, the terms "mutant" or "mutation" in the context of a protein, polypeptide, or amino acid sequence refer to a sequence that has been mutagenized or altered such that it contains one or more residues of amino acids not present in the corresponding wild type sequence. Said mutagenesis or alteration consists of one or more additions, deletions or substitutions or replacements of amino acid residues. A mutant polypeptide shows increased or decreased insecticidal activity or represents an amino acid sequence that confers increased insecticidal activity on a polypeptide containing it. Therefore, the terms "mutant" or "mutation" refer to the mutant nucleotide sequence and / or the encoded amino acids. The mutants can be used alone or in any compatible combination with other mutants of the modalities or with other mutants. Conversely, a "mutant polypeptide" may show a reduction in insecticidal activity. When more than one mutation is added to a particular nucleic acid or protein, the mutations may be added at the same time or in sequence; if sequential, the mutations may be added in any suitable order. As used herein, the terms "higher insecticidal activity" or "higher pesticidal activity" refer to an insecticidal polypeptide of the embodiments that has improved insecticidal activity relative to the activity of its corresponding wild-type protein and / or a insecticidal polypeptide effective against a broader range of insects and / or an insecticidal polypeptide specific for an insect that is not sensitive to the toxicity of the wild-type protein. To consider that a pesticidal activity is greater or improved, it must be demonstrated that the increase in pesticidal activity is at least 10%, against the target insect or that the increase in pesticidal activity is at least 20%, 25%, 30 %, 35%, 40%, 45%, 50%, 60%, 70%, 100%, 150%, 200% or 300% or higher with respect to the pesticidal activity of the wild type insecticidal polypeptide determined against the same insect. For example, greater pesticidal or insecticidal activity is provided when the polypeptide affects a broader or smaller range of insects relative to the range of insects affected by a wild-type Bt toxin. A broader range of impact may be desirable when versatility is preferred, while a narrower range of impact may be desirable when, for example, the use or presence of the toxin might otherwise affect beneficial insects. Although the modalities are not subject to any particular mechanism of action, changes in one or more characteristics of a polypeptide may additionally provide enhanced pesticidal activity; for example, the stability or longevity of a polypeptide in the gut of an Insect may be increased relative to the stability or longevity of a corresponding wild-type protein. The term "toxin" as used herein refers to a polypeptide that exhibits pesticidal activity or insecticidal activity or increased pesticidal activity or increased insecticidal activity. The "Sf" or Badilus thuringiensis" toxin is intended to include the broader class of Cry toxins found in various Bt strains, including toxins such as, for example, Cryis, Cry2s, or Cry3s. The terms "proteolytic site" or "cleavage site" refer to an amino acid sequence that confers sensitivity to a class of proteases or a particular protease such that the particular class of proteases or protease will digest a polypeptide containing the sequence of proteases. amino acids. A proteolytic site is said to be "sensitive" to the protease(s) that recognizes that site. It is recognized in the art that digestion efficiency will vary and that a reduction in digestion efficiency may lead to increased stability or prolonged duration of the polypeptide in the gut of an insect. Thus, a proteolytic site may confer sensitivity to more than one protease or classes of proteases, but the efficiency of digestion at that site caused by various proteases may vary. Proteolytic sites include, for example, trypsin sites, chymotrypsin sites, and elastase sites. Research has shown that the gut proteases of insects of the order Lepidoptera include trypsins, chymotrypsins, and elastases. See, for example, Lenz et al. (1991) Arch. Insect Biochem. physiol. 16:201-212; and Hedegus et al. (2003) Arch. Insect Biochem. physiol. 53:30-47. For example, approximately 18 different trypsins have been found in the midgut of Helicoverpa armigera larvae (see, Gatehouse et al. (1997) Insect Biochem. Mol. Biol. 27: 929-944 ). The preferred proteolytic substrate sites of these proteases. See, p. e.g., Peterson et al. (1995) Insect Biochem. Mol. Biol. 25: 765-774. Efforts have been made to understand the mechanism of action of Bt toxins and to develop toxins with greater properties by genetic engineering. It has been shown that insect gut proteases can affect the impact of Bt Cry proteins on the insect. Some proteases activate Cry proteins by processing them from a "protoxin" form into a toxic or "toxin" form. See, Oppert (1999) Arch. Insect Biochem. Phys. 42:1-12; and Carroll et al. (1997) J. Invertebrate Pathology 70: 41-49. This activation of the toxin may include removal of the N-terminal and C-terminal peptides from the protein and, in addition, may include internal cleavage of the protein. Other proteases can degrade Cry proteins. See Oppert, ibid. A comparison of the amino acid sequences of Cry toxins of different specifications reveals five blocks of highly conserved sequences. Structurally, the toxins comprise three distinct domains which are, from the N-terminal to the C-terminal: a cluster of seven alpha-helices involved in pore formation (referred to as “Domain I”), three antiparallel beta sheets involved in cell attachment (referred to as “Domain 2”) and a beta sandwich (referred to as “Domain 3”). The location and properties of these domains are known to those of skill in the art. See, for example, Li et al. (1991) Nature, 305:815821 and Morse et al. (2001) Structure, 9:409-417. When referring to a particular Domain, such as Domain I, it is understood that the precise boundaries of the Domain with respect to a particular sequence are not critical as long as the sequence or portion thereof includes a sequence that provides at least some attributed function. to the private Domain. Thus, for example, when referring to "Domain I", a particular sequence is intended to include a group of seven alpha-helices, but the exact boundaries of the sequence used or referred to with respect to that group are not critical. . A person skilled in the art knows the determination of said limits and the evaluation of said functions. In an effort to improve the Cry2B toxins, an effort was undertaken to identify the nucleotide sequences encoding the crystal proteins of the selected strains, which had improved activity compared to the native toxin. Depending on the characteristics of a given preparation, it was recognized that to demonstrate pesticidal activity it was sometimes necessary to perform trypsin pretreatment to activate the pesticidal proteins. Thus, it is understood that some pesticidal proteins require protease digestion (eg, by trypsin, chymotrypsin, and the like) for activation, while other proteins are biologically active (eg, pesticides) in the absence of activation. Such molecules can be altered by methods described, for example, in US Pat. 7,462,760. In addition, nucleic acid sequences can be developed by genetic engineering to encode polypeptides that contain additional mutations that confer increased or altered pesticidal activity relative to the pesticidal activity of the naturally occurring polypeptide. The nucleotide sequences of such genetically engineered nucleic acids comprise mutations not found in wild-type sequences. Mutant polypeptides of the embodiments are generally prepared by a process that involves the steps of: obtaining a nucleic acid sequence encoding a Cry family polypeptide; analyze the structure of the polypeptide to identify particular "target" sites for mutagenesis of the underlying gene sequence based on consideration of the proposed role of the target domain in the mode of action of the toxin; introducing one or more mutations into the nucleic acid sequence to produce a desired change in one or more amino acid residues of the encoded polypeptide sequence; and testing the produced polypeptide for pesticidal activity. Many of the Bt insecticidal toxins are related to varying degrees of similarity in their amino acid sequences and tertiary structure, and methods for obtaining the crystal structures of Bt toxins are known. Illustrative resolution of Cry3A and Cry3B polypeptides. The resolved structure of Cry3A (Li et al. (1991) Nature 353:815-821) provides information on the relationship between the structure and function of the toxin. A combined consideration of the published structural analyzes of Bt toxins and the reported function associated with particular structures and motifs and the like indicates that specific regions of the toxin correlate with particular functions and distinct stages of the protein's mode of action. For example, many toxins isolated from Bt are generally described as comprising three domains: a seven-helix cluster involved in pore formation, a three-sheet domain that has been implicated in receptor binding, and a beta-sandwich motif (Li et al (1991) Nature 305: 815-821). As reported in US Pat. Nos. 7,105,332 and 7,462,760, the toxicity of the Cry proteins can be increased by targeting the region between alpha helices 3 and 4 of Domain I of the toxin. This theory was argued against a knowledge base related to insecticidal toxins including: 1) that alpha-helices 4 and 5 of the Domain I Cry3A toxins are reported to insert into the lipid bilayer of cells lining the midgut of sensitive insects (Gazit et al. (1998) Proc. Nati. Acad. Sci. USA 95: 12289-12294) ; 2) the inventors' knowledge of the location of the trypsin and chymotrypsin cleavage sites within the amino acid sequence of the wild-type protein; 3) the observation that the wild-type protein is more active against certain insects after in vitro activation by trypsin or chymotrypsin treatment; and 4) reports that digestion of toxins from the 3' end results in decreased toxicity to insects. A series of mutations can be created and placed in various background sequences to create novel polypeptides that have enhanced or altered pesticidal activity. See, p. eg, US patent no. 7,462,760. These mutants include, but are not limited to; adding at least one additional protease sensitive site (eg, trypsin cleavage site) in the region between helices 3 and 4 of Domain I; replacing an original protease sensitive site in the wild-type sequence with a different protease sensitive site; the addition of several protease sensitive sites at a particular site; the addition of amino acid residues near the protease sensitive site(s) to alter the folding of the polypeptide and thus improve digestion of the polypeptide at the protease sensitive site(s) the protease; and adding mutations to protect the polypeptide from degradative digestion that reduce toxicity (eg, producing a series of mutations where the wild type amino acid is replaced by valine to protect the polypeptide from digestion). The mutations can be used alone or in any combination to provide polypeptides of the embodiments. Homologous sequences were identified by similarity search in the non-redundant (nr) database of the National Center for Bioinformatics. Information (NCBI) with the use of BLAST and PSI-BLAST. Homologous proteins were formed with Cry toxins mainly from Bacillus thuringiensis. A mutation consisting of an additional or alternative protease sensitive site may be sensitive to several classes of proteases, such as the serine proteases, including trypsin and chymotrypsin, or enzymes such as elastase. Therefore, a mutation consisting of an additional or alternative protease-sensitive site can be designed such that a category of proteases, such as mammalian proteases or insect proteases, readily recognize and / or clive the site. A protease responsive site can further be designed so that cleavage results from a particular class of enzymes or a particular enzyme produced in an organism such as, for example, a chymotrypsin produced by the earworm Heliothis zea (Lenz et al (1991) Arch Insect Biochem Physiol 16:201-212). In addition, the mutations may confer resistance to proteolytic digestion, eg, chymotrypsin digestion at the C-terminus of the peptide. The presence of an additional and / or alternative protease-responsive site in the amino acid sequence of the encoded polypeptide may increase the pesticidal activity and / or specificity of the polypeptide encoded by the nucleic acids of the embodiments. Accordingly, the nucleotide sequences of the modalities can be developed by recombinant genetic engineering or manipulated to produce polypeptides that have increased or altered insecticidal activity and / or specificity compared to that of an unmodified wild-type toxin. In addition, the mutations described herein can be positioned or used in conjunction with other nucleotide sequences to provide further properties. For example, a protease-sensitive site easily cleaved by chymotrypsin of the insect, p. a chymotrypsin found in bertha armyworm or earworm (Hegedus et al. (2003) Arch. Insect Biochem. Physiol. 53: 30-47; and Lenz et al. (1991) Arch. Insect Biochem Physiol 16:201-212) can be placed in a Cry background sequence to provide greater toxicity to that sequence. In this way, the modalities provide toxic polypeptides with increased properties. For example, a mutagenized Cry nucleotide sequence may comprise additional mutants comprising additional codons that introduce a second trypsin-sensitive amino acid sequence (in addition to the naturally occurring trypsin site) into the encoded polypeptide. An alternative addition mutant of the embodiments comprises additional codons designed to introduce at least one additional different protease-sensitive site into the polypeptide, for example, a chymotrypsin-sensitive site located immediately 5' or 3' of the trypsin site of origin. natural. Alternatively, substitution mutants can be created in which at least one codon of the nucleic acid encoding the naturally occurring protease sensitive site is destroyed and alternative codons are introduced into the nucleic acid sequence to provide a different protease sensitive site. (eg, substitute). In addition, a replacement mutant can be added to a Cry sequence in which the naturally occurring trypsin cleavage site present in the encoded polypeptide is destroyed and a chymotrypsin or elastase cleavage site is introduced in its place. It is recognized that any nucleotide sequences encoding amino acid sequences that are proteolytic sites or putative proteolytic sites (eg, sequences such as RR or LKM) can be used and that the exact identity of the codons used to introduce any of these may be used. Cleavage sites in a variant polypeptide may vary depending on the use, that is, expression in a particular plant species. Furthermore, it is recognized that any of the described mutations can be introduced into any of the embodiments polynucleotide sequences comprising codons for amino acid residues that provide the specified native trypsin cleavage site for the modification. Accordingly, full-length toxin variants or fragments thereof may be modified to contain additional or alternative cleavage sites and the scope of the embodiments described herein is intended to encompass these embodiments. Those of skill in the art will appreciate that any useful mutations can be added to the sequences of the modalities as long as the encoded polypeptides retain pesticidal activity. Thus, the sequences can be further mutated such that the encoded polypeptides are resistant to proteolytic digestion by chymotrypsin. More than one recognition site can be added at a particular site in any combination, and multiple recognition sites can be added to or removed from the toxin. Therefore, additional mutations may comprise three, four or more recognition sites. It is recognized that multiple mutations can be designed in any suitable polynucleotide sequence; consequently, full-length sequences or fragments thereof can be modified to contain additional or alternative cleavage sites and, furthermore, to be resistant to proteolytic digestion. Thus, the embodiments provide Cry toxins containing mutations that produce increased pesticidal activity as well as improved compositions and methods for affecting pests using other Bt toxins. Mutations can protect the polypeptide from protease degradation, for example, by deletion of putative proteolytic sites such as putative serine protease sites and elastase recognition sites from different areas. Some or all of these putative sites can be deleted or altered in a way that reduces proteolysis at the site of the original site. Changes in proteolysis can be assessed by comparison of a mutant polypeptide with wild type toxins or by comparison of mutant toxins that differ in their amino acid sequence. Putative proteolytic sites and proteolytic sites include, but are not limited to, the following sequences: RR, a trypsin cleavage site; LKM, a chymotrypsin site; and a trypsin site. These sites can be altered by the addition or deletion of any number and type of amino acid residues, as long as the pesticidal activity of the polypeptide is increased. Therefore, the polypeptides encoded by the nucleotide sequences comprising mutations will comprise at least one amino acid change or addition from the native or background sequence or 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, 32, 35, 38, 40, 45, 47, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, or 280 or more amino acid changes or additions. The pesticidal activity of a polypeptide can be further increased by truncation of the full-length or native sequence, as is known in the art. Compositions of the embodiments include nucleic acids and fragments and variants thereof that encode pesticidal polypeptides. Particularly, the embodiments provide isolated nucleic acid molecules comprising nucleotide sequences that encode the amino acid sequence of sec. with no. of ident.. 3, sec. with no. of ident.: 5, sec. with no. from ident: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. from ident: 21, sec. with no. from ident: 23, sec. with no. of ident.: 25, sec. with no. of ident.: 27, sec. with no. of ident.: 29, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. of ident.: 39, sec. with no. from ident: 41, sec. with no. of ident.: 43 and sec. with no. of ident.:45 or the nucleotide sequences encoding that amino acid sequence, eg, the amino acid sequence set forth in sec. with no. of ident.: 4, sec. with no. of ident.: 6, sec. with no. of ident.: 8, sec. with no. of ident.: 10, sec. with no. of ident.: 12, sec. with no. from ident: 14, sec. with no. from ident: 16, sec. with no. of ident.: 18, sec. with no. of ident.: 20, sec. with no. of ident.: 22, sec. with no. of ident.: 24, sec. with no. of ident.: 26, sec. with no. of ident.: 28, sec. with no. of ident.: 30, sec. with no. of ident.: 32, sec. with no. of ident.: 34, sec. with no. of ident.: 36, sec. with no. of ident.: 38, sec. with no. of ident.: 40, sec. with no. of ident.: 42, sec. with no. of ident.: 44 or sec. with no. of ident.: 46, and fragments and variants of these. Particularly, the embodiments provide isolated nucleic acid molecules that encode the amino acid sequence illustrated in sec. with no. of ident.: 4 or sec. with no. of ident.: 8 or the nucleotide sequences encoding that amino acid sequence, eg, the amino acid sequence set forth in sec. with no. of ident.: 4, sec. with no. of ident.: 6, sec. with no. of ident.: 8, sec. with no. of ident.: 10, sec. with no. of ident.: 12, sec. with no. of ident.: 14, sec. with no. of ident.: 16, sec. with num. of ident.: 18, sec. with no. of ident.: 20, sec. with no. of ident.: 22, sec. with no. of ident.: 24, sec. with no. of ident.: 26, sec. with no. of ident.: 28, sec. with no. of ident.: 30, sec. with no. of ident.: 32, sec. with no. of ident.: 34, sec. with no. of ident.: 36, sec. with no. of ident.: 38, sec. with no. of ident.: 40, sec. with no. of ident.: 42, sec. with no. of ident.: 44, and sec. with no. of ident.: 46, and fragments and variants of these. In addition, optimized nucleotide sequences encoding the pesticidal proteins of the modalities are of interest. As used herein, the phrase "optimized nucleotide sequences" refers to nucleic acids optimized for expression in a particular organism, eg, a plant. Optimized nucleotide sequences can be prepared for any organism of interest using methods known in the art. See, for example, US patent no. 7,462,760, which describes an optimized nucleotide sequence encoding a disclosed pesticidal protein. In this example, the amino acid sequence was prepared by reverse translating the amino acid sequence of the protein and modifying the amino acid sequence to comprise maize-preferred codons while encoding the same amino acid sequence. amino acids. This procedure is described in more detail by Murray et al. (1989) Nucleic Acids Res. 17:477-498. The optimized nucleotide sequences are useful for increasing the expression of a pesticidal protein in a plant, for example, monocot plants of the Gramineae (Poaceae) family, such as, for example, a maize plant. In some embodiments, polypeptides are provided that comprise an amino acid sequence set forth in sec. with no. of ident.: 3, sec. with no. of ident.: 5, sec. with no. of ident.: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 23, sec. with no. of ident.: 25, sec. with no. of ident.: 27, sec. with no. of ident.: 29, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. from dent: 37, sec. with no. of ident.: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with no. of ident.: 45 and fragments and variants of these. In some embodiments, polypeptides are provided that comprise an amino acid sequence set forth in sec. with no. of ident.: 3, sec. with no. of ident.: 5, sec. with no. of ident.: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. of ident.: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with no. of ident.: 45 and fragments and variants of these. In some embodiments, polypeptides are provided that comprise an amino acid sequence set forth in sec. with no. of ident.: 23, sec. with no. of ident.: 25, sec. with no. of ident.: 27 or sec. with no. of ident.: 29, and fragments and variants of these. In some embodiments, variant Cry1B polypeptides are provided that have one amino acid substitution compared to the corresponding reference Cry1B polypeptide that have increased insecticidal activity against earworm and / or fall armyworm compared to the "reference Cry1B polypeptide". correspondent". By "corresponding reference Cry1B polypeptide" is meant a wild-type or native Cry1B polypeptide or Cry1B variant polypeptide of the present embodiments, which can serve as the amino acid sequence that is mutagenized to create the Cry1B variant polypeptide. In some embodiments, the corresponding reference Cry1B polypeptide comprises a CrylBe-like Domain I and a CrylAh-like Domain III. By "CrylBe-like Domain I" is meant an amino acid sequence having a sequence identity of at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99% or higher with amino acids 36-276 of sec. with no. of ident.: 58 (CrylBe) or amino acids 35-276 of the sec. with no. ID NO: 47. An amino acid sequence alignment of Domain I of CrylBe (SEQ ID NO: 58) and MP258 (SEQ ID NO: 47) is shown in Figure 3. Similarly, other native Cry1B polypeptides can be aligned with CrylBe (SEQ ID NO: 58) and MP258 (SEQ ID NO: 47) to identify other CrylBe-like Domain I regions. By "CrylAh-type Domain III" is meant an amino acid sequence having a sequence identity of at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, to at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92% at least 93% at least 94%, at least 95% at least 96% , at least 97%, at least 98%, at least 99% or higher with amino acids 483-643 of sec. with no. of ident.: 61 (CrylAh) or 494-655 of sec. with no. ID No: 47. A Domain III amino acid sequence alignment of CrylAh (SEQ ID NO: 61), CrylBd (SEQ ID NO: 1), CrylBh (SEQ ID NO: 47). Similarly, other native Cry1B polypeptides can align with CrylAh (Sec ID No: 61), CrylBd, CrylBh (SEQ ID NO: 52), CryIBi (SEQ ID NO: 54), and / or MP258 (SEQ ID NO: 47) to identify other Domain III regions CrylAh type. In some embodiments, the corresponding reference Cry1B polypeptide comprises a CrylBa-like Domain I and Domain II. By "Domain I and Domain type II CrylBa" is meant an amino acid sequence having at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 74% sequence identity. 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% at least 96%, at least 97%, at least 98%, at least 99% or higher with amino acids 30-489 of sec. with no. of ident.: 55 (CrylBa). An amino acid sequence alignment of Domain I and Domain II of MP258 (sec. ident. no: 47), CrylBe (sec. with no. ident. no.: 58), CryIBi (sec. ident. no.: 54), CrylBg (sec. with no. ident. no.: 60), CrylBf (sec. ident. no.: 59), CrylBa (sec. with no. ident. no.: 55), CrylBh (sec. ident. no.: 52), CrylBd (sec. with no. 1), CrylBb (SEQ ID NO: 56), and CrylBe (SEQ ID NO: 57) are shown in Figure 5. Similarly, other native Cry1B polypeptides can be aligned with CrylBa (SEQ ID NO: 55) and MP258 (SEQ ID NO: 47) to identify other CrylBa-like Domain I and Domain II regions. In some embodiments, the corresponding reference Cry1B polypeptide comprises a CrylBe-like Domain I and Domain II. By "Domain I and Domain type II CrylBe" is meant an amino acid sequence having a sequence identity of at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% at least 96%, at least 97%, at least 98%, at least 99% or greater with amino acids 35-494 of sec. with no. from ident: 58 (CrylBe) or amino acids 35-493 of sec. with no. ID No: 47. A Domain I and Domain II amino acid sequence alignment of MP258 (SEQ ID NO: 47), CrylBe (SEQ ID NO: 58), CryIBi (SEQ ID NO: 58). . with ident. no.: 54), CrylBg (sec. with ident. no.: 60), CrylBf (sec. with ident. no.: 59), CrylBa (sec. with ident. no.: 59). : 55), CrylBh (sec. ident. no.: 52), CrylBd (sec. ident. no.: 1), CrylBb (sec. ident. no.: 56), and CrylBe (sec. Similarly, other native Cry1B polypeptides can align with CrylBe (SEQ ID NO: 58) and MP258 (SEQ ID NO: 57). 47) to identify other CrylBe-like Domain I and Domain II regions. By "improved activity" or "increased activity" is meant an increase of at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35% , at least approximately 40%, at least approximately 50%, at least approximately 60%, at least approximately 70%, at least approximately 80%, at least approximately 90%, at least approximately 100%, at least approximately 110%, at least approximately less about 120%, at least about 130%, at least approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately approximately roughly 140%, at least approximately 150%, at least 160%, at least approximately 170%, at least 180%, at least approximately 190%, at least 200%, at least approximately 210% at least 220%, at least approximately 230 %, at least 240%, at least approximately 250%, at least 260%, at least approximately 270%, at least 280%, at least approximately 290%, at least 300%, at least approximately 310%, at least 320% , at least approximately 330%, at least 340%, at least approximately 350%, at least 360%, at least approximately 370%, at least 380%, at least approximately 390%, at least 400%, at least approximately 410% , at least 420%, at least approximately 430%, at least 440%, at least approximately 450%, at least 460%, at least approximately 470%, at least 480%, at least approximately 490%, at least 500%, at least approximately 510%, at least 520%, at least approximately 530%, at least 540%, at least approximately 550%, at least 560%, at least approximately 570%, at least 580%, at least approximately 590%, at least 600%, at least approximately 650%, at least 700%, at least approximately 750%, at least 800%, at least approximately 850%, at least 900%, at least approximately 950%, at least about 1000% or greater or at least about 1.1-fold, at least about 1.2-fold, at least about 1.3-fold, at least about 1.4-fold, or at least about 1.5-fold increase, at at least about 1.6 times, at least about 1.7 times, at least about 1.8 times, at least about 1.9 times, at least about 2 times, at least about 2.1 times, at least about 2, 2 times, at least approximately 2.3 times, at least approximately 2.4 times, at least approximately 2.5 times, at least approximately 2.6 times, at least approximately 2.7 times, at least approximately 2.8 times , at least about 2.9 times, at least about 3 -times, at least about 3.1 times, at least about 3.2 times, at least about 3.3 times, at least about 3.4 times, at least about 3.5 times, at least about 3.6 times, at least about 3.7 times is, at least approximately 3.8 times, at least approximately 3.9 times, at least approximately 4 times, at least approximately 4.1 times, at least approximately 4.2 times, at least approximately 4.3 times, at least about 4.4 times, at least about 4.5 times, at least about 4.6 times, at least about 4.7 times, at least about 4.8 times, at least about 4.9 times, at least about 5 times, at least about 5.1 times, at least about 5.2 times, at least about 5.3 times, at least about 5.4 times, at least about 5.5 times, at least about 5.6 times, at least about 5.7 times, at least about 5.8 times, at least about 5.9 times, at least about 6 times, at least about 6.1 times, at least about 6.2 times, at at least about 6.3 times, at least about 6.4 times, at least about 6.5 times, at least about 6.6 times, at least about 6.7 times, at least about 6.8 times, at least about 6.9 times, at least about 7 times, at least about 7.1 times, at least about 7.2 times, at least about 7.3 times, at least about 7.4 times, at least about 7.5 times , at least about 7.6 times, at least about 7.7 times, at least about 7.8 times, at least about 7.9 times, at least about 8 times, at least about 8.1 times, at least about 8.2 times, at least about 8.3 times, at least about 8.4 times, at least about 8.5 times, at least about 8.6 times, at least about 8.7 times, at least about 8, 8 times, at least approximately 8.9 times, at least approximately 9 times, at least approximately at least about 9.1 times, at least about 9.2 times, at least about 9.3 times, at least about 9.4 times, at least about 9.5 times, at least about 9.6 times, at least about 9 times 0.7-fold, at least about 9.8-fold, at least about 9.9-fold, at least about 10-fold or higher in the pesticidal activity of the protein variant compared to the activity of the corresponding reference Cryl B polypeptide. In some embodiments, the improvement consists of a decrease in EC50 of at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least 36 about 80%, at least about 90%, at least about 100%, at least about 110%, at least about 120%, at least about 130%, at least about 140%, at least about 150%, at least about 160%, at least approximately 170%, at least approximately 180%, at least approximately 190%, at least approximately 200%, at least approximately 210%, at least approximately 220%, at least approximately 230%, at least approximately 240%, at least about 250%, at least about 260%, at least about 270%, at least about 280%, at least about 290%, at least about 300%, at least about 310%, at least about 320%, at least about 330%, at least about 340%, at least about 350%, at least about 360%, at least about 370%, at least about 380%, at least about 39 0%, at least approximately 400%, at least approximately 410%, at least approximately 420%, at least approximately 430%, at least approximately 440%, at least approximately 450%, at least approximately 460%, at least approximately 470% , at least approximately 480%, at least approximately 490%, at least approximately 500%, at least approximately 510%, at least approximately 520%, at least approximately 530%, at least approximately 540%, at least approximately 550%, at least approximately least about 560%, at least about 570%, at least about 580%, at least about 590%, at least about 600%, at least about 650%, at least about 700%, at least about 750%, at least about 800%, at least about 850%, at least about 900%, at least about 950%, at least about 1000% or greater or at least about 1 reduction, 1 times, at least about 1.2 times, at least about 1.3 times, at least about 1.4-times or at least about 1.5 times, at least about 1.6 times, at least about 1.7 times , at least about 1.8 times, at least about 1.9 times, at least about 2 times, at least about 2.1 times, at least about 2.2 times, at least about 2.3 times, at least about 2.4 times, at least about 2.5 times, at least about 2.6 times, at least about 2.7 times, at least about 2.8 times, at least about 2.9 times, at least about 3 times , at least approximately 3.1 times, at least approximates at least about 3.2 times, at least about 3.3 times, at least about 3.4 times, at least about 3.5 times, at least about 3.6 times, at least about 3.7 times, at least about 3 8 times, at least about 3.9 times, at least about 4 times, at least about 4.1 times, at least about 4.2 times, at least about 4.3 times, at least about 4.4 times, at least about 4.5 times, at least about 4.6 times, at least about 4.7 times, at least about 4.8 times, at least about 4.9 times, at least about 5 times, at least about 5 times .1 times, at least about 5.2 times, at least about 5.3 times, at least about 5.4 times, at least about 5.5 times, at least about 5.6 times, at at least about 5.7 times, at least about 5.8 times, at least about 5.9 times, at least about 6 times, at least about 6.1 times, at least about 6.2 times, at least about 6, 3 times, at least about 6.4 times, at least about 6.5 times, at least about 6.6 times, at least about 6.7 times, at least about 6.8 times, at least about 6.9 times , at least about 7 times, at least about 7.1 times, at least about 7.2 times, at least about 7.3 times, at least about 7.4 times, at least about 7.5 times, at least about 7.6 times, at least about 7.7 times, at least about 7.8 times, at least about 7.9 times, at least about 8 times, at least about 8.1 times, at least about 8.2 times , at least about 8.3 times, at least about 8.4 times, at least about 8.5 times, at least about 8.6 times, at least about 8.7 times, at least about 8.8 times, at least about 8.9 times, at least about 9 times, at least about 9.1 times times, at least about 9.2 times, at least about 9.3 times, at least about 9.4 times, at least about 9.5 times, at least about 9.6 times, at least about 9.7 times, at least about 9.8-fold, at least about 9.9-fold, at least about 10-fold or higher in the EC50 of the Cry1B variant polypeptide relative to the pesticidal activity of the corresponding reference Cry1B polypeptide. In some modalities, the EC50 of the variant Cry1B polypeptide is <100 ppm, <90 ppm, <80 ppm, <70 ppm, <60 ppm, <50 ppm, <45 ppm, <40 ppm, <35 ppm, <30 ppm , <25 ppm, <20 ppm, <19 ppm, <18 ppm, <17 ppm, <16 ppm, <15 ppm, <14 ppm, <13 ppm, <12 ppm, <11 ppm, <10 ppm, < 9ppm, <8ppm, <7ppm, <6ppm, <5ppm, <4ppm, <3ppm, <2ppm, <1ppm, <0.9ppm, <0.8ppm, <0, 7 ppm, <0.6 ppm, <0.5 ppm, <0.4 ppm, <0.3 ppm, <0.2 ppm, or <0.1 ppm. In some modalities, the improvement consists of an increase in the index Average FAE of at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 50% , at least approximately 60%, at least approximately 70%, at least approximately 80%, at least approximately 90%, at least approximately 100%, at least approximately 110%, at least approximately 120%, at least approximately 130%, at least approximately least about 140%, at least about 150%, at least about 160%, at least about 170%, at least about 180%, at least about 190%, at least about 200%, at least about 210% at least about 220 %, at least approximately 230%, at least approximately 240%, at least approximately 250%, at least approximately 260%, at least approximately 270%, at least approximately 280%, at least approximately imately 290%, at least approximately 300%, at least approximately 310%, at least approximately 320%, at least approximately 330%, at least approximately 340%, at least approximately 350%, at least approximately 360%, at least approximately 370 %, at least approximately 380%, at least approximately 390%, at least approximately 400%, at least Yo about 410%, about 430%, about 450%, about 470%, about 490%, about 510%, about 530%, about 550%, about 570%, about 590%, about about 650%, to about 750%, to about 850%, to about 420%, to about 440%, to about 460%, to about 480%, to about 500%, to about 520%, at least about 540%, at least about 560%, at least about 580%, at least about 600%, at least about 700%, at least about 800%, at least less less less less less less less less less less less less least about 900%, to about 950%, at least about 1000% or greater or an increase of at least about 1.1-fold, at least about 1.2-fold, at least about 1.3-fold, at least about 1.4-fold or at least about 1.5-fold, at least about 1.6-fold, at least about 1.7 times, at least approximately 1.8 times, at least approximately 1.9 times, at least approximately 2 times, at least approximately 2.1 times, at least approximately 2.2 times, at least approximately 2.3 times, at least about 2.4 times, at least about 2.5 times, at least about 2.6 times, at least about 2.7 times, at least about 2.8 times, at least approximately 2.9 times, at least approximately 3 times, at least approximately 3.1 times, at least approximately 3.2 times, at least approximately 3.3 times, at least about 3.4 times, at least about 3.5 times, at least about 3.6 times, at least about 3.7 times, at least about 3.8 times, at least about 3.9 times, at least approximately 4 times, at least approximately 4.1 times, at least approximately 4.2 times, at least approximately 4.3 times, at least approximately 4.4 times, at least approximately 4.5 times, at least approximately 4.6 times, at least approximately 4.7 times , at least approximately 4.8 times, at least approximately 4.9 times, at least approximately 5 times, at least approximately 5.1 times, at least approximately 5.2 times, at least approximately 5.3 times, at least approximately 5.4 times, at least approximately 5.5 times, at least approximately 5.6 times, at least approximately 5.7 times, at least approximately 5.8 times , at least approximately 5.9 times, at least approximately 6 times, at least approximately 6.1 times, at least approximately 6.2 times, at least approximately 6.3 times, at least approximately 6.4 times, at least approximately 6.5 times, at least approximately 6.6 times, at least approximately 6.7 times, at least approximately 6.8 times, at least approximately 6.9 times , at least approximately 7 times, at least approximately 7.1 times, at least approximately 7.2 times, at least approximately 7.3 times, at least approximately 7.4 times, at least approximately 7.5 times, at least approximately 7.6 times, at least approximately 7.7 times, at least approximately 7.8 times, at least approximately 7.9 times, at least approximately 8 times, at least about 8.1 times, at least about 8.2 times, at least about 8.3 c times, at least approximately 8.4 times, at least approximately 8.5 times, at least approximately 8.6 times, at least approximately 8.7 times, at least approximately 8.8 times, at least approximately 8.9 times, at least approximately 9 times, at least approximately 9.1 times, at least about 9.2 times, at least about 9.3 times, at least about 9.4 times, at least about 9.5 times, at least about 9.6-fold, at least about 9.7-fold, at least about 9.8-fold, at least about 9.9-fold, at least about 10-fold or higher in the average FAE index of the Cry1B polypeptide variant relative to the pesticidal activity of the corresponding reference Cry1B polypeptide. "average FAE index" (MFI) refers to the mean of multiple FAEGNs and an arithmetic mean of FAEGNs. As used herein, the "mean deviation score" refers to the arithmetic mean of multiple deviation scores. In some modalities, the improvement consists of an increase in the mean deviation score of at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90 %, at least approximately 100%, at least approximately 110%, at least approximately 120%, at least approximately 130%, at least approximately 140%, at least approximately 150%, at least approximately 160%, at least about 170%, at least about 190%, at least about 210%, at least about 230%, at least about 250%, at least about 270%, at least about 290%, at least about 310%, at least about 330% , at least approximately 350%, at least approximately 370%, at least approximately 390%, at least approximately 410%, at least approximately 430%, at least approximately 450%, at least approximately 470%, at least approximately 490%, at least approximately least about 510%, at least about 530%, at least about 550%, at least about 570%, at least about 590%, at least about 650%, at least about 750%, at least about 850%, at least about 950%, at least less an increase of about about 180%, at least about 200%, at least about 220%, at least about 240%, at least about 260%, at least about 280%, at least about 300% , at least approximately 320%, at least approximately 340%, at least approximately 360%, at least approximately 380%, at least approximately 400%, at least approximately 420%, at least approximately 440%, at least approximately 460%, at least approximately least about 480%, at least about 500%, at least about 520%, at least about 540%, at least about 560%, at least about 580%, at least about 600%, at least about 700%, at least about 800%, at least approximately 900%, at least □approximately 1000% or greater or at least 1.1 times, at least c about 1.2 times, at least about 1.3 times, at least about 1.4 times or at least about 1.5 times, at least about 1.6 times, at least about 1.7 times, at least approximately 1.8 times, at least approximately 1.9 times, at least approximately 2 times, at least approximately 2.1 times, at least approximately 2.2 times, at least approximately 2.3 times, at least about 2.4 times, at least about 2.5 times, at least about 2.6 times, at least about 2.7 times, at least about 2.8 times, at least approximately 2.9 times, at least approximately 3 times, at least approximately 3.1 times, at least approximately 3.2 times, at least approximately 3.3 times, at least approximately 3.4 times, at least about 3.5 times, at least about 3.6 times, at least about 3.7 times, at least about 3.8 times, at least about 3.9 times, at least approximately 4 times, at least approximately 4.1 times, at least approximately 4.2 times, at least approximately 4.3 times, at least approximately 4.4 times, at least approximately 4.5 times, at least approximately 4.6 times, at least approximately 4.7 times , at least approximately 4.8 times, at least approximately 4.9 times, at least approximately 5 times, at least approximately 5.1 times, at least approximately 5.2 times, at least approximately 5.3 times, at least approximately 5.4 times, at least approximately 5.5 times, at least approximately 5.6 times, at least approximately 5.7 times, at least approximately 5.8 times , at least about 5.9 times, at least about 6 times, at least about 6.1 c times, at least approximately 6.2 times, at least approximately 6.3 times, at least approximately 6.4 times, at least approximately 6.5 times, at least approximately 6.6 times, at least approximately 6.7 times, at least approximately 6.8 times, at least approximately 6.9 times , at least approximately 7 times, at least approximately 7.1 times, at least approximately 7.2 times, at least approximately 7.3 times, at least approximately 7.4 times, at least approximately 7.5 times, at least approximately 7.6 times, at least approximately 7.7 times, at least approximately 7.8 times, at least approximately 7.9 times, at least approximately 8 times, at least about 8.1 times, at least about 8.2 times, at least about 8.3 times, at least about 8.4 times, at least about 8.5 times, at least approximately 8.6 times, at least approximately 8.7 times, at least approximately 8.8 times, at least approximately 8.9 times, at least approximately 9 times, at least approximately 9.1 times, at least about 9.2 times, at least about 9.3 times, at least about 9.4 times, at least about 9.5 times, at least about 9.6-fold, at least about 9.7-fold, at least about 9.8-fold, at least about 9.9-fold, at least about 10-fold or greater in Cry1B variant polypeptide mean deviation score relative to activity pesticide from the corresponding reference Cry1B polypeptide. In some embodiments, the enhanced activity of the Cry1B variant polypeptide is relative to the pesticidal activity of sec. with no. of ident.: 1 (CrylBd), sec. with no. of ident.: 47 (MP258), sec. with no. ident.: 52 c (CrylBh), sec. with no. ID: 54 (CryIBi), sec. with no. of ident.: 3, sec. with no. of ident.: 5, sec. with no. of ident.: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 31, sec. with ident. no.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. of ident.: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with no. of ident.: 45. In particular embodiments, the pesticidal proteins of the embodiments provide full-length insecticidal polypeptides, full-length insecticidal polypeptide fragments, and variant polypeptides produced from mutagenized nucleic acids designed to introduce particular amino acid sequences into polypeptides of the embodiments. In particular embodiments, the amino acid sequences that are introduced into the polypeptides comprise a sequence that provides a cleavage site for an enzyme such as a protease. It is known in the art that the pesticidal activity of Bt toxins is typically activated by peptide cleavage in the insect gut by the action of various proteases. Since peptide cleavage cannot always be carried out with full efficiency in the insect gut, some fragments of a full-length toxin may have enhanced pesticidal activity compared to the full-length toxin itself. Therefore, some of the polypeptides of the embodiments include fragments of a full-length insecticidal polypeptide, and some of the polypeptide fragments, variants, and mutations will have enhanced pesticidal activity relative to the activity of the naturally occurring insecticidal polypeptide from the polypeptide. which they are derived, particularly if the insecticidal polypeptide naturally occurring is not activated in vitro with a protease prior to screening for activity. Therefore, the present application covers fragments or truncated versions of the sequences. Mutations can be placed in any background sequence that includes such truncated polypeptides, as long as the polypeptide retains pesticidal activity. One of skill in the art can easily compare two or more proteins with respect to pesticidal activity using tests known in the art or described elsewhere in the present disclosure. It will be understood that the polypeptides of the modalities can be produced by the expression of a nucleic acid described in the present description or through the use of conventional molecular biology techniques. It is recognized that pesticidal proteins can be oligomeric and will vary in molecular weight, amount of residues, component peptides, activity against particular pests, and other characteristics. However, by the methods set forth herein, proteins active against various pests can be isolated and characterized. The pesticidal proteins of the embodiments can be used in conjunction with other Bt toxins or other insecticidal proteins to increase the target range of insects. Furthermore, the use of the pesticidal proteins of the embodiments in conjunction with other Bt toxins or other insecticidal principles of a different nature is particularly useful for the prevention and / or management of insect resistance. Other insecticidal agents include inhibitors of protease (of the serine and cysteine ​​types), α-amylase, and peroxidase. In addition, the embodiments encompass fragments and variants of nucleotide and amino acid sequences and polypeptides so encoded. As used herein, the term "fragment" is refers to a portion of a nucleotide sequence of a polynucleotide or a portion of an amino acid sequence of a polypeptide of the embodiments. Fragments of a nucleotide sequence may encode protein fragments that retain the biological activity of the corresponding full-length or native protein and, consequently, have pesticidal activity. Therefore, it is recognized that some of the amino acid and polynucleotide sequences of the embodiments can be correctly referred to as fragments and as mutants. It will be understood that the term "fragment", as used to refer to nucleic acid sequences of the embodiments, further encompasses sequences useful as hybridization probes. This class of nucleotide sequences generally does not encode fragment proteins that retain biological activity. Thus, fragments of a nucleotide sequence can range from at least about 20 nucleotides, about 50 nucleotides, about 100 nucleotides, and up to the full-length nucleotide sequence that encodes the proteins of the embodiments. A fragment of a nucleotide sequence of the embodiments encoding a biologically active portion of a pesticidal protein of the embodiments will encode at least 15, 25, 30, 50, 100, 200, 250, or 300 contiguous amino acids or up to the total number of amino acids present in a pesticidal polypeptide of the embodiments (eg, 651 amino acids for SEQ ID NO: 3). Thus, it is understood that the modalities further encompass polypeptides that are fragments of the illustrative pesticidal proteins of the modalities and that are at least 15, 25, 30, 50, 100, 200, 250 or 300 contiguous amino acids in length or up to the total number of amino acids present in a polypeptide pesticide of the embodiments (eg, 651 amino acids for SEQ ID NO: 3). Fragments of a nucleotide sequence of embodiments useful as hybridization probes or PCR primers generally need not encode a biologically active portion of a pesticidal protein. Thus, a fragment of a nucleic acid of the embodiments may encode a biologically active portion of a pesticidal protein or may be a fragment that can be used as a hybridization probe or PCR primer using the methods described herein. . A biologically active portion of a pesticidal protein can be prepared by isolating a portion of one of the nucleotide sequences of the embodiments, expressing the encoded portion of the pesticidal protein (eg, by recombinant expression in vitro), and assessing the activity of the encoded portion of the pesticidal protein. Nucleic acids that are fragments of a nucleotide sequence of the embodiments comprise at least 16, 20, 50, 75, 100, 150, 200, 250, 300, 350, 400, 450, 500, 600, 700, 800, 850 , 900 or 950 nucleotides or up to the number of nucleotides present in a nucleotide sequence described herein (eg, 1953 nucleotides for SEQ ID NO: 4). Some particular embodiments contemplate fragments derived from (eg, produced from) a first nucleic acid of the embodiments, wherein the fragment encodes a truncated toxin having pesticidal activity. Truncated polypeptides encoded by the polynucleotide fragments of the embodiments have pesticidal activity either equivalent to or greater than the activity of the corresponding full-length polypeptide encoded by the first nucleic acid from which the fragment is derived. It is contemplated that such nucleic acid fragments of the embodiments may be truncated at the 3' end of the corresponding full-length or native coding sequence. The nucleic acid fragments may further be truncated at the 5' end and the 3' end of the corresponding full-length or native coding sequence. The term "variants" is used in the present description to refer to substantially similar sequences. For nucleotide sequences, conservative variants include those sequences which, due to degeneracy of the genetic code, encode the amino acid sequence of one of the pesticidal polypeptides of the modalities. Those skilled in the art will readily appreciate that due to the degeneracy of the genetic code there are a multitude of nucleotide sequences that encode polypeptides of the present disclosure. In some embodiments, the nucleic acid molecule encoding the polypeptide is a non-genomic nucleic acid sequence. As used herein, a "non-genomic nucleic acid sequence" or "non-genomic nucleic acid molecule" or "non-genomic polynucleotide" refers to a nucleic acid molecule that has one or more sequence changes. nucleic acid in comparison to a natural or genomic nucleic acid sequence. In some embodiments, the change to a native or genomic nucleic acid molecule includes but is not limited to: changes in the nucleic acid sequence due to degeneracy of the genetic code; nucleic acid sequence optimization per codon for 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; removal of one or more introns associated with the genomic nucleic acid sequence; c insertion of one or more heterologous introns; deletion of one or more upstream or downstream regulatory regions associated with the genomic nucleic acid sequence; insertion of one or more heterologous upstream or downstream regulatory regions; deletion of a 5' and / or 3' untranslated region associated with the genomic nucleic acid sequence; insertion of a heterologous 5' and / or 3' untranslated region; and modification of a polyadenylation site. In some embodiments, the non-genomic nucleic acid molecule is a cDNA. In some embodiments, the non-genomic nucleic acid molecule is a synthetic nucleic acid sequence. When appropriate, a nucleic acid can be optimized for increased expression in the host organism. Thus, when the host organism is a plant, synthetic nucleic acids can be synthesized through the use of plant-preferred codons for improved expression. See, for example, Campbell and Gowri (1990) Plant Physiol. 92:1-11 for a discussion of host-preferred codon usage. For example, although the nucleic acid sequences of the modalities can be expressed in both monocot and dicot plant species, the sequences can be modified to respond to specific codon preferences and GC content preferences of monocots or dicots because it has been shown that those preferences differ (Murray et al. (1989) Nucleic Acids Res. 17:477-498). Thus, the maize preference codon for a particular amino acid can be derived from known maize gene sequences. The codon usage in maize for the 28 maize plant genes is listed in Table 4 of Murray, et al., supra. Methods are available in the art for synthesizing plant-specific genes. See, for example, US Pat. num. 5,380,831, and 5,436,391 and Murray, et al., (1989) Nucleic Acids Res. 17:477-498, and Liu H et al. Mol Bio Rep 37:677-684, 2010, which are incorporated herein by reference. A table of codon usage for Zea maize can also be found at kazusa.or.jp / codon / cgi-bin / showcodon.cgi?species=4577, which you can access using the prefix “www”. A listing of Glycine max codon usage is shown in Table 3 and can also be found at kazusa.or.jp / codon / cgibin / showcodon.cgi?species=3847&aa=1&style=N, which can be accessed with the prefix www. The skilled artisan will further appreciate that changes can be introduced by mutating nucleic acid sequences to produce changes in the amino acid sequence of the encoded polypeptides, without altering the biological activity of the proteins. Therefore, variants of nucleic acid molecules can be created by introducing one or more nucleotide substitutions, additions, and / or deletions into the corresponding nucleic acid sequence described in the present description, such that one or more substitutions, additions, or Amino acid deletions are introduced into the encoded protein. Mutations can be introduced by conventional techniques, such as site-directed mutagenesis and PCR-mediated mutagenesis. Such variant nucleic acid sequences are further encompassed by the present disclosure. Naturally occurring allelic variants such as these can be identified using recognized molecular biology techniques, such as, for example, polymerase chain reaction (PCR) and hybridization techniques, as described in the present invention. c In some embodiments, the polynucleotide encoding the polypeptide of sec. with no. of ident.: 3, sec. with no. of ident.: 5, sec. with no. of ident.: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 23, sec. with no. of ident.: 25, sec. with no. of ident.: 27, sec. with no. of ident.: 29, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. from ident: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with no. ID:45 is a non-genomic nucleic acid sequence. Variant nucleotide sequences further include synthetically derived nucleotide sequences, such as those generated, for example, through the use of site-directed mutagenesis, but still encoding a pesticidal protein of the modalities, such as a mutant toxin. Generally, variants of a particular nucleotide sequence of the embodiments will be at least about 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or greater sequence identity to that particular nucleotide sequence as determined by sequence alignment programs described elsewhere in this disclosure with the use of default parameters. A variant of a nucleotide sequence of the embodiments may differ from that sequence by as low as 1-15 nucleotides, as low as 1-10, such as 6-10, as low as 5, as low as 4, 3 , 2 or even 1 nucleotide. Variants of a particular nucleotide sequence of the embodiments (i.e., an illustrative nucleotide sequence) can be further assessed by comparison of percent sequence identity between the polypeptide encoded by a nucleotide sequence variant and the polypeptide encoded by the reference nucleotide sequence. Thus, for example, isolated nucleic acids encoding a polypeptide with a given percent sequence identity to the polypeptides of sec. with no. of ident.: 3, sec. with no. of ident.: 5, sec. with no. of ident.: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 23, sec. with no. of ident.: 25, sec. with no. of ident.: 27, sec. with no. of ident.: 29, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. of ident.: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with no. ID: 45. Percent sequence identity between any two polypeptides can be calculated using sequence alignment programs described elsewhere in the present disclosure using predetermined parameters. When any given polynucleotide pair of the embodiments is evaluated by comparison of the percent sequence identity shared by the two polypeptides they encode, the percent sequence identity between the two encoded polypeptides is at least about 40%, 45%, 50% , 55%, 60%, 65%, 70%, generally, at least about 75%, 80%, 85%, at least about 90%, 91%, 92%, 93%, 94%, 95%, 96% , 97%, or at least about 98%, 99% or greater sequence identity. As used herein, the term "variant protein" encompasses polypeptides that are derived from a native protein by: deletion (called truncation) or addition of one or more amino acids to the N-terminus and / or C-terminus of the native protein; deletion or addition of one or more c amino acids at one or more sites in the native protein; or substitution of one or more amino acids at one or more sites in the native protein. Accordingly, the term "variant protein" encompasses biologically active fragments of a native protein that comprise a sufficient number of contiguous amino acid residues to retain the biological activity of the native protein, ie, to have pesticidal activity. Said pesticidal activity may be different from or may be higher than the native protein or may be unmodified, as long as the pesticidal activity is retained. The variant proteins encompassed by the modalities are biologically active, ie they still have the desired biological activity of the native protein, ie the pesticidal activity as described herein. Such variants can be produced, for example, from genetic polymorphism or from manipulation by a human. Biologically active variants of a native pesticidal protein of the modalities will be at least about 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91 %, 92%, %, 94%, 95%, 96%, 97%, 98%, 99% or more sequence identity to the amino acid sequence for the native protein as determined by sequence alignment programs described in other parts of this description with the use of default parameters. A biologically active variant of a protein of the modalities may differ from that protein by as low as 1-15 amino acid residues, as low as 1-10, such as 6-10, as low as 5, as low as 4 , 3, 2 or even 1 amino acid residue. In one embodiment, the insecticidal polypeptide is at least 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93 %, %, 95%, 96%, 97%, 98%, 99% or more sequence identity with c the amino acid sequence of sec. with no. of ident.: 3, sec. with no. of ident.: 5, sec. with no. of ident.: 7, sec. with no. of ident.: 9, sec. with no. of ident.: 11, sec. with no. of ident.: 13, sec. with no. of ident.: 15, sec. with no. of ident.: 17, sec. with no. of ident.: 19, sec. with no. of ident.: 21, sec. with no. of ident.: 23, sec. with no. of ident.: 25, sec. with no. of ident.: 27, sec. with no. of ident.: 29, sec. with no. of ident.: 31, sec. with no. of ident.: 33, sec. with no. of ident.: 35, sec. with no. of ident.: 37, sec. with no. of ident.: 39, sec. with no. of ident.: 41, sec. with no. of ident.: 43 or sec. with no. of ident.: 45. In some embodiments, the polypeptide has a modified physical property. As used in the present description, the term "physical property" refers to any suitable parameter to describe the physicochemical characteristics of a protein. As used herein, "physical property of interest" and "property of interest" are used, interchangeably, to refer to the physical properties of the proteins being investigated and / or modified. Examples of physical properties include, but are not limited to, net surface charge and charge distribution on the protein surface, net hydrophobicity and distribution of the hydrophobic residue on the protein surface, surface charge density, hydrophobicity density of surface, total count of ionizable groups on the surface, surface tension, protein size and its distribution in solution, melting temperature, heat capacity, and second virial coefficient. Additionally, examples of physical properties include, but are not limited to, solubility, folding, stability, and digestibility. In some embodiments, the polypeptide's ability to digest proteolytic fragments in the gut of an insect is enhanced. In some embodiments, the polypeptide has increased stability in the insect gut. c Models for digestion by simulated gastric fluids are known to those skilled in the art (Fuchs, R.L. and J.D. Astwood. Food Technology 50: 83-88, 1996; Astwood, J.D., et al Nature Biotechnology 14: 1269-1273, 1996 Fu TJ et al J. Agrie Food Chem. 50: 7154-7160, 2002). The embodiments further encompass a microorganism that is transformed with at least one nucleic acid of the embodiments, with an expression cassette comprising the nucleic acid, or with a vector comprising the expression cassette. In some embodiments, the microorganism multiplies in plants. One embodiment of the disclosure refers to an encapsulated pesticidal protein comprising a transformed microorganism capable of expressing at least one pesticidal protein of the embodiments. The embodiments provide pesticidal compositions comprising a microorganism transformed from the embodiments. In such embodiments, the transformed microorganism is generally present in the pesticidal composition in a pesticidally effective amount, together with a suitable carrier. The modalities further encompass pesticidal compositions comprising an isolated protein of the modalities, alone or in conjunction with a transformed organism of the modalities and / or an encapsulated pesticidal protein of the modalities, in an insecticidally effective amount, together with a carrier suitable. The embodiments further provide a method of increasing the target range of insects by using a pesticidal protein of the embodiments in conjunction with at least one other pesticidal protein or a "second" pesticidal protein. Any pesticidal protein known in the art can be used in the methods of the embodiments. Such pesticidal proteins include, but are not limited to, Bt toxins, protease inhibitors, α-amylases, and peroxidases. c The modalities further encompass transformed or transgenic plants comprising at least one nucleotide sequence of the modalities. In some embodiments, the plant is stably transformed with a nucleotide construct comprising at least one nucleotide sequence of the embodiments operatively linked to a promoter that drives expression in a plant cell. As used in the present description, the terms "transformed plant" and "transgenic plant" refer to a plant that comprises within its genome a heterologous polynucleotide. Generally, the heterologous polynucleotide is stably integrated into the genome of a transgenic or transformed plant such that the polynucleotide is passed on to successive generations. The heterologous polynucleotide could be integrated into the genome alone or as part of a recombinant expression cassette. It will be understood that, as used herein, the term "transgenic" includes any cell, cell line, callus, tissue, plant or plant part whose genotype has been altered by the presence of heterologous nucleic acid and includes those transgenic organisms initially altered in this way as well as those created by sexual interbreeding or asexual propagation from the initial transgenic event. As used herein, the term "transgenic" does not encompass genome alteration (chromosomal or extrachromosomal) by conventional plant breeding methods or by naturally occurring events, such as random cross-fertilization, non-recombinant viral infection, transformation nonrecombinant bacterial, nonrecombinant transposition, or spontaneous mutation. As used herein, the term "plant" includes whole plants, plant organs (eg, leaves, stems, roots, etc.), seeds, plant cells, and the progeny thereof. The parts of plants c Transgenic cells are within the scope of the modalities and include, for example, plant cells, plant protoplasts, plant cell tissue cultures from which plants can be regenerated, plant callus, plant clumps, and intact plant cells in the plants or parts of plants, such as embryos, pollen, ovules, seeds, leaves, flowers, branches, fruits, corn kernels, ears, ears, pods, stems, roots, root tips, anthers and the like, originating from in transgenic plants or their progeny previously transformed with a DNA molecule of the embodiments and therefore consisting at least in part of transgenic cells. Generally, the class of plants that can be used in the methods of the modalities is as broad as the class of higher plants that can be processed by transformation techniques, and includes monocotyledonous and dicotyledonous plants. Although the modalities do not rely on a particular biological mechanism to increase a plant's resistance to a plant pest, expression of the nucleotide sequences of the modalities in a plant can result in the production of the pesticidal proteins of the modalities and an increase in plant resistance to a plant pest. The plants of the modalities are useful in agriculture in methods to affect insect pests. Certain embodiments provide transformed crop plants, such as, for example, corn plants, useful in methods of affecting insect pests of plants, such as, for example, pests of the order Lepidoptera. A “subject plant or plant cell” is a plant or plant cell in which a genetic alteration, such as a transformation, has been affected, such as a gene of interest, or is a plant or plant cell descended from an altered plant or cell in this way and that includes the alteration. A “control”, c "control plant" or "control plant cell" provides a reference point for determining changes in the phenotype of the subject plant or plant cell. A control plant or plant cell may comprise, for example; (a) a wild-type plant or cell, that is, of the same genotype as the raw material for the genetic alteration that produced the subject plant or cell; (b) a plant or plant cell of the same genotype as the starting material but that has been transformed with a null construct (i.e., with a construct that has no known effect on the trait of interest, such as a construct comprising a marker gene); (c) a plant or plant cell that is an untransformed segregant into the progeny of a subject plant or plant cell; (d) a plant or plant cell genetically identical to the subject plant or plant cell but not exposed to conditions or stimuli that would induce expression of the gene of interest; or (e) the subject plant or plant cell themselves under conditions in which the gene of interest is not expressed. One of skill in the art will readily recognize that advances in the field of molecular biology, such as random and site-specific mutagenesis, polymerase chain reaction methods, and genetically engineered protein development techniques provide a comprehensive collection of suitable tools and protocols useful for altering or engineering both the amino acid sequence and the underlying protein genetic sequences of agricultural interest. Therefore, the proteins of the modalities can be altered in various ways including amino acid substitutions, deletions, truncations, and insertions. Methods for such manipulations are generally known in the art. For example, variant sequences of c Amino acids from pesticidal proteins can be prepared by introducing mutations into a synthetic nucleic acid (eg, DNA molecule). Methods for nucleic acid mutagenesis and alterations are well known in the art. For example, the designated changes can be introduced using an oligonucleotide-mediated site-directed mutagenesis technique. See, for example, Kunkel (1985) Proc. nati. Acad. Sci. USA 82:488-492; Kunkel et al. (1987) Methods in Enzymol. 154:367-382; US patent no. 4,873,192; Walker and Gaastra, eds. (1983) Techniques in Molecular Biology (MacMillan Publishing Company, New York) and references cited therein. The mutagenized nucleotide sequences of the embodiments can be modified to change approximately 1, 2, 3, 4, 5, 6, 8, 10, 12, or more of the amino acids present in the primary sequence of the encoded polypeptide. Alternatively, further changes to the native sequence can be introduced such that the encoded protein can be at least about 1% or 2% or about 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12% or even approximately 13%, 14%, 15%, 16%, 17%, 18%, 19% or 20%, 21%, 22%, 23%, 24% or 25%, 30%, 35% or 40% or more of the codons altered or otherwise modified compared to the corresponding wild-type protein. Likewise, the encoded protein can be at least about 1% or 2% or about 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12% or still about 13%, 14%, 15%, 16%, 17%, 18%, 19% or 20%, 21%, 22%, 23%, 24% or 25%, 30%, 35% or 40% or plus additional codons compared to the corresponding wild type protein. It is to be understood that the mutagenized nucleotide sequences of the embodiments are c intended to encompass biologically functional equivalent peptides having pesticidal activity, such as increased pesticidal activity as determined by antifeeding properties against European corn borer larvae. Such sequences may arise as a consequence of the codon redundancy and functional equivalence known to occur naturally within nucleic acid sequences and the proteins so encoded. One of skill in the art would recognize that amino acid additions and / or substitutions are generally based on the relative similarity of the amino acid side chain substituents, eg, their hydrophobicity, charge, size, and the like. Illustrative amino acid substitution groups that take into account various of the above features are well known to those skilled in the art and include: arginine and lysine; glutamate and aspartate; serine and threonine; glutamine and asparagine; and valine, leucine, and isoleucine. Guidance regarding appropriate amino acid substitutions that do not affect the biological activity of the protein of interest can be found in the model of Dayhoff et al. (1978) Atlas of Protein Sequence and Structure (Nati. Biomed. Res. Found., Washington, D.C.), incorporated herein by reference. Conservative substitutions can be made, such as exchanging one amino acid for another that has similar properties. Therefore, the genes and nucleotide sequences of the modalities include both the naturally occurring sequences and the mutant forms. Similarly, proteins of the modalities encompass both naturally occurring proteins and variations (eg, truncated polypeptides) and modified forms (eg, mutants) thereof. Such variants will still have the c desired pesticidal activity. Obviously, the mutations to be made in the nucleotide sequence encoding the variant must not place the sequence out of reading frame and generally will not create complementary regions that could produce secondary mRNA structure. See, EP patent application publication no. 75,444. Deletions, insertions and substitutions of the protein sequences covered in the present disclosure are not expected to cause radical changes in the characteristics of the protein. However, where it is difficult to predict the exact effect of the substitution, deletion or insertion before performing it, one of skill in the art will appreciate that the effect will be assessed by routine screening assays, such as insect feeding assays. See, for example, Marrone et al. (1985) J. Econ. Entomol. 78: 290-293 and Czapla and Lang (1990) J. Econ. Entomol. 83:2480-2485, incorporated herein by reference. Protein and nucleotide variant sequences further encompass sequences and proteins derived from a mutagenic and recombinogenic procedure such as DNA shuffling. With such a procedure, one or more different coding sequences can be manipulated to create a new pesticidal protein having the desired properties. In this manner, libraries of recombinant polynucleotides are generated from a population of sequence-related polynucleotides that comprise regions of sequences that have substantial sequence identity and that can be homologously recombined in vitro or in vivo. For example, using this method, full-length coding sequences, sequence motifs encoding a domain of interest, or any fragment of a nucleotide sequence of the modalities can be shuffled between the nucleotide sequences of the modalities and the corresponding portions of other known Cry nucleotide sequences to obtain encoding a new gene for a protein with an improved property of interest. Properties of interest include, but are not limited to, pesticidal activity per unit of pesticidal protein, stability of the protein, and toxicity to non-target species, particularly humans, livestock, and plants and microbes expressing the pesticidal polypeptides of the modalities. . The modalities are not limited to a particular shuffling strategy, only that at least one nucleotide sequence of the modalities or a part thereof is involved in said shuffling strategy. Shuffling may involve only nucleotide sequences described herein, or may additionally involve shuffling other nucleotide sequences known in the art. Strategies for DNA sequence shuffling are known in the art. See, for example, Stemmer (1994) Proc. nati. Acad. Sci. USA 91:10747-10751; Stemmer (1994) Nature 370:389-391; Crameri et al. (1997) Nature Biotech. 15:436-438; Moore et al. (1997) J. Mol. Biol. 272.33Q-347; Zhang et al. (1997) Proc. nati. Acad. Sci. USA 94:45044509; Crameri et al. (1998) Nature 391:288-291; and US Pat. Nos. 5,605,793 and 5,837,458. The nucleotide sequences of the embodiments can further be used to isolate corresponding sequences from other organisms, particularly other bacteria, and more particularly other Bacillus strains. Thus, methods such as PCR, hybridization, and the like can be used to identify such sequences based on their sequence homology to the sequences set forth herein. Sequences that are selected based on their sequence identity to the complete sequences set forth herein or fragments thereof are encompassed by the embodiments. Such sequences include sequences that are orthologous to the disclosed sequences. The term "orthologs" refers to genes derived from a common ancestral gene and found in different species as a result of speciation. Genes found in different species are considered orthologous when their nucleotide sequences and / or their encoded protein sequences share substantial identity as defined elsewhere in the present disclosure. Frequently, the functions of orthologs are very well conserved between species. In a PCR method, oligonucleotide primers can be designed for use in PCR reactions to amplify the corresponding DNA sequences from cDNA or genomic DNA that is extracted from any organism of interest. Methods for PCR primer design and PCR cloning are generally known in the art and are described in Sambrook et al. (1989) Molecular Cloning: A Laboratory Manual (2nd ed., Cold Spring Harbor Laboratory Press, Plainview, New York), hereinafter "Sambrook". See also Innis et al., eds. (1990) PCR Protocols: A Guide to Methods and Applications (Academic Press, New York); Innis and Gelfand, eds. (1995) PCR Strategies (Academic Press, New York); and Innis and Gelfand, eds. (1999) PCR Methods Manual (Academic Press, New York). Known PCR methods include, but are not limited to, methods using paired primers, nested primers, unique specific primers, degenerate primers, gene-specific primers, vector-specific primers, partially mismatched primers, and the like. Hybridization techniques use all or part of a nucleotide sequence known as a probe that selectively hybridizes to other corresponding nucleotide sequences present in a population of cloned genomic DNA fragments or cDNA fragments (i.e., genomic or genomic libraries). cDNA) from a selected organism. Hybridization probes can be genomic DNA fragments, cDNA fragments, RNA fragments, or other oligonucleotides and can be labeled with a detectable group, such as 32P or any other detectable marker. Thus, for example, hybridization probes can be prepared by labeling synthetic oligonucleotides based on the sequences of the modalities. Methods for the preparation of hybridization probes and for the construction of genomic and cDNA libraries are generally known in the art and are described in Sambrook. For example, an entire sequence described herein or one or more portions thereof can be used as a probe capable of specifically hybridizing to the corresponding sequences and messenger RNAs. To achieve specific hybridization under various conditions, such probes include sequences that are unique to the sequences of the modalities and are generally at least about 10 or 20 nucleotides in length. Such probes can be used to amplify the corresponding Cry sequences from a selected organism by PCR. This technique can be used to isolate additional coding sequences from a desired organism or as a diagnostic assay to determine the presence of coding sequences in an organism. Hybridization techniques include selection by hybridization of plate-grown DNA libraries (either on plates or colonies), see, for example, Sambrook. Hybridization of such sequences can be performed under stringent conditions. The terms "stringent conditions" or "stringent hybridization conditions" as used herein refer to conditions under which a probe will hybridize to its target sequence at a detectably higher level than to other sequences (eg ., at least 2-fold, 5-fold or 10-fold on background Stringent conditions are sequence dependent and will be different under different circumstances By controlling the stringency of hybridization and / or wash conditions, it is possible to identify sequences that are 100% complementary to the probe (homologous probing). Alternatively, stringent conditions can be adjusted to allow for some sequence mismatches so that lesser degrees of similarity are detected (heterologous probing). Generally, a probe has less than about 1,000 or 500 nucleotides in length. Typically, stringent conditions will be those where the salt concentration is less than about 1.5 M Na ions, typically with a concentration of about 0.01 to 1.0 M Na ions (or other salts) at a pH of 7.0 to 8.3 and a temperature of at least about 30°C for short probes (eg, 10 to 50 nucleotides) and at least about 60°C for long probes (eg. , greater than 50 nucleotides). Stringent conditions can also be obtained with the addition of destabilizing agents such as formamide. Illustrative low stringency conditions include hybridization with 30 to 35% formamide buffer, 1 M NaCI, 1% SDS (sodium dodecyl sulfate) at 37°C, and a wash in 1X to 2X SSC (SSC 20X = 3.0 M NaCI / 0.3 M trisodium citrate) at 50 to 55 °C. Illustrative moderate stringency conditions include hybridization in 40 to 45% formamide, 1.0 M NaCI, 1% of SDS at 37°C, and a wash in 0.5X to 1X SSC at 55 to 60°C. Illustrative high stringency conditions include hybridization in 50% formamide, 1 M NaCI, 1% SDS at 37°C, and a final wash in 0.1X SSC at 60 to 65°C for at least about 20 minutes. Optionally, the wash buffers can comprise about 0.1% to about 1% SDS. The duration of hybridization is generally less than about 24 hours, usually from about 4 to about 12 hours. The following terms are used to describe sequence relationships between two or more nucleic acids or polynucleotides: (a) “reference sequence”, (b) “comparison window”, (c) “sequence identity”, (d) "percent sequence identity" and (e) "substantial identity". (a) As used herein, "reference sequence" is a defined sequence that is used as the basis for sequence comparison. A reference sequence can be a subset or all of a specific sequence, for example, as a segment of a full-length cDNA or genetic sequence or the complete cDNA or genetic sequence. (b) As used herein, "comparison window" refers to a contiguous and specified segment of a polynucleotide sequence, wherein the comparison window polynucleotide sequence may comprise additions, or deletions (i.e., , breaks) compared to the reference sequence (comprising neither additions nor deletions) for optimal alignment of the two sequences. Generally, the comparison window is at least 20 contiguous nucleotides in length, and can optionally be 30, 40, 50, 100, or more. Those skilled in the art will understand that to avoid high similarity to a reference sequence due to the inclusion of breaks in the polynucleotide sequence, a break penalty is typically introduced and subtracted from the number of matches. Sequence alignment methods for comparison are well known in the art. Thus, determination of percent sequence identity between two sequences can be obtained using a mathematical algorithm. Non-limiting examples of these mathematical algorithms are the algorithm of Myers and Miller (1988) CABIOS 4:11-17; the local alignment algorithm of Smith et al. (1981) Adv. Appl. Math. 2:482; the global alignment algorithm of Needleman and Wunsch (1970) J. Mol. Biol. 48:443453; the local alignment search method of Pearson and Lipman (1988) Proc. nati. Acad. Sci. 85:2444-2448; the algorithm of Karlin and Altschul (1990) Proc. nati. Acad. Sci. USA 872264, modified as in Karlin and Altschul (1993) Proc. nati. Acad. Sci. USA 90:5873-5877. Computer implementations of these mathematical algorithms can be used to compare sequences and determine sequence identity. These implementations include, but are not limited to: CLUSTAL in the PC / Gene program (available from Intelligenetics, Mountain View, California); the ALIGN program (version 2.0) and GAP, BESTFIT, BLAST, FASTA, and TFASTA from the GCG Wisconsin Package for genetics, version 10 (available from Accelrys Inc., 9685 Scranton Road, San Diego, California, USA) . Alignments with these programs can be done with the default parameters. The CLUSTAL program is well described by Higgins et al. (1988) Gene 73:237-244 (1988); Higgins et al. (1989) CABIOS 5:151-153; Corpet et al. (1988) Nucleic Acids Res. 16:10881-90; Huang et al. (1992) CABIOS 8:155-65; and Pearson et al. (1994) Meth. Mol. Biol. 24:307-331. The ALIGN program is based on the Myers and Miller (1988) algorithm mentioned above. With the ALIGN program, a PAM120 weight residue table, a break length penalty of 12, and a break penalty of 4 can be used when comparing amino acid sequences. The BLAST programs of Altschul et al. (1990) J. Mol. Biol. 215:403 are based on the algorithm of Karlin and Altschul (1990) mentioned above. BLAST nucleotide searches can be performed with the BLASTN program, score=100, wordlength=12, to obtain nucleotide sequences homologous to a nucleotide sequence encoding a protein of the modalities. BLAST searches for proteins can be performed with the BLASTX program, score=50, wordlength=3, to obtain amino acid sequences homologous to a protein or polypeptide of the modalities. To obtain gap alignments for comparison purposes, Gapped BLAST (in BLAST 2.0) can be used, as described by Altschul et al. in. (1997) Nucleic Acids Res. 25:3389. Alternatively, PSI-BLAST (in BLAST 2.0) can be used to perform an iterative search that detects distant relationships between molecules. See Altschul et al. (1997) supra. When using BLAST, Gapped BLAST, PSIBLAST, it is possible to use the default parameters of the respective programs (eg, BLASTN for nucleotide sequences, BLASTX for proteins). See the National Center for Biotechnology Information website on the world wide web at ncbi.hlm.nih.gov. Alignment can also be done manually for inspection. (c) As used herein, "sequence identity" or "identity" in the context of two nucleic acid or polypeptide sequences refers to residues in the two sequences that are the same when aligned for maximal match in a specified comparison window. When percent sequence identity is used with reference to proteins, it is recognized that the positions of the Residues that are not identical often differ by conservative amino acid substitutions, where amino acid residues are replaced by other amino acid residues with similar chemical properties (eg, charge or hydrophobicity) and thus do not alter the functional properties of the molecule. When the sequences differ by conservative substitutions, the percent sequence identity can be adjusted upward to correct for the conservative nature of the substitution. Sequences that differ by such conservative substitutions are said to have "sequence similarity" or "similarity." Means for making this adjustment are well known to those skilled in the art. Typically, this requires scoring a conservative substitution as a partial rather than a complete mismatch, thereby increasing the percent sequence identity. Thus, for example, when a score of 1 is assigned to an identical amino acid and a score of 0 to a non-conservative substitution, a score between 0 and 1 is assigned to a conservative substitution. The conservative substitutions score is calculated, for example, as implemented in the PC / GENE program (Intelligenetics, Mountain View, California). (d) As used herein, "percent sequence identity" refers to the value determined by comparing two optimally aligned sequences in a comparison window, where the portion of the polynucleotide sequence in the comparison window may comprise additions or deletions (ie, breaks) compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. To calculate the percentage, determine the number of positions at which the identical nucleic acid base or amino acid residue occurs in the two sequences to obtain the number of matching positions, divide the total number of matching positions by the total number of positions in the comparison window and the result is multiplied by 100 to obtain the percent sequence identity. (e)(i) The term "substantial identity" of polynucleotide sequences means that a polynucleotide comprises a sequence that has at least 70%, 80%, 90%, or 95% or more sequence identity when compared to a sequence of reference with the use of the alignment programs described with the use of standard parameters. One of skill in the art will recognize that these values ​​can be appropriately adjusted to determine the identity of corresponding proteins encoded by two nucleotide sequences taking into account codon redundancy, amino acid similarity, reading frame positioning , and the like. Substantial amino acid sequence identity for these purposes generally means a sequence identity of at least 60%, 70%, 80%, 90%, or 95% or more. Another indication that nucleotide sequences are substantially identical is when two molecules hybridize to each other under stringent conditions. Generally, stringent conditions are selected to be approximately 5'C less than the Tm for the specific sequence at a defined ionic strength and pH. However, stringent conditions encompass temperatures ranging from about 1°C to about 20°C less than the Tm depending on the desired degree of stringency for the conditions, as otherwise qualified herein. Nucleic acids that do not hybridize to each other under stringent conditions are still substantially identical if the polypeptides they encode are substantially identical. This can occur, for example, when a copy of a nucleic acid is created by using the maximum codon redundancy allowed by the genetic code. An indication that two nucleic acid sequences are substantially identical is the case in which the polypeptide encoded by the first nucleic acid is immunologically cross-reactive with the polypeptide encoded by the second nucleic acid. (e)(ii) The term "substantial identity" in the context of a peptide indicates that a peptide comprises a sequence with at least 70%, 80%, 85%, 90%, 95% or more sequence identity with a reference sequence in a specified comparison window. Optimal alignment for these purposes can be accomplished with the use of the Needleman and Wunsch (1970) global alignment algorithm mentioned above. An indication that two peptide sequences are substantially identical is that one peptide is immunologically reactive with antibodies raised against the second peptide. Thus, a peptide is substantially identical to a second peptide, for example, when the two peptides differ by only one conservative substitution. Peptides that are "substantially similar" share sequence, as noted above, except that non-identical residue positions may differ by conservative amino acid changes. The use of the term "nucleotide constructs" in the present description is not intended to limit the modalities of nucleotide constructs that comprise DNA. Those of skill in the art will recognize that nucleotide constructs, particularly polynucleotides and oligonucleotides comprised of ribonucleotides and combinations of ribonucleotides and deoxyribonucleotides, may additionally be used in the methods described herein. The nucleotide constructs, nucleic acids, and nucleotide sequences of the embodiments include, furthermore, all complementary forms of such constructs, molecules, and sequences. In addition, the nucleotide constructs, nucleotide molecules, and nucleotide sequences of the embodiments include all nucleotide constructs, molecules, and sequences that can be used in the methods of the embodiments to transform plants including, but not limited to, those composed of deoxyribonucleotides, ribonucleotides, and combinations of these. Such deoxyribonucleotides and ribonucleotides include naturally occurring molecules and synthetic analogues. The nucleotide constructs, nucleic acids, and nucleotide sequences of the embodiments further include all forms of nucleotide constructs including, but not limited to, single-stranded forms, double-stranded forms, hairpins, stem-and-loop structures, and the like. . Another embodiment relates to a transformed organism, such as an organism selected from the group consisting of plant and insect cells, bacteria, yeast, baculovirus, protozoa, nematodes, and algae. The transformed organism comprises: a DNA molecule of the embodiments, an expression cassette comprising that DNA molecule, or a vector comprising that expression cassette, which can be stably incorporated into the genome of the transformed organism. The sequences of the modalities are provided in DNA constructs for expression in the organism of interest. The construct will include 5' and 3' regulatory sequences operatively 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, wherein the promoter sequence initiates and mediates transcription of the DNA sequence corresponding to the second sequence. Generally, "operably linked" means that the nucleic acid sequences being linked are contiguous and, where necessary, join two protein-coding regions, contiguous and in the same reading frame. The construct may further contain at least one additional gene for cotransformation in the organism. Alternatively, the additional gene(s) may be provided in multiple DNA constructs. A plurality of restriction sites are provided in the DNA construct for insertion of the Cry toxin sequence so that it is transcriptionally regulated by the regulatory regions. The DNA construct may additionally contain selectable marker genes. The DNA construct will include in the 5' to 3' direction of transcription: a transcriptional and translational initiation region (i.e., a promoter), a DNA sequence of the modalities, and a transcriptional and translational termination region (i.e., a termination region) functional in the host organism. The transcription initiation region (ie, the promoter) can be natural, analogous, foreign, or heterologous to the host organism and / or to the sequence of modalities. Additionally, the promoter can be the natural sequence or alternatively a synthetic sequence. The term "foreign", as used herein, indicates that the promoter is not found in the native organism into which the promoter is introduced. When the promoter is "foreign" or "heterologous" to the sequence of the modalities, it is meant that the promoter is not native or naturally occurring to the operably linked sequence of the modalities. As used herein, a chimeric gene comprises a coding sequence operatively linked to a transcription initiation region that is heterologous to the coding sequence. When the promoter is a native or wild-type sequence, expression of the operably linked sequence is altered from wild-type expression, resulting in an alteration in phenotype. The termination region may be native to the transcriptional initiation region, may be native to the operably linked DNA sequence of interest, may be native to the plant host, or may be derived from another source (i.e., foreign or heterologous to the promoter). , the sequence of interest, the host plant, or any combination of these). Suitable termination regions are available from the A. tumefaciens Ti plasmid, such as the octopine synthase and nopaline synthase termination regions. See also Guerineau et al. (1991) Mol. Gen. Genet. 262:141-144; Proudfoot (1991) Ce / / 64:671-674; Sanfacon et al. (1991) Genes Dev. 5:141-149; Mogen et al. (1990) Plant Cell 2:1261-1272; Munroe et al. (1990) Gene 91:151-158; Bailas et al. (1989) Nucleic Acids Res. 17:78917903; and Joshi et al. (1987) Nucleic Acid Res. 15:9627-9639. When appropriate, a nucleic acid can be optimized for increased expression in the host organism. Thus, when the host organism is a plant, synthetic nucleic acids can be synthesized using plant-preferred codons for enhanced expression. See, for example, Campbell and Gowri (1990) Plant Physiol. 92:1-11 for a discussion of host-preferred codon usage. For example, although the nucleic acid sequences of the modalities can be expressed in both monocot and dicot plant species, the sequences can be modified to respond to specific codon preferences and GC content preferences of monocots or dicots because it has been shown that those preferences differ (Murray et al. (1989) Nucleic Acids Res. 17:477-498). Thus, the maize preference codon for a particular amino acid can be derived from known maize gene sequences. The codon usage in maize for the 28 maize plant genes is listed in Table 4 of Murray et al., mentioned above. Methods are available in the art for synthesizing plant-specific genes. See, for example, US Pat. Nos. 5,380,831, and 5,436,391, and Murray et al. (1989) Nucleic Acids Res. 17:477-498, incorporated herein by reference. Additional sequence modifications are known to enhance gene expression in a cellular host. These include removal of sequences encoding false polyadenylation signals, exon-intron splice site signals, transposon-like repeats, and other highly characterized sequences that may be detrimental to gene expression. The GC content of the sequence can be adjusted to average levels for a specific host cell, calculated with reference to known genes expressed in the host cell. The term "host cell", as used in the present description, refers to a cell that contains a vector and supports the repetition and / or expression of the expression vector intended for it. The host cells may be prokaryotic cells, such as E. coli, or eukaryotic cells, such as yeast, insect, amphibian, or mammalian cells, or monocot or dicot plant cells. An example of a monocot host cell is a maize host cell. When possible, the sequence is modified to avoid the expected hairpin secondary structures of the mRNA. Expression cassettes may additionally contain 5' leader sequences. These leader sequences can act to enhance translation. Translational leader sequences are known in the art and include: picornavirus leaders, eg, EMCV leader (encephalomyocarditis 5' non-coding region) (Elroy-Stein et al. (1989) Proc. Nati. Acad. Sel. USA 86: c 6126-6130); potyvirus leaders, eg, TEV (tobacco etch virus) leader (Gallie et al. (1995) Gene 165(2): 233-238), MDMV (maize dwarf mosaic virus) leader, binding to human immunoglobulin heavy chain (BiP) (Macejak et al. (1991) Nature 353: 90-94); alfalfa mosaic virus mRNA coat protein untranslated leader (AMV RNA 4) (Jobling et al. (1987) Nature 325: 622-625); tobacco mosaic virus (TMV) leader (Gallie et al. (1989) in Molecular Biology of RNA, ed. Cech (Liss, New York), pp. 237-256); and the maize chlorotic mottle virus (MCMV) leader sequence (Lommel et al. (1991) VirOlogy 81:382385). See also Della-Cioppa et al. (1987) Plant Physioi. 84:965-968. In preparing the expression cassette, the various DNA fragments may be manipulated for the purpose of providing the DNA sequences with the proper orientation and, as appropriate, in the proper reading frame. For this purpose, adapters or linkers can be used to join the DNA fragments or other manipulations can be performed to provide suitable restriction sites, remove superfluous DNA, remove restriction sites, or the like. For this purpose, in vitro mutagenesis, primer repair, restriction, annealing, rearrangements, eg, transitions and transversions can be used. It is possible to use various promoters in the practice of the modalities. The promoters can be selected based on the desired result. The nucleic acids can be combined with constitutive, tissue-specific, inducible or other promoters for expression in the host organism. Constitutive promoters suitable for use in a plant cell host include, for example, the minimal promoter of the Rsyn7 promoter and other constitutive promoters described in US Pat. WO 99 / 43838 and in US patent no. 6,072,050; c min promoter 35S CaMV (Odell et al. (1985) Natura 313: 810-812); rice actin (McEIroy et al. (1990) Plant Cell 2: 163-171); ubiquitin (Christensen et al. (1989) Plant Mol. Biol. 12: 619-632 and Christensen et al. (1992) Plant Mol. Biol. 18: 675-689); pEMU (Last et al. (1991) Theor. Appl. Genet. 81: 581-588 ); MAS (Velten et al. (1984) EMBC J. 3:2723-2730 ); ALS promoter (US Patent No. 5,659,026), and the like. Other constitutive promoters include, for example, those described in US Pat. 5,608,149; 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 an inducible promoter. The injury-inducible promoters stand out for the regulation of the expression of the nucleotide sequences of the modalities in plants. Such injury-inducible promoters can respond to damage caused by insect feeding and include the potato proteinase inhibitor (pin II) gene (Ryan (1990) Ann. Rev. Phytopath. 28: 425-449; Duan et al. (1996) Nature Biotechnology 14: 494-498); wun1 and wun2, US patent no. 5,428,148; win1 and win2 (Stanford et al. (1989) Mol. Gen. Genet. 215:200-208); systemin (McGurl et al. (1992) Science 225: 1570-1573); WIP1 (Rohmeier et al. (1993) Plant Mol. Biol. 22: 783-792; Eckelkamp et al. (1993) FEBS Letters 323: 73-76); MPI gene ( Corderok et al. (1994) Plant J. 6(2): 141-150 ); and the like, incorporated herein by reference. Additionally, pathogen-inducible promoters can be used in the methods and nucleotide constructs of the embodiments. Such pathogen-inducible promoters include those from pathogenesis-related proteins (PR proteins) that are induced after infection by a pathogen, e.g. eg, PR proteins, SAR proteins, beta-1,3-glucanase, chitinase, etc. See, for example, Redolfi et al. (1983) Neth. J.Plant i c Pathol. 89:245-254; UKnes et al. (1992) Plant Cell 4: 645-656; and Van Loon (1985) Plant Mol. Virol. 4:111-116. See also patent no. WO 99 / 43819, incorporated herein by reference. Promoters that are expressed locally at or near the pathogen infection site are of interest. See, for example, Marineau et al. (1987) Plant Mol. Biol. 9:335-342; Matton et al. (1989) Molecular Plant Microbe Interactions 2:325-331; Somsisch et al. (1986) Proc. nati. Acad. Sci. USA 83:2427-2430; Somsisch et al. (1988) Mol. Gen. Genet. 2:93-98; and Yang (1996) Proc. nati. Acad. Sci. USA 93:14972-14977. See also Chen et al. (1996) Plant J. 10:955-966; Zhang et al. (1994) Proc. nati. Acad. Sci. USA 91:2507-2511; Warner et al. (1993) Plant J. 3:191-201; Siebertz et al. (1989) Plant Cell 1:961-968; US patent no. 5,750,386 (inducible by nematodes); and the references cited therein. Of particular interest is the inducible promoter for the maize PRms gene, the expression of which is induced by the pathogen Fusarium moniliforme (see, for example, Cordero, et al, (1992) Physiol. Mol. Plant Path. 41:189-200). . Chemically regulated promoters can be used to modulate the expression of a gene in a plant through the application of an exogenous chemical regulator. Depending on the purpose, the promoter may be a chemical-inducible promoter, where application of the chemical induces gene expression, or a chemical-repressed promoter, where application of the chemical represses gene expression. Chemically inducible promoters are known in the art and include, but are not limited to, the maize ln2-2 promoter, which is activated by benzenesulfonamide herbicidal protectants, the maize GST promoter, which is activated by electrophilic hydrophobic compounds used as pre-emergent herbicides and the tobacco PR-1a promoter, which is activated by salicylic acid. Other chemically regulated promoters of interest include spheroid-responsive promoters (see, for example, the glucocorticoid-inducible promoter in Schena et al. (1991) Proc. Nati. Acad. Sci. USA 88:10421-10425 and McNellis et al (1998) Plant J. 14(2):247-257) and tetracycline-inducible and tetracycline-repressible promoters (see, for example, Gatz et al. (1991) Mol. Gen. Genet. 227:229 -237 and US Patent Nos. 5,814,618 and 5,789,156), incorporated herein by reference. Tissue-preferred promoters can be used to direct expression of the improved pesticidal protein within a particular plant tissue. Tissue preferred promoters include those described in Yamamoto et al. (1997) Plant J. 12(2)255-265; Kawamata et al. (1997) Plant Cell Physiol. 38(7)792-803; Hansen et al. (1997) Mol. Gene Genet. 254(3):337-343; Russell et al. (1997) Transgenic Res. 6(2): 157-168; Rinehart et al. (1996) Plant Physiol. 112(3): 1331-1341; VanCamp et al. (1996) Plant Physiol. 112(2):525535; Canevascini et al. (1996) Plant Physiol. 112(2):513-524; Yamamoto et al. (1994) Plant Cell Physiol. 35(5)773-778; Lam (1994) Results Probl. Cell Differ. 20:181-196; Orozco et al. (1993) Plant Mol Biol. 23(6): 1129-1138; Matsuoka et al. (1993) Proc Nati. Acad. Sci. USA 90(20):9586-9590; and Guevara-Garcia et al. (1993) Plant J. 4(3):495-505. If necessary, such promoters can be modified for weak expression. Leaf-specific promoters are known in the art. See, for example, Yamamoto et al. (1997) Plant J. 12(2):255-265; Kwon et al. (1994) Plant Physiol. 105:357-67; Yamamoto et al. (1994) Plant Cell Physiol. 35(5)773-778; Gotor et al. (1993) Plant J. 3:509-18; Orozco et al. (1993)c Plant Mol. Biol. 23(6):1129-1138; and Matsuoka et al. (1993) Proc. nati. Acad. Sci. USA 90(20):9586-9590. Root-preferential or root-specific promoters are known and can be selected from the many available in the literature or isolated de novo from various compatible species. See, for example, Hire et al. (1992) Plant Mol. Biol. 20(2):207-218 (soybean-specific glutamine synthetase gene); Keller and Baumgartner, (1991) Plant Cell 3(10):10511061 (root-specific control element in green bean GRP 1.8 gene); Sanger, et al., (1990) Plant Mol. Biol. 14(3):433-443 (root-specific promoter of the Agrobacterium tumefaciens mannopine synthase (MAS) gene); and Miao et al. (1991) Plant Cell 3(1):11-22 (full-length cDNA clone encoding cytosolic glutamine synthetase (GS), which is expressed in soybean roots and root nodules). See also Bogusz et al. (1990) Plant Cell 2(7):633-641, describing two root-specific promoters isolated from hemoglobin genes of the nitrogen-fixing non-legume Parasponia andersonii and the related non-nitrogen-fixing non-legume Trema tomentosa . The promoters of these genes were linked to a β-glucuronidase reporter gene and introduced into the non-legume Nicotiana tabacum and the legume Lotus comiculatus, and in both examples root-specific promoter activity was preserved. Leach and Aoyagl (1991) describe their analysis of the promoters of the highly expressed root-inducing genes rolC and roID from Agrobacterium rhizogenes (see Plant Science (Limerick) 79(1):69-76). They concluded that the enhancer and tissue-specific DNA determinants dissociate at these promoters. Teeri et al. (1989) used gene fusion to lacZ to show that the Agrobacterium T-DNA gene encoding octopine synthase is especially active in the epidermis of the root tip and that the TR2' gene is root-specific in the epidermis of the root. intact plant and is stimulated by leaf tissue damage, a combination of traits especially desirable for use with an insecticidal or larvicidal gene (see EMBO J. 8(2):343-350). The TRT gene, fused to nptll (neomycin phosphotransferase II), presented similar characteristics. Additional root-specific promoters include the VIENOD-GRP3 gene promoter (Kuster et al. (1995) Plant Mol. Biol. 29(4)759-772); and the rolB promoter (Capana et al. (1994) Plant Mol. Biol. 25(4):681-691. See also US Patent Nos. 5,837,876; 5,750,386; 5,633. 363; 5,459,252; 5,401,836; 5,110,732; and 5,023,179. "Seed-preferred" promoters include both "seed-specific" promoters (promoters active during seed development, such as seed storage protein promoters) as well as "seed germination" promoters (promoters active during seed development). during seed germination). See Thompson et al. (1989) BioEssays 10:108, incorporated herein by reference. Such seed-preferred promoters include, but are not limited to, Cim1 (cytokinin-induced message); cZ19B1 (19 kDa corn zein); and milps (myo-inositol-1-phosphate synthase) (see, US Patent No. 6,225,529 incorporated herein by reference). Gamma-zein and Glob-1 are endosperm-specific promoters. For dicot plants, seed-specific promoters include, but are not limited to, bean β-phaseolin, napin, β-conglycinin, soybean lectin, cruciferin, and the like. For monocot plants, seed-specific promoters include, but are not limited to, maize 15 kDa zein, kDa, zein 27 kDa, g-zein, waxy, shrunken 1, shrunken 2, globulin 1, etc. See also patent no. WO 00 / 12733, describing seed preferential promoters from the end1 and end2 genes, incorporated herein by reference. A promoter that has "preferred" expression in a particular tissue is expressed in that tissue to a greater degree than in at least one other plant tissue. Some tissue preferred promoters show expression almost exclusively in the particular tissue. Where low level expression is desired, weak promoters will be used. Generally, the term "weak promoter" as used herein refers to a promoter that drives expression of a coding sequence at a low level. By low level expression levels are planned from about 1 / 1000 transcripts to about 1 / 100,000 transcripts to about 1 / 500,000 transcripts. Alternatively, the term "weak promoters" is recognized to further encompass promoters that drive expression in only a few cells and not in others, to give a low overall level of expression. When a promoter drives expression to unacceptably high levels, portions of the promoter sequence can be removed or modified to lower expression levels. Such weak constitutive promoters include, for example, the minimal promoter of the Rsyn7 promoter (Patent No. WO 99 / 43,838 and US Patent No. 6,072,050), the 35S CaMV minimal promoter, and the like. Other constitutive promoters include, for example, those described in US Pat. 5,608,149; 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, which are incorporated herein by reference. c Generally, the expression cassette will further comprise a transformed cell selection marker gene. Selection marker genes are used for the selection of transformed cells or tissues. Marker genes include genes that code for resistance to antibiotics, such as those for neomycin phosphotransferase II (NEO) and hygromycin phosphotransferase (HPT), as well as genes that confer resistance to herbicidal compounds, such as glufosinate ammonium, bromoxynil, imidazolinones and 2,4-dichlorophenoxyacetate (2,4-D). Additional examples of suitable selection marker genes include, but are not limited to, genes encoding chloramphenicol resistance (Herrera Estrella et al. (1983) EMBO J. 2:987-992); methotrexate (Herrera Estrella ef al. (1983) Nature 303:209-213; and Meijer et al. (1991) Plant Mol. Biol. 16:807-820); streptomycin (Jones et al. (1987) Mol. Gen. Genet. 210:86-91); spectinomycin (Bretagne-Sagnard et al. (1996) Transgenic Res. 5:131-137); bleomycin (Hille et al. (1990) Plant Mol. Biol. 7:171-176); sulfonamide (Guerineau et al. (1990) Plant Mol. Biol. 15:127-136); bromoxynil (Stalker et al. (1988) Science 242:419-423); glyphosate (Shaw et al. (1986) Science 233:478-481; and US Patent Nos. 7,709,702; and 7,462,481); phosphinothricin (DeBlock et al. (1987) EMBO J. 6:2513-2518). See generally Yarranton (1992) Curr. Opinion. Biotech. 3:506-511; Christopherson et al. (1992) Proc. nati. Acad. Sci. USA 89: 6314-6318; Yao et al. (1992) Ce / / 71: 63-72; Reznikoff (1992) Mol. Microbiol. 6:2419-2422; Barkley et al. (1980) in The Operon, pp. 177220; Hu et al. (1987) Ce / / 48: 555-566; Brown et al. (1987) Ce / / 49: 603612; Figge et al. (1988) Cell 52: 713-722; Deutschle et al. (1989) Proc. nati. Acad. Sci. USA 86: 5400-5404; Fuerst et al. (1989) Proc. nati. Acad. Sci. USA 86: 2549-2553; Deutschle et al. (1990) Science 248: 480-483; gossen c (1993) Ph.D. Thesis, University of Heidelberg; Reines et al. (1993) Proc. nati. Acad. Sci. USA 90: 1917-1921; Labow et al. (1990) Mol. Cell. Biol. 10: 3343-3356; Zambretti et al. (1992) Proc. nati. Acad. Sci. USA 89: 39523956; Baim et al. (1991) Proc. nati. Acad. Sci. USA 88: 5072-5076; Wyborski et al. (1991) Nucleic Acids Res. 19: 4647-4653; Hillen and Wissman (1989) Topics Mol. struc. Biol. 10: 143-162; Degenkolb et al. (1991) Antimicrob. Agents Chemother. 35: 1591-1595; Kleinschnidt et al. (1988) Biochemistry 27: 1094-1104; Bonin (1993) Ph.D. Thesis, University of Heidelberg; Gossen et al. (1992) Proc. nati. Acad. Sci. USA 89: 55475551; Olive et al. (1992) Antimicrob. Agents Chemother. 36:913-919; Hlavka et al. (1985) Handbook of Experimental Pharmacology, Vol. 78 (Springer-Verlag, Berlin); and Gili et al. (1988) Nature 334: 721-724. These descriptions are incorporated herein by reference. The above list of selectable marker genes is not exclusive. Any selectable marker gene can be used in the modalities. Methods of the embodiments include introducing a polypeptide or polynucleotide into a plant. "Introducing" means presenting the polynucleotide or polypeptide to the plant in such a way that the sequence gains access into the interior of a plant cell. The methods of the embodiments do not depend on a particular method of introducing a polynucleotide or polypeptide into a plant, only that the polynucleotide or polypeptide gain access into the interior of at least one cell of the plant. Methods for introducing polynucleotides or polypeptides into plants are known in the art and include, but are not limited to, stable transformation methods, transient transformation methods, and virus-mediated methods. "Stable transformation" refers to the fact that the nucleotide construct introduced into a plant integrates into the plant's genome and has the c ability to be inherited by its progeny. "Transient transformation" means that a polynucleotide is introduced into the plant and does not integrate into the plant's genome or a polypeptide is introduced into the plant. Transformation protocols, as well as protocols for introducing nucleotide sequences into plants, may vary depending on the type of plant or plant cell, ie, monocot or dicot, targeted for transformation. Suitable methods for the introduction of nucleotide sequences into plant cells and subsequent insertion into the plant genome include microinjection (Crossway et al. (1986) Biotechniques 4: 320-334), electroporation (Riggs et al. (1986) Proc. Nati. Acad. Sci. USA 83: 5602-5606), Agrobacterium-mediated transformation (US Patent Nos. 5,563,055 and 5,981,840), direct gene transfer (Paszkowski et al. (1984 ) EMBO J. 3: 2717-2722), and particle acceleration with bioballistics techniques (see, e.g., US Patent Nos. 4,945,050; 5,879,918; 5,886,244; and 5,932,782, Tomes et al (1995) in Plant Cell, Tissue, and Organ Culture: Fundamental Methods, ed Gamborg and Phillips (Springer-Verlag, Berlin), and McCabe et al (1988) Biotechnology 6: 923- 926); and Lecl transformation (WO 00 / 28058). For transformation into potato see Tu et al. (1998) Plant Molecular Biology 37: 829-838 and Chong et al. (2000) Transgenic Research 9: 71-78. Other transformation procedures can be found in Weissinger et al. (1988) Ann. Rev. Genet. 22:421-477; Sanford et al. (1987) Particulate Science and Technology 5: 27-37 (onion); Christou et al. (1988) Plant Physiol. Q7: 671-674 (soybean); McCabe et al. (1988) Bio / Technology 6: 923-926 (soybean); Finer and McMullen (1991) In Vitro Cell Dev. Biol. 27P: 175-182 (soybean); Singh et al. (1998) Theor. Appl. Genet. 96: 319-324 (soybean); Datta et al. (1990) Biotechnology 8: 736-740 (rice); Klein et al. (1988) Proc. nati. c Acad. Sci. USA 85: 4305-4309 (corn); Klein et al. (1988) Biotechnology 6:559-563 (corn); US patents no. 5,240,855, 5,322,783 and 5,324,646; Klein et al. (1988) Plant Physiol. 91: 440-444 (corn); Fromm et al. (1990) Biotechnology 8: 833-839 (corn); Hooykaas-Van Slogteren et al. (1984) Nature (London) 311: 763-764; US patent no. 5,736,369 (cereals); Bytebier et al. (1987) Proc. nati. Acad. Sci. USA 84: 5345-5349 (Liliaceae); De Wet et al. (1985) in The Experimental Manipulation of Ovule Tissues, ed. Chapman et al. (Longman, New York), pp. 197-209 (pollen); Kaeppler et al. (1990) Plant Cell Reports 9: 415-418 and Kaeppler et al. (1992) Theor. Appl. Genet. 84: 560-566 (ceramic fiber-mediated transformation); D'Halluin et al. (1992) Plant Cell A: 1495-1505 (electroporation); Li et al. (1993) Plant Cell Reports 12: 250-255 and Christou and Ford (1995) Annals of Botany 75: 407-413 (rice); Osjoda et al. (1996) Nature Biotechnology 14: 745-750 (corn via Agrobacterium tumefaciens); all incorporated herein by reference. In specific embodiments, the sequences of the embodiments can be provided to a plant using a variety of transient transformation methods. Such transient transformation methods include, but are not limited to, introduction of the Cry toxin protein or variants and fragments thereof directly into the plant or introduction of the Cry toxin transcript into the plant. Such methods include, for example, microinjection or particle bombardment. See, for example, Crossway et al. (1986) Mol Gen. Genet. 202: 179-185; Nomura et al. (1986) Plant Sci. 44: 5358; Hepler et al. (1994) Proc. nati. Acad. Sci. 91: 2176-2180 and Hush et al. (1994) The Journal of Cell Science 107: 775-784, incorporated herein by reference. Alternatively, the Cry toxin polynucleotide can be temporarily transformed in the plant using c techniques. known in the art. These techniques include the viral vector system and precipitation of the polynucleotide in a manner that precludes subsequent release of the DNA. Therefore, transcription from particle-bound DNA can occur, but the frequency with which it is released for integration into the genome is greatly reduced. These methods include the use of polyethylimine (PEI; Sigma #P3143) coated particles. Methods for the targeted insertion of a polynucleotide into a specific site in the plant genome are known in the art. In one embodiment, insertion of the polynucleotide into a desired genomic site is accomplished through the use of a site-specific recombination system. See, for example, patents no. WO99 / 25821, WO99 / 25854, WO99 / 25840, WO99 / 25855 and WO99 / 25853, incorporated herein by reference. Briefly, the polynucleotide of the embodiments may be contained in the transfer cassette flanked by two non-identical recombination sites. The transfer cassette is introduced into a plant that has a target site stably incorporated into its genome flanked by two non-identical recombination sites corresponding to the sites on the transfer cassette. An appropriate recombinase is provided and the transfer cassette is integrated into the target site. In this way, the polynucleotide of interest integrates into a specific chromosomal position in the plant genome. Cells that have been transformed can be grown into plants according to conventional methods. See, for example, McCormick et al. (1986) Plant Cell Reports 5. 81-84. These plants can then be grown and pollinated with either the same transformed strain or with different strains, and the resulting hybrid has constitutive or inducible expression of the identified desired phenotypic characteristic. May two or more generations should be grown to ensure that the expression of the desired phenotypic characteristic is maintained and stably inherited, and then the seeds are harvested to ensure that the expression of the desired phenotypic characteristic has been achieved. The nucleotide sequences of the embodiments can be provided to the plant by contacting the plant with a virus or viral nucleic acids. Generally, such methods involve incorporating the nucleotide construct of interest into a viral DNA or RNA molecule. It is recognized that recombinant proteins of the modalities can be initially synthesized as part of a viral polyprotein which can then be processed by proteolysis in vivo or in vitro to produce the desired pesticidal polypeptide. It is further recognized that such a viral polyprotein, comprising at least a portion of the amino acid sequence of the pesticidal protein of the embodiments, may have the desired pesticidal activity. Such viral polyproteins and the nucleotide sequences encoding them are encompassed by the embodiments. Methods for providing plants with nucleotide constructs and producing the encoded proteins in plants involve viral DNA or RNA molecules known in the art. See, for example, US Pat. Nos. 5,889,191; 5,889,190; 5,866,785; 5,589,367 and 5,316,931, incorporated herein by reference. Modalities further refer to plant propagation material of a transformed plant of modalities including, but not limited to, seeds, tubers, corms, bulbs, leaves, and root and shoot clippings. The modalities can be used for the transformation of any plant species, including, but not limited to, monocots and dicots. Examples of plant species of interest include, but not limited to, corn (Zea mays), Brassica sp. (eg, B. napus, B. rapa, B. júncea), particularly those of Brassica species useful as sources of seed oil, alfalfa (Medicago sativa), rice (Oryza sativa), rye (Secale cereale ), sorghum (Sorghum bicolor, Sorghum vulgare), millet (eg, pearl millet (Pennisetum glaucum), proso millet (Panicum miliaceum), foxtail millet (Setaria italica), African millet (Eleusine coracana)), sunflower (Helianthus annuus), safflower (Carthamus tinctorius), wheat (Triticum aestivum), soybean (Glycine max), tobacco (Nicotiana tabacum), potato (Solanum tuberosum), peanut (Arachis hypogaea), cotton (Gossypium barbadense, Gossypium hirsutum), sweet potato (Ipomoea batatus), cassava (Manihot esculenta), coffee (Coffea spp.), coconut (Cocos nucífera), pineapple (Ananas comosus), citrus trees (Citrus spp.), cocoa (Theobroma cacao), tea (Camellia sinensis) , banana (Musa spp.), avocado (Persea americana), fig (Ficus casica), guava (Psidium guajava), mango (Mangifera indica), olive (Olea europaea), papaya (Carica p apaya), cashew (Anacardium occidentale), macadamia (Macadamia integrifolia), almond (Prunus amygdalus), sugar beet (Beta vulgaris), sugar cane (Saccharum spp.), oats, barley, vegetables, ornamentals and conifers. Vegetables include tomatoes (Lycopersicon esculentum), lettuce (eg, Lactuca sativa), green beans (Phaseolus vulgaris), broad beans (Phaseolus limensis), peas (Lathyrus spp.), and members of the Cucumis genus such as cucumber (C . sativus), cantaloupe (C. cantaiupensis), and musk melon (C. meló). Ornamental plants include azalea (Rhododendron spp.), hydrangea (Macrophylla hydrangea), Chinese rose (Hibiscus rosasanensis), roses (Rosa spp.), tulips (Tulipa spp.), daffodils (Narcissus spp.), petunias (Petunia hybrida) , carnation (Dianthus c caryophyllus), federal star (Euphorbia pulcherrima) and chrysanthemum. Conifers that can be used to implement the modalities include, for example, pines such as grand pine (Pinus taeda), slash pine (Pinus elliotii), ponderosa pine (Pinus ponderosa), lodgepole pine (Pinus contorta), and Monterey pine. (Pinus radiata); Douglas-fir (Pseudotsuga menziesii); western hemlock (Tsuga canadensis); Sitka spruce (Picea glauca)', redwood (Sequoia sempervirens); true firs such as silver fir (Abies amabilis) and Canada fir (Abies balsamea); and cedars such as western red cedar (Thuja plicata) and Alaskan yellow cedar (Chamaecyparis nootkatensis). Plants of the embodiments include crop plants, including, but not limited to: corn, alfalfa, sunflower, Brassica spp, soybean, cotton, safflower, peanut, sorghum, wheat, millet, tobacco, sugarcane, etc. Grasses include, but are not limited to: spikelet (Poa annua); Italian vallico (Lolium multiflorum); bluegreengrass (Poa compressa); chewing fescue (Festuca rubra); common bentgrass (Agrostis tenuis); creeping bentgrass (Agrostis palustris); desert wheatgrass (Agropyron desertorum); crested wheatgrass (Agropyron cristatum); hard fescue (Festuca longifolia); grass poa (Poa pratensis); orchard grass (Dactylis glomerata); English vallico (Lolium perenne); red fescue (Festuca rubra); little castles (Agrostis alba); common poa (Poa trivialis); sheep fescue (Festuca ovina); inerme bromine (Bromus inermis); tall fescue (Festuca arundinacea); timothy of the meadows (Phleum pratense); canine bentgrass (Agrostis canina); alkaline tearsweed (Puccinellia distans); western wheatgrass (Agropyron smithii); Bermuda grass (Cynodon spp.); St. Augustine's wort (Stenotaphrum secundatum); zoysia grass (Zoysia spp.); Bay grass (Paspalum notatum); Brazilian grass (Axonopus affinis); grass centipede (Eremochloa ophiuroides); Kikuyu grass (Pennisetum clandestinum); seagrass (Paspalum vaginatum); bluegrass (Bouteioua gracilis); buffalo grass (Buchloe dactyloids); banderilla grass (Bouteioua curtipendula). Plants of interest include cereal plants that provide seeds of interest, oilseed plants, and leguminous plants. Seeds of interest include cereal seeds, such as corn, wheat, barley, rice, sorghum, rye, millet, etc. Oilseed plants include cotton, soybean, safflower, sunflower, Brassica, corn, alfalfa, palm, coconut, flax, castor, olive etc. Leguminous plants include beans and peas. Beans include guar, carob, fenugreek, soybean, garden bean, cowpea, soybean sprout, lima bean, broad bean, lentil, garbanzo, etc. In certain embodiments, the nucleic acid sequences of the embodiments can be stacked with any combination of polynucleotide sequences of interest to create plants with a desired phenotype. For example, the polynucleotides of the embodiments can be stacked with certain other polynucleotides encoding polypeptides that have pesticidal and / or insecticidal activity, such as other Bt toxic proteins (described in US Pat. Nos. 5,366,892; 5,747,450, 5,736,514, 5,723,756, 5,593,881, and Geiser et al (1986) Gene 48:109), pentin (described in US Patent No. 5,981,722) and the similar. Generated combinations can further include multiple copies of any of the polynucleotides of interest. The polynucleotides of the embodiments can be stacked with any other gene or combination of genes to produce plants with various combinations of desired traits including, but not limited to, traits desired for animal feeding, such as high oil genes (p eg, US Patent No. 6,232,529); balanced amino acids (eg, c hordothionins (US Patent Nos. 5,990,389, 5,885,801, 5,885,802, and 5,703,049); high lysine barley (Williamson et al. (1987) Eur. J. Biochem. 165: 99-106; and patent no. WO 98 / 20122) and high metlonin protein (Pedersen et al. (1986 ) J Biol Chem 261:6279, Kirlhara et al (1988) Gene 71:359 and Musumura et al (1989) Plant Mol Biol 12:123)); increased digestibility (eg, modified storage proteins (US Patent 6,858,778); and thioredoxins (US Patent 7,009,087), the disclosures of which are incorporated herein as reference. The polynucleotides of the modalities can be further stacked with desirable traits for disease or herbicide resistance (eg, fumonisin detoxification genes (US Pat. No. 5,792,931); avirulence genes and disease resistance (Jones et al. (1994) Science 266:789; Martin ef al. (1993) Science 262: 1432; and Mindrinos ef al. (1994) Ce / / 78:1089); acetolactate synthase mutants ( ALS) leading to resistance to herbicides such as S4 and / or Hra mutations, glutamine synthase inhibitors such as phosphinothricin or basta (eg, bar gene), and glyphosate resistance (EPPSS gene and GAT gene such as described in US Patent Nos. 7,709,702 and 7,462,481, and desirable traits for processing or process products such as high oil content products (eg, US Patent U.S. No. 6,232,529);modified oils (eg, fatty acid desaturase genes (U.S. Patent No. 5,952,544; WO 94 / 11516)); modified starches (eg, ADPG pyrophosphollases (AGPase), starch synthase (SS), starch branching enzymes (SBEs), and starch debranching enzymes (SDBEs)), and polymers or bioplastics (eg, US patent No. 5,602,321, betac ketothiolase, polyhydroxybutyrate synthase, and acetoacetyl-CoA reductase (Schubert et al. (1988) J. Bacteriol. 170: 5837-5847) which facilitate the expression of polyhydroxyalkanoates (PHAs)), the disclosures of which are incorporated herein by reference. In addition, polynucleotides of the embodiments can be combined with polynucleotides that provide agronomic traits, such as male sterility (see, for example, US Patent No. 5,583,210), stem strength, flowering time, or traits transformation technologies, such as cell cycle regulation or gene selection (eg, Patent Nos. WO 99 / 61619; WO 00 / 17364; WO 99 / 25821); the descriptions of which are incorporated herein by reference. In some embodiment, the grouped trait may be a regulatory-approved trait or event that is well known to a person with expertise in the art and can be found at the Center for Environmental Risk Assessment (ceragmc.org / ?action=gm_crop_database, a which can be accessed on the Internet with the prefix www) and at the International Service for the Acquisition of Agri-Biotech Applications (isaaa.org / gmapprovaldatabase / default.asp, which can be accessed on the Internet with the prefix prefix). These pooled combinations can be created by any of the methods including, but not limited to, insemination of plants by any conventional or TOPCROSS® methodology or by genetic transformation. If the traits are stacked by genetic transformation of plants, the polynucleotide sequences of interest can be combined at any time and in any order. For example, a transgenic plant comprising one or more desired traits can be used as the target to introduce additional traits by subsequent transformation. The traits can c simultaneously introduced into a co-transformation protocol with polynucleotides of interest provided by any combination of transformation cassettes. For example, if two sequences are to be introduced, the two sequences may be contained in separate (trans) transformation cassettes or in the same (cis) transformation cassette. Expression of the sequences may be controlled by the same promoter or by different promoters. In certain cases it may be desirable to introduce a transformation cassette that will abolish expression of the polynucleotide of interest. This can be combined with any combination of other deletion or overexpression cassettes to generate the desired combination of traits in the plant. Furthermore, it is recognized that polynucleotide sequences can be stacked at a desired genomic site by means of a site-specific recombination system. See, for example, patents no. WO99 / 25821, WO99 / 25854, WO99 / 25840, WO99 / 25855 and WO99 / 25853, incorporated herein by reference. Compositions of the embodiments are useful for protecting plants, seeds, and plant products in various forms. For example, the compositions can be used in a method that involves placing an effective amount of the pesticidal composition into the pest's environment by a method selected from the group consisting of spraying, dusting, broadcasting, or seed coating. Before marketing the propagation material of the plant (fruit, tuber, bulb, corm, grains, seed), but especially the seed, as a commercial product, it is usually treated with a protective coating that includes herbicides, insecticides, fungicides, bactericides, nematicides, molluscicides, or mixtures of several of these preparations, if desired, together with other carriers, surfactants, or promoter adjuvants c of application used in the formulation subject matter to provide protection against damage caused by bacterial, fungal or animal pests. To treat the seed, the protective coating can be applied to the seeds by soaking the tubers or kernels with a liquid formulation or by coating them with a combined wet or dry formulation. In addition, in special cases, other application methods on the plants are possible, for example, treatment directed at the buds or the fruit. The seed of the plant of the embodiments comprising a nucleotide sequence encoding a pesticidal protein of the embodiments may be treated with a protective seed coating comprising a seed treatment compound, such as, for example, captan, carboxin , thiram, metalaxyl, pirimiphos-methyl and others commonly used in seed treatment. In one embodiment, a seed coating comprising a pesticidal composition of the embodiments is used alone or in conjunction with one or more seed coatings commonly used in seed treatment. It is recognized that genes encoding pesticidal proteins can be used to transform insect pathogenic organisms. Such organisms include baculoviruses, fungi, protozoa, bacteria, and nematodes. A gene encoding a pesticidal protein of the embodiments can be introduced via a suitable vector into a microbial host and that host applied to the environment or to plants or animals. The term "introduced", in the context of the insertion of a nucleic acid into a cell, means "transfection" or "transformation" or "transduction" and includes reference to the incorporation of a nucleic acid into a eukaryotic or prokaryotic cell, wherein the nucleic acid can be incorporated into the genome of the cell (eg, c chromosome, plasmid, plastid, or mitochondrial DNA), converted to an autonomous replicon, or transiently expressed (eg, transfected mRNA). Host microorganisms known to occupy the "phytosphere" (phylloplane, phyllosphere, rhizosphere, and / or rhizoplana) of one or more cultures of interest may be selected. These microorganisms are selected so that they can compete successfully in the particular environment with wild-type microorganisms, provide maintenance and stable expression of the gene expressing the pesticide protein, and preferably provide greater protection of the pesticide against environmental degradation and inactivation. Such microorganisms include bacteria, algae, and fungi. Of particular interest are microorganisms such as bacteria, e.g. eg, Pseudomonas, Erwinia, Serratia, Klebsiella, Xanthomonas, Streptomyces, Rhizobium, Rhodopseudomonas, Methylius, AgrObacterium, Acetobacter, Lactobacillus, ArthrObacter, Azotobacter, Leuconostoc, and Alcaligenes, fungi, particularly yeast, e.g. eg, SaccharOmyces, Cryptococcus, Kluyveromyces, SporObolomyces, Rhodotomla, and Aureobasidium. Of particular interest are phytosphere bacterial species such as Pseudomonas syringae, Pseudomonas fluorescens, Serratia maroescens, Acetobacter xylinum, Agrobacteria, Rhodopseudomonas spheroides, Xanthomonas campestrís, Rhizobium melioti, Alcaligenes entrophus, Clavibacter xyli and Azotobacter vinelandii and phytosphere yeast species, such such as Rhodotorula rubra, R. glutinis, R. marina, R. aurantiaca, Cryptococcus albidus, C. diffiuens, C. laurentii, SaccharOmyces rosei, S. pretoriensis, S. cerevisiae, Sporobolomyces roseus, S. odorus, Kluyveromyces veronae, and Aureobasidium pollulans. Pigmented microorganisms are of particular interest. There are several ways to introduce a gene that expresses the pesticidal protein into the host of the microorganism under conditions that allow the maintenance and stable expression of the gene. For example, expression cassettes can be constructed that include the nucleotide constructs of interest operably linked with the transcriptional and translational regulatory signals for expression of the nucleotide constructs and a nucleotide sequence homologous to a sequence in the host organism, in where integration will occur and / or a replication system operating in the host, whereby integration or stable maintenance will occur. Transcriptional and translational regulatory signals include, but are not limited to, promoters, transcriptional initiation sites, operators, activators, enhancers, other regulatory elements, rlbosome binding sites, a start codon, termination signals, and the like. . See, for example, US Pat. Nos. 5,039,523 and 4,853,331; EPO patent 0480762A2; Sambrook; Maniatis et al. (Coid Spring Harbor Laboratory Press, Cold Spring Harbor, New York); Davis et al., eds. (1980) Advanced Bacterial Genetics (Coid Spring Harbor Laboratory Press, Cold Spring Harbor, New York) and references cited therein. Suitable host cells, wherein the cells containing pesticidal proteins will be treated to prolong the activity of the pesticidal proteins in the cells when the treated cell is applied to the environment of the target pest(s), may include prokaryotes or eukaryotes. , normally limited to those cells that do not produce substances toxic to larger organisms, such as mammals. However, organisms that produce substances toxic to higher organisms could be used, where the toxin is unstable or the level of application is low enough to avoid any possibility of toxicity to a mammalian host. As hosts, prokaryotes and lower eukaryotes stand out, such as 100 mushrooms. Illustrative prokaryotes, both Gram negative and Gram positive, include Entenobacteriaceae, such as Escherichia, Erwinia, Shigella, Salmonella, and Proteus; Bacillaceae; Rhizobiaceae, such as Rhizobium; Spirillaceae, such as photobacterium, Zymomonas, Serratia, Aeromonas, Vibrio, Desulfovibrio, Spirillum; Lactobacillaceae; Pseudomonadaceae, such as Pseudomonas and Acetobacter, Azotobacteraceae and Nitrobacteraceae. Among the eukaryotes are fungi, such as Phycomycetes and Ascomycetes, including yeasts, such as Saccharomyces and Schizosaccharomyces and Basidiomycetes yeasts, such as Rhodotomla, Aureobasidium, Sporobolomyces and the like. Characteristics of particular interest in selecting a host cell for the purposes of pesticidal protein production include ease of introduction of the pesticidal protein gene into the host, availability of expression systems, efficiency of expression, stability of the protein in the host and the presence of auxiliary genetic capacities. Characteristics of interest for use as a pesticide microcapsule include protective qualities for the pesticide, such as thick cell walls, pigmentation and intracellular packing or inclusion body formation; leaf affinity; lack of toxicity in mammals; pest acceptance for ingestion; ease of destruction and fixation without damaging the toxin; and the like. Other considerations include ease of formulation and handling, economy, storage stability, and the like. Host organisms of particular interest include yeast, such as Rhodotorula spp., Aureobasidium spp., Saccharomyces spp. (such as S. cerevisiae), Sporobolomyces spp., phylloplane organisms such as Pseudomonas spp. (such as P. aeruginosa, P. fluorescens), c 101 Erwinia spp., and Flavobacterium spp., and other such organisms, including Bt, E. coli, Bacillus subtilis, and the like. The genes encoding the pesticidal proteins of the embodiments can be introduced into microorganisms multiplying on plants (epiphytes) to supply pesticidal proteins to potential target pests. Epiphytes, for example, can be gram positive or gram negative bacteria. Root colonizing bacteria, for example, can be isolated from the plant of interest by methods known in the art. Specifically, a root-colonizing strain of Bacillus cereus can be isolated from the roots of a plant (see, for example, Handelsman et al. (1991) Appl. Environ. Microbio!. 56:713-718 ). The genes encoding the pesticidal proteins of the embodiments can be introduced into a root-colonizing Bacillus cereus by standard methods known in the art. The genes encoding the pesticidal proteins can be introduced, for example, into the Bacillus root colonizer by electrotransformation methods. Specifically, the genes encoding the pesticidal proteins can be cloned into a carrier vector, for example, pHT3101 (Lerecius et al. (1989) FEMS Microbio!. Letts. 60: 211218. The pHT3101 carrier vector containing the coding sequence for the gene of the particular pesticidal protein, for example, can be transformed into root-colonizing Bacillus by electroporation (Lerecius et al. (1989) FEMS Microbiol. Letts. 60: 211-218). Expression systems can be designed such that the pesticidal proteins are secreted outside the cytoplasm of gram negative bacteria, such as E. coli, for example. The advantages of secreting pesticidal proteins are: (1) avoiding possible cytotoxic effects of the expressed pesticidal protein; and (2) improve the purification efficiency of the pesticidal protein, which c 102 includes, but is not limited to, increased efficiency in protein recovery and purification per volume of cell culture broth and reduced recovery and purification time and / or costs per unit of protein. Pesticidal proteins can be prepared so that they are secreted in E. coli, for example, by fusing a suitable E. coli signal peptide to the amino-terminus of the pesticidal protein. Signal peptides recognized by E. coli can be found in proteins known to be secreted in E. coli, for example, the OmpA protein ( Ghrayeb et al. (1984) EMBO J, 3:2437-2442 ). OmpA is a major outer membrane protein of E. coli and therefore its signal peptide is believed to be effective in the translocation process. Furthermore, it is not necessary to modify the OmpA signal peptide prior to processing as may be the case with other signal peptides, eg, the signal peptide of lipoproteins (Duffaud et al. (1987) Meth. Enzymol. 153:492). The pesticidal proteins of the embodiments can be fermented in a bacterial host and the resulting bacteria can be processed and used as a microbial spray in the same way that Bt strains have been used as insecticidal sprays. In the case of one or more pesticidal proteins secreted from Bacillus, the secretion signal is deleted or mutated using procedures known in the art. Such mutations and / or deletions prevent the secretion of the pestilda protein(s) into the growth medium during the fermentation process. The pesticidal proteins are retained within the cell, and the cells are then processed to produce the encapsulated pesticidal proteins. Any suitable microorganism can be used for this purpose. Pseudomonas has been used to express Bt toxins as encapsulated proteins and c 103 resulting cells have been processed and sprayed as an insecticide (Gaertner et al. (1993), iir. Advanced Engineered Pesticides, ed. Kim). Alternatively, pesticidal proteins are produced by introducing a heterologous gene into a host cell. Expression of the heterologous genes results, directly or indirectly, in the intracellular 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 the toxin. These naturally encapsulated pesticidal proteins can then be formulated according to conventional techniques for application in the environment of a target pest, eg, soil, water, and plant foliage. See, for example, patent no. EP0192319 and the references cited therein. In the embodiments, a transformed microorganism (including whole organisms, cells, spore(s), pesticidal protein(s), pesticidal component(s), pest-affecting component(s), mutant(s) , live or dead cells and cellular components, including mixtures of live and dead cells and cellular components and including decayed cells and cellular components) or an isolated pesticidal protein may be formulated with an acceptable carrier in one or more pesticidal composition(s), i.e., by For example, a suspension, a solution, an emulsion, a dusting powder, a dispersible granule or bead, a wettable powder and an emulsifiable concentrate, an aerosol or spray, an impregnated granule, an adjuvant, a coatable paste, a colloid, and, in addition, encapsulations, for example, in polymeric substances. Such formulated compositions can be prepared by conventional means such as drying, lyophilization, c 104 homogenization, extraction, filtration, centrifugation, sedimentation, or concentration of a cell culture comprising the polypeptide. These compositions described above can be obtained by adding a surfactant, an inert carrier, a preservative, a humectant, a feeding stimulant, an attractant, an encapsulating agent, a binder, an emulsifier, a dye, a lightning protector UV, a regulator, a flow agent or fertilizer, micronutrient donors or other preparations that affect plant growth. One or more agrochemicals including, but not limited to, herbicides, insecticides, fungicides, bactericides, nematicides, molluscicides, acaricides, plant growth regulators, crop aids, and fertilizers, may be combined with carriers, surfactants, or adjuvants commonly employed in formulation matter or other components to facilitate handling and application of the product to particular target pests. Suitable carriers and adjuvants can be solid or liquid and correspond to substances typically used in formulation technology, eg natural or regenerated mineral substances, solvents, dispersants, wetting agents, tackifiers, binders or fertilizers. The active ingredients of the modalities are typically applied in the form of compositions, and may be applied to the crop, plant, or seed area to be treated. For example, the compositions of the embodiments can be applied to grain when it is prepared for storage or during storage in a grain bin or silo, etc. Compositions of the embodiments can be applied simultaneously or successively with other compounds. Methods for applying an active ingredient of the modalities or an agrochemical composition of the modalities that contains at least one of c The pesticidal proteins produced by the bacterial strains of the modalities include, but are not limited to, foliar application, seed coating, and soil application. The quantity and the ratio of the applications depend on the intensity of the infestation by the corresponding pest. Surfactant agents include, but are not limited to, anionic compounds, such as a carboxylate, eg, of a metal, a carboxylate of a long-chain fatty acid, an N-acylsarcosinate, mono or diesters of phosphoric acid with ethoxylates of fatty alcohol or salts of said esters, fatty alcohol sulfates, such as sodium dodecyl sulfate, sodium octadecyl sulfate or sodium cetyl sulfate, ethoxylated fatty alcohol sulfates, ethoxylated alkylphenol sulfates, lignin sulfonates, petroleum sulfonates, alkyl aryl sulfonates, such as alkylbenzene sulfonates or low molecular weight alkylnaphthalene sulfonates, for example, butylnaphthalene sulfonate, salts of sulfonated naphthalene-formaldehyde condensates, salts of sulfonated phenol-formaldehyde condensates, more complex sulfonates, such as the amide sulfonates , for example, the sulfonated product of the condensation of oleic acid and N-methyl taurine or dialkyl sulfosuccinates, for example For example, sodium sulfonate or dioctyl succinate. Nonionic agents include the condensation products of fatty acid esters, fatty alcohols, fatty acid amides or ethylene oxide substituted fatty alkyl or alkenyl phenols, fatty esters of polyhydric alcohol ethers, e.g. sorbitan fatty esters, condensation products of said esters with ethylene oxide, e.g. fatty acid esters of polyoxyethylene sorbitan, block copolymers of ethylene oxide and propylene oxide, acetylenic glycols such as 2,4,7,9-tetraethyl-5-decyne-4,7-diol or ethoxylated acetylenic glycols . Examples of a cationic surfactant include, for example, an aliphatic mono-, di-, or polyamine, such as an acetate, naphthenate, or oleate; or an amine that c 106 contains oxygen, such as a polyoxyethylene alkylamine amine oxide; an amide-linked amine prepared by the condensation of a carboxylic acid with a di- or polyamine; or a quaternary ammonium salt. Examples of inert materials include, but are not limited to, inorganic minerals, such as kaolin, phyllosilicates, carbonates, sulfates, phosphates, or botanical materials, such as cork, corncob powder, peanut shell, rice husk, and shell. Castile walnut. The compositions of the embodiments may be in a form suitable for direct application or as a primary composition concentrate to be diluted with a suitable amount of water or other diluent prior to application. The pesticide concentration will vary depending on the nature of the particular formulation, specifically whether it is a concentrate or whether it will be used directly. The composition contains 1 to 98% of a solid or liquid inert carrier and 0 to 50% or 0.1 to 50% of a surfactant. These compositions will be administered according to the label rate for the commercial product, for example, approximately 0.005 kg-2.3 kg per 4047 m2 (0.01 lb-5.0 lb. per acre) when dry and at approximately 0.01 pts -10 pts per 4047 m2 (per acre) when in liquid form. In another embodiment, the compositions, as well as the transformed pesticidal microorganisms and proteins of the embodiments, may be treated prior to formulation to prolong pesticidal activity when applied to the environment of a target pest as long as the pretreatment is not detrimental to pesticidal activity. . Said treatment can be carried out by chemical and / or physical means as long as the treatment does not detrimentally affect the properties of the composition(s). Examples of chemical reagents include, but are not limited to halogenating agents; aldehydes such as formaldehyde and glutaraldehyde; anti-infectives, such 107 as zefiran chloride; alcohols, such as isopropanol and ethanol; and histological fixatives, such as Bouin's fixative and Helly's fixative (see, for example, Humason (1967) Animal Tissue Techniques (W.H. Freeman and Co.). In other embodiments, it may be advantageous to treat the Cry toxin polypeptides with a protease, eg, trypsin, to activate the protein prior to application of a pesticidal protein composition of the embodiments to the environment of the target pest. Methods for activation of the protoxin by a serine protease are well known in the art. See, for example, Cooksey (1968) Biochem. J. 6:445-454 and Carroll and Ellar (1989) Biochem. J. 261:99-105, the teachings of which are incorporated herein by reference. For example, a suitable activation protocol includes, but is not limited to, combining a polypeptide to be activated, eg, a purified novel Cry polypeptide (eg, having the amino acid sequence set forth in sec. con ID NO: 4 or SEQ ID NO: 8, and trypsin in a 1 / 100 protein / trypsin weight ratio in 20 nM NaHCO3, pH 8 and sample digestion 36 °C by Three hours. To apply the compositions (including the transformed microorganisms and pesticidal proteins of the embodiments) to the environment of an insect pest, they may, for example, be sprayed, misted, dusted, splashed, coated or poured, introduced into or on the soil. , introduced into irrigation water, by seed treatment or general application or dusting at the time the pest begins to appear or before the pests appear, as a protective measure. For example, the pesticidal protein and / or transformed microorganisms of the embodiments can be mixed with grain to protect the grain during storage. Generally, it is important to control Avoid pests well in the early stages of plant growth, as this is the time when the plant can suffer the most severe damage. Compositions of the embodiments may conveniently contain another insecticide if this is deemed necessary. In one embodiment, the composition is applied directly to the soil, at the time of planting, in a granular form of a composition of a carrier and dead cells of a Bacillus strain or transformed microorganism of the embodiments. Another embodiment is a granular form of a composition comprising an agrochemical such as, for example, a herbicide, an insecticide, a fertilizer, an inert carrier, and killed cells of a Bacillus strain or transformed microorganism of the embodiments. Those of skill in the art will recognize that not all compounds are equally effective against all pests. Compounds of the modalities show activity against insect pests, which may include economically important agronomic, forest, greenhouse, nursery, food and fiber, public and animal health, domestic and commercial structure, home, and stored product pests. Insect pests include insects selected from the orders Coleoptera, Diptera, Hymenoptera, Lepidoptera, Mallophaga, Homoptera, Hemiptera, Orthoptera, Thysanoptera, Dermaptera, Isoptera, Anoplura, Siphonaptera, Trichoptera, etc., particularly Coleoptera and Lepidoptera. Insects of the order Lepidoptera include, but are not limited to, military caterpillars, cutworms, looper caterpillars, and sunworms of the family Noctuidae: Agrotis ipsilon Hufnagel (tracer worm); A. orthogonia Morrison (western cutworm); A. segetum Denis & Schiffermüller (turnip moth); A. fabricius subterranean (granular cutworm); Alabama argillacea Hübner (cotton leafworm); Anticarsia gemmatalis 109 Hübner (legume caterpillar); Athetis mindara Barnes and McDunnough (rough-skinned cutworm); Earias insulana Boisduval (spiny cotton caterpillar); E. vittella Fabricius (speckled worm); Aegira (Xylomyges) curialis Grote (citrus cutworm); Euxoa messoria Harris (black-sided cutworm); Helicoverpa armigera Hübner (American worm); H. zea Boddie (cobworm or bolillera caterpillar); Heliothis virescens Fabricius (tobacco armyworm); Hypena scabra Fabricius (green clover worm); Mamestra set it up Walker (bertha soldierworm); M. brassicae Linnaeus (cabbage moth); Melanchra ask Harris (zebra caterpillar); Pseudaletia unipunda Haworth (military caterpillar); Pseudoplusia includens Walker (soybean false looper); Richia albicosta Smith (western bean cutworm); Spodoptera frugiperda JE Smith (fall armyworm); S. exigua Hübner (beet armyworm); S. litura Fabricius (tobacco gray bollworm, cluster caterpillar); Trichoplusia ni Hübner (false cabbage looper); borers, borers, web worms, pine acorn worms, and skeletonizing worms of the families Pyralidae and Crambidae such as Achroia grisella Fabricius (small hive moth); Amyelois transitella Walker (naval orange worm); Anagasta kuehniella Zeller (mill moth); Cadra cautella walker (almond moth); Chito partellus Swinhoe (Spotted Stem Borer); C. suppressafis Walker (striped rice / stem borer); C. terrenellus Pagenstecher (sugarcane stem borer); Corcyra cephalonica Stainton (rice moth); Crambus caliginosellus Clemens (corn root webworm); C. teterrellus Zincken (grass webworm); Cnaphalocrocis medinalis Guenée (rice leafroller); Desmia funeralis Hübner (grape roller worm); Diaphania hyalinata Linnaeus (melon worm); D. nitidalis Stoll (cucumber borer); Diatraea grandiosella Dyar 110 corn stalk), D. saccharalis Fabricius (sugar cane borer); Elasmopalpus lignosellus Zeller (small corn stalk borer); Eoreuma loftini Dyar (Mexican rice borer); Ephestia elutella Hübner (tobacco (cocoa) moth); Galleria mellonella Linnaeus (greater hive moth); Hedylepta accepta Butler (sugarcane leafroller); Herpetogramma licarsisalis Walker (lawn webworm); Homoeosoma electellum Hulst (sunflower moth); Loxostege sticticalis Linnaeus (beet webworm); Maruca testulalis Geyer (bean pod borer); Orthaga thyrisalis Walker (tea weaver moth); Ostrinia nubilalis Hübner (European corn borer); Plodia interpunctella Hübner (Indian flour moth); Scirpophaga incertulas Walker (yellow stem borer); Udea rubigalis Guenée (celery leaf binder); and leafrollers, armyworms, seedworms, and fruitworms of the family Tortricidae Acleris gloverana Walsingham (western black-headed armyworm); A. variaria Femald (Eastern black-headed armyworm); Adoxophyes orana Fischer von Rósslerstamm (summer fruit tortilla moth); Archips spp. including A. argyrospila Walker (fruit leafroller) and A. resana Linnaeus (European leafroller); Argyrotaenia spp.; Bonagota salubricola Meyrick (Brazilian apple leafroller); Choritoneura spp.; Cochylis hospes Walsingham (striped sunflower moth); Cydia latiferreana Walsingham (hazelnut worm); C. pomonella Linnaeus (codling moth); Endopiza viteana Clemens (grape berry moth); Eupoecilia ambiguella Hübner (vine moth); Grapholita molesta Busck (Oriental fruit moth); Lobesia botrana Denis & Schiffermüller (European grape moth); Platynota flavedana Clemens (Multicolored Leafroller); P. stultana Walsingham (leafroller 111 omnivorous); Spilonota ocellana Denis & Schiffermüller (eye-spotted shoot moth); and Suleima helianthana Riley (sunflower shoot moth). Other selected agronomic pests of the order Lepidoptera include, but are not limited to, Alsophila pometaria Harris (winter canker worm); Anarsia ineatella Zeller (peach leafminer); Anisota Senator J.E. Smith (orange-striped oak moth); Antheraea pemyi Guérin-Méneville (Chinese oak silkworm); Bombyx mori Linnaeus (silkworm); Bucculatrix thurberiella Busck (cotton leaf borer); Colias eurytheme Boisduval (alfalfa caterpillar); Datana integerrima Grote & Robinson (walnut caterpillar); Dendrolimus sibiricus Tschetwerlkov (Siberla silk moth), Ennomos subsignaria Hübner (elm caterpillar); Erannis would filiate Harris (false linden meter); Erechthias flavistriata Walsingham (sugarcane shoot moth); Euproctis chrysorrhoea Linnaeus (brown-tailed moth); Hamsina americana Guérin-Méneville (vine leaf skeletonizer); Heliothis subflexa Guenée; Hemileuca oliviae Cockrell (interval caterpillar); Hyphantria cunea Drury (autumn webworm), Keiferia lycopersicella Walsingham (tomato pinworm); Lambdina fiscellaria fiscellaria Hulst (eastern false fir looper); L. fiscellaria lugubrosa Hulst (western false-fir looper); Leucoma salicis Linnaeus (satin moth); Lymantria dispar Linnaeus (gypsy moth); Malacosoma spp.; Manduca quinquemaculata Haworth (five-spotted hawk-moth, tomato worm); M. sexta Haworth (tomato bollworm, tobacco bollworm); Operophtera brumata Linnaeus (winter moth); Orgyia spp.; Paleacrita vemata Peck (spring canker caterpillar); Papilio cresphontes Cramer (giant swallowtail, orange dog); Phryganidia califomica Packard (California oak moth); Phyllocnistis citrella Stainton (citrus leafminer); Phyllonorycter blancardella Fabricius 112 (spotted netiform miner); Pieris brassicae Linnaeus (great white butterfly); P. rapae Linnaeus (small white butterfly); P. napi Linnaeus (green-veined white butterfly); Platyptilia carduidactyla Riley (Artichoke Moth); Plutella xylostella Linnaeus (diamondback moth); Pectinophora gossypiella Saunders (pink caterpillar); Pontia protodice Boisduval & Leconte (southern cabbage caterpillar); Sabulodes aegrotata Guenée (omnivorous false looper); Schizura concinna J.E. Smith (red humped caterpillar); Sitotroga cerealella Olivier (Angoumois grain moth); Thaumetopoea pityocampa Schiffermuller (pine processionary caterpillar); Tineola bisselliella Hummel (clothes moth)); Tuta absoluta Meyrick (tomato leafminer moth) and Yponomeuta padella Linnaeus (ermine moth). Of interest are the larvae and adults of the order Coleoptera, which include weevils of the families Anthribidae, Bruchidae, and Curculionidae which include, but are not limited to; Anthonomus grandis Boheman (cotton weevil); Cylindrocopturus adspersus LeConte (sunflower stem weevil); Diaprepes abbreviatus Linnaeus (Diaprepes root weevil); Hypera punctata Fabricius (cloverleaf weevil); Lissorhoptrus oryzophilus Kuschel (rice water weevil); Metamasius hemipterus hemipterus Linnaeus (West Indian cane weevil); M. hemipterus sericeus Olivier (silky cane weevil); Sitophilus granarius Linnaeus (wheat weevil); S. oryzae Linnaeus (rice weevil); Smicronyx fulvus LeConte (red sunflower seed weevil); S. sordidus LeConte (gray sunflower seed weevil); Sphenophorus maidis Chittenden (corn weevil); Rhabdoscelus obscurus Boisduval (New Guinea sugarcane weevil); flea beetles, cucumber beetles, rootworms, leaf beetles, potato beetles, and leafminers of the family Chrysomelidae including, but not limited to: Chaetocnema ectypa 113 Horn (desert corn flea beetle); C. pulicaria Melsheimer (corn flea beetle); Colaspis brunnea Fabricius (grape colaspis); Diabrotica barben Smith & Lawrence (northern corn rootworm); D. undecimpunctata howardi Barber (southern corn rootworm); D. virgifera virgifera LeConte (western corn rootworm); Leptinotarsa ​​decemlineata Say (Colorado potato beetle); Oulema melanopus Linnaeus (cereal leaf beetle); Phyllotreta cruciferae Goeze (corn flea beetle); Zygogramma exclamationis Fabricius (sunflower beetle); beetles of the family Coccinellidae including, but not limited to: Epilachna varivestis Mulsant (Mexican bean beetle); scarabs and other beetles in the family Scarabaeidae (including, but not limited to; Antitrogus parvulus Britton (Chllders cane worm); Cyclocephala borealis Arrow (northern white worm); C. immaculata Olivier (northern white worm); southern, white grub); Dermolepida albohirtum Waterhouse (Greyback cane beetle); Euetheola humilis rugiceps LeConte (sugar cane beetle); Lepidiota frenchi Blackburn (French's cane worm); Tomarus gibbosus De Geer (Greyback carrot); T. subtropicus Blatchley (sugarcane worm); Phyllophaga crinita Burmeister (white worm); P. latifrons LeConte (June beetle); Popillia japonica Newman (Japanese beetle); Rhizotrogus majalis Razoumowsky (European beetle); Carpet beetles of the family Dermestidae, wireworms of the family Elateridae, Eleodes spp., Melanotus spp., including M. communis Gyllenhal (wireworm), Conoderus spp., Limonius spp.; Agriotes spp.; Ctenicera spp.; Aeolus spp.; bark beetles of the family Scolytidae; beetles of the family Tenebrionidae; beetles of the 114 family Cerambycidae such as, but not limited to, Migdolus fryanus Westwood (long-horned beetle); and beetles of the family Buprestidae including, but not limited to, Aphanisticus cochinchinae seminulum Obenberger (buprestid leafminer beetle). Of interest are adult and immature species of the order Diptera which include Agromyza parvicornis Loew leaf borer (corn speckled leaf borer); Mosquitoes (including, but not limited to: Contarinia sorghicola Coquillett (sorghum mosquito); Mayetiola destructor Say (Hessian fly); Neolasioptera murtfeldtiana Felt, (sunflower seed mosquito); Sitodiplosis mosellana Géhln (wheat mosquito) ; fruit flies (Tephritidae), Oscinella frít Linnaeus (fry flies); flies (including but not limited to: Delia spp. including Delia platura Meigen (seed larva); D. coarctata Fallen (fly of wheat bulb); Fannia canicularis Linnaeus, F. femoralis Stein (minor houseflies); Meromyza americana Fitch (wheat stem larva); Musca domestica Linnaeus (houseflies); Stomoxys calcitrans Linnaeus (stable flies)); face flies, horn flies, death flies, Chrysomya spp.; Phormia spp.; and other muscoid fly pests, Tabanus spp. spp.; deer flies or from Chrysops spp.; Melophagus ovinus Linnaeus (sheep fly); and other Brachycera, Aedes spp. mosquitoes; Anopheles spp.; Culex spp.; black flies of Prosimulium spp.; Simulium spp.; midges, simulid mosquitoes, ciarids, and other Nematocera. Insects of interest include those of the order Hemiptera such as, but not limited to, the following families: Adelgidae, Aleyrodidae, Aphididae, Asterolecaniidae, Cercopidae, Cicadellidae, Cicadidae, Cixiidae, Coccidae, Coreidae, Dactylopiidae, Delphacidae, Diaspididae, 115 Eriococcidae, Flatidae, Fulgoridae, Issidae, Lygaeidae, Margarodidae, Membracidae, Miridae, Ortheziidae, Pentatomidae, Phoenicococcidae, Phylloxeridae, Pseudococcidae, Psyllidae, Pyrrhocoridae, and Tingidae. Agriculturally important members of the order Hemiptera include, but are not limited to: Acrostemum hilare Say (green stink bug); Acyrthisiphon pisum Harris (pea aphid); Adelges spp. (adelgids); Adelphocoris rapidus Say (rapid bug); Anasa tristis De Geer (squash bug); Aphis craccivora Koch (black legume aphid); A. fabae Scopoli (black bean aphid); A. gossypii Glover (cotton aphid, melon aphid); A. maidiradicis Forbes (corn root aphid); A. pomi De Geer (apple aphid); A. spiraecola Patch (green citrus aphid); Aulacaspis tegalensis Zehntner (sugarcane mealybug); Aulacorthum solani Kaltenbach (potato aphid); Bemisia tabaci Gennadius (tobacco whitefly, sweet potato whitefly); B. argentifolii Bellows & Perring (silverleaf whitefly); Say bug (Blissus leucopterus leucopterus); Blostomatidae spp.; Brevicoryne brassicae Linnaeus (cabbage aphid); Cacopsylla pyricola Foerster (pear tree psyllid); Calocoris norvegicus Gmelin (potato capsid aphid); Chaetosiphon fragaefolii Cockerell (strawberry aphid); Cimicidae spp.; Coreidae spp.; Corythuca gossypii Fabrlcius (cotton lace bug); Cyrtopeltis modesta Distant (tomato bug); C. notatus Distant (sucker fly); Deois flavopicta Stál (spittlebug); Dialeurodes citri Ashmead (citrus whitefly); Diaphnocoris chlorionis Say (carob bug); Diuraphis noxia Kurdjumov / Mordvilko (Russian wheat aphid); Duplachionaspis divergens Green (armored mealybug); Dysaphis plantaginea Paaserini (ashy apple aphid); Dysdercus suturellus Herrich-Scháffer (cotton stainer); Dysmicoccus boninsis 116 Kuwana (gray sugarcane mealy bug); Empoasca fabae Harris (potato hopper); Eriosoma lanigerum Hausmann (woolly apple aphid); Erythroneoura spp. (vine snappers); Eumetopina flavipes Muir (Sugarcane Island hopper); Eurygaster spp.; Euschistus servus Say (brown stink bug); E. variolarius Palisot de Beauvois (spotted stink bug); Graptostethus spp. (seed bug complex); and Hyalopterus pruni Geoffroy (mealy plum aphid); Icerya purchasi Maskell (cottony mealybug); Labopidicola allii Knight (onion bug); Laodelphax striatellus Fallen (brown planthopper); Leptoglossus corculus Say (pine leaf foot seed bug); Leptodictya tabida Herrlch-Schaeffer (sugarcane lace bug); Lipaphis erysimi Kaltenbach (turnip aphid); Lygocoris pabulinus Linnaeus (common green capsid); Lygus lineolaris Palisot de Beauvois (spotting bug); L. Hesperus Knight (western spotted bug); L. pratensis Linnaeus (common meadow bug); L. rugulipennis Poppius (European spotting bug); Macrosiphum euphorbiae Thomas (potato aphid); Macrosteles quadrilineatus Forbes (Aster hopper); Magicicada septendecim Linnaeus (periodic cicada); Mahanarva fimbriolata Stál (sugarcane spittlebug); Melanaphis sacchari Zehntner (sugarcane aphid); Melanaspis glomerata Green (black mealybug); Metopolophium dirhodum Walker (pink grain aphid); Myzus persicae Sulzer (potato peach aphid, green peach aphid); Nasonovia ribisnigri Mosley (lettuce aphid); Nephotettix cinticeps Uhler (green jumper); N. nigropictus Stál (rice skipper); Nezara viridula Linnaeus (green bug); Nilaparvata lugens Stál (brown planthopper); Nysius ericae Schilling (false bug); Nysius raphanus Howard (false bug); oebalus 117 pugnax Fabricius (rice stink bug); Oncopeltus fasciatus Dallas (large silk cotton bug); Orthops campestris Linnaeus; Pemphigus spp. (rhizophagous aphids and gall-forming aphids); Peregrinas Ashmead maidis (Corn Plant Springer); Perkinsiella saccharicida Kírkaldy (sugarcane delphacid); Phylloxera devastatrix Pergande (Hickory phylloxera); Pianococcus citri Risso (citrus mealy bug); Plesiocoris rugicollis Fallen (apple capsid); Poecilocapsus lineatus Fabricius (four-striped bug); Pseudatomoscelis seriatus Reuter (jumping cotton flea); Pseudococcus spp. (another mealybug complex); Pulvinaria elongata Newstead (cottony grass mealybug); Pyrilla perpusilla Walker (sugarcane hopper); Pyrrhocoridae spp.; Quadraspidiotus pemiciosus Comstock (San Jose louse); Reduviidae spp.; Rhopalosiphum maidis Fitch (corn aphid); R. padi Linnaeus (stem aphid); Saccharicoccus sacchari Cockerell (pink sugarcane mealy bug); Schizaphis graminum Rondani (green cereal aphid); Sipha flava Forbes (yellow sugarcane aphid); Sitobion avenae Fabricius (dark green tang aphid); Sogatella furcifera Horvath (white-backed hopper); Sogatodes oryzicola Muir (rice delphic acid); Spanagonicus albofasciatus Reuter (white-marked jumping flea); Therioaphis maculata Buckton (spotted alfalfa aphid); Tinidae spp.; Toxoptera aurantii Boyer de Fonscolombe (black citrus aphid); and T. citricida Kirkaldy (brown citrus aphid); Trialeurodes abutiloneus (striped-wing whitefly) and T. vaporariorum Westwood (greenhouse whitefly); Trioza diospyri Ashmead (Persimmon psyllids); and Typhlocyba pomaria McAtee (apple white leafhopper). 118 Also included are adults and larvae of the order Acari (mites) such as Acería tosichella Keifer (curly wheat mite); Panonychus ulmi Koch (European red mite); Petrobia latens Müller (brown wheat mite); Steneotarsonemus bancrofti Michael (sugarcane stem mite); spider mites and red mites of the family Tetranychidae, Oligonychus grypus Baker & Pritchard, O. indicus Hirst (sugarcane leaf mite), O. pratensis Banks (Banks grass mite), O. stickneyi McGregor (spider mite from sugar cane); Tetranychus urticae Koch (spotted spider mite); T. mcdanieli McGregor (McDaniel mite); T. cinnabarinus Boisduval (carmine spider mite); T. turkestani Ugarov & Nikolski (strawberry spider mite), flat mites of the family Tenuipalpidae, Brevipalpus lewisi McGregor (citrus flat mite); bud and erinosis mites of the family Eriophyidae and other foliphagous mites and mites important to human and animal health, i.e. dust mites of the family Epidermoptidae, follicular mites of the family Demodicidae, grain mites of the family Glycyphagidae, ticks of the order Ixodidae. Ixodes scapularis Say (black-legged or deer tick); I. holocyclus Neumann (Australian paralysis tick); Dermacentor variabais Say (American dog tick); Amblyomma americanum Linnaeus (lone star tick); and scabies mites in the families Psoroptidae, Pyemotidae, and Sarcoptidae. Of interest are insect pests of the order Thysanura, such as Lepisma saccharina Linnaeus (silverfish); Thermobia domestica Packard (fire bug). Other arthropod pests covered include: spiders in the order Araneae, such as Loxosceles reclusa Gertsch & Mulaik (brown or violinist spider); and Latrodectus mactans Fabricius (black widow spider); and centipedes in the order c 119 Scutigeromorpha, such as Scutigera coleoptrata Linnaeus (house centipede). In addition, insect pests of the order Isoptera are of interest, and include those of the family termitidae, such as, but not limited to, Cylindmtermes nordenskioeldi Holmgren and Pseudacanthotermes militaris Hagen (sugarcane termite). Insects of the order Thysanoptera are furthermore of interest, and include, but are not limited to, thrips, such as Stenchaetothrips minutus van Deventer (sugarcane thrips). Insect pests can be tested for pesticidal activity of compositions of the embodiments in early stages of development, e.g. g., as larvae or other immature forms. Insects can be grown in total darkness at a temperature of about 20°C to about 30°C and a relative humidity of about 30% to about 70%. Bioassays can be performed, as described in Czapla and Lang (1990) J. Econ. environment 83(6): 2480-2485. Methods for rearing insect larvae and performing bioassays are well known to a person skilled in the art. A person skilled in the art knows a wide variety of bioassay techniques. General procedures include the addition of experimental compound or organism to the diet source in a closed container. Pesticidal activity can be determined by, for example, but not limited to, changes in mortality, weight loss, attractiveness, repellency, and other physical and behavioral changes after feeding and exposure for a suitable period of time. The bioassays described herein can be used with any feeding insect pest in the larval or adult stage. The following examples are included by way of illustration and not by way of limitation. c 120 Experimentation Example 1. Generation of Cry1B variants with improved spectrum of insecticidal activity The insecticidal protein Cry 1 Bd has an amino acid sequence of sec. with no. ID: 1 (US Patent No. US 8,692,065) has high insecticidal activity (ILC50 = 1 ppm) against the European corn borer larva (Ostrinia nubilalis) but low insecticidal activity (ILC50 > 1000 ppm and ~400 ppm respectively) against earworm (Helicoverpa zea) and armyworm (Spodoptera frugiperda). The Cry1B insecticidal protein, referred to as MP258 (serial no. PCT / US14 / 49923) having an amino acid sequence of sec. with no. from ident: 47 have high insecticidal activity (ILC50 = 4 ppm) against the larva of the European corn borer (Ostrinia nubilalis) but lower insecticidal activity (ILC50 24 ppm and 62 ppm respectively) against the earworm (Helicoverpa zea) and the fall armyworm (Spodoptera frugiperda). A series of variant Cry1 B polypeptides derived from Cry1 Bd (SEQ ID NO: 1) and MP258 were designed to enhance insecticidal activity against corn ear worm (CEW) and / or fall army worm (FAW). compared to CrylBd (SEQ ID NO: 1) and / or MP258 (SEQ ID NO: 47) while maintaining ECB insecticidal activity. Cry1B variant polypeptides having improved insecticidal activity that were generated include those listed in Table 1. The insecticidal activity of the Cry1B variants was determined as described in Example 4 and the results of insecticidal activity are shown in Table 3. An amino acid sequence alignment of the Cry1 B variant polypeptides is shown in Figure 1. Table 1 ident. from the CrylBd clone Polypeptide sec. with no. of ident.: 1 polynucleotide sec. with no. of ident.: 2 c 121 ident. of the clone Polypeptide Polynucleotide IP1B-B1 The sec. with no. of ident.: 3 The sec. with no. of ident.: 4 IP1B-B21 The sec. with no. of ident.: 5 The sec. with no. of ident.: 6 IP1B-B22 The sec. with no. of ident.: 7 The sec. with no. of ident.: 8 IP1B-B23 The sec. with no. of ident.: 9 The sec. with no. of ident.: 10 IP1B-B24 The sec. with no. of ident.: 11 The sec. with no. of ident.: 12 IP1B-B25 The sec. with no. of ident.: 13 The sec. with no. of ident.: 14 IP1B-B26 The sec. with no. of ident.: 15 The sec. with no. of ident.: 16 IP1B-B27 The sec. with no. of ident.: 17 The sec. with no. of ident.: 18 IP1B-B28 The sec. with no. of ident.: 19 The sec. with no. of ident.: 20 IP1B-B29 The sec. with no. of ident.: 21 The sec. with no. of ident.. 22 IP1B-B31 The sec. with no. of ident.: 23 The sec. with no. of ident. . 24 IP1B-B32 Sec. with no. of ident.: 25 The sec. with no. of ident.: 26 IP1B-B33 The sec. with no. of ident.: 27 The sec. with no. of ident.: 28 IP1B-B34 The sec. with no. of ident.: 29 The sec. with no. of ident.: 30 IP1B-B40 The sec. with no. of ident.: 31 The sec. with no. of ident.: 32 IP1B-B41 The sec. with no. of ident.: 33 The sec. with no. of ident.: 34 IP1B-B42 The sec. with no. of ident.: 35 The sec. with no. of ident.: 36 IP1B-B43 The sec. with no. of ident.: 37 The sec. with no. of ident.: 38 IP1B-B44 The sec. with no. of ident.: 39 The sec. with no. of ident.: 40 IP1B-B45 The sec. with no. of ident.: 41 The sec. with no. of ident.: 42 IP1B-B46 The sec. with no. of ident.: 43 The sec. with no. of ident.: 44 IP1B-B47 The sec. with no. of ident.: 45 The sec. with no. of ident.: 46 MP258 The sec. with no. of ident.: 47 The sec. with no. of ident.: 48 GS060 The sec. with no. of ident.: 49 The sec. with no. of ident.: 50 The percent amino acid sequence identity of variant Cry1B polypeptides calculated using the Needleman-Wunsch algorithm, as implemented in the Needle program (EMBOSS toolkit), are shown as a matrix table in Table 2a-2b. The empty part of the parent table is not displayed. Table 2a O § w o 5 1 co CL v- CN cp ώ τ- Ο. CN CN CO < ω Ξ CO CN Cp ώ CL V CN cp CO CL m CN cp ώ τ— O. co CN m 1 m Q- r- CN co 1 co T“ a co CN CO co 0- o CN cp co τ-Ω. CrylBd 65.6 95.4 84.3 82.6 82.5 84.3 84.3 84.2 83.7 83.7 83.7 c 122 GS060 67.0 60.1 60.2 60.1 60.1 60.2 60.1 60.0 59.9 60.1 IP1B-B1 - - 83.4 82.6 84.5 83.4 83, 4 83.2 82.9 82.9 82.9 IP1B-B21 - - - 95.4 96.9 99.7 99.7 99.5 99.1 99.1 99.1 IP1B-B22 - - - - 95.4 95.1 95.1 95.0 94.5 94.8 94.8 IP1B-B23 - - - - - 96.6 96.6 96.5 96.0 96.0 96.0 IP1B-B24 - - - - - - 99.4 99.2 98.8 98.8 98.8 IP1B-B25 - - - - - - - 99.8 99.4 99.4 99.4 IP1B-B26 - - - - - - - - 99.5 99.2 99.2 IP1B-B27 - - - - - - - - - 99.4 99.4 IP1B-B28 - - - 99.8 Table 2b CO CO 1 co £ CSI co co 1 co r- Q. CO CO co 1 co £ 2 co 1 co Τ- Ο. O 2 1 co £ s 1 co £ 04 2 t co £ CQ Xt W S 1 m T- Q_ <o ω 1 co £ b- 2 1 co £ CO m CN Q. 2 00 ώ £ 1 co £ CrylBd 80.4 80.4 81.0 82.0 83.7 83.9 83.9 83.9 83.9 83.9 83.9 83.9 82.3 GS060 66.6 66.9 66.3 65.5 59 .8 59.9 60.1 60.1 60.1 60.1 59.9 59.9 59.9 IP1B-B1 83.6 83.0 82.7 81.6 82.8 82.9 83.1 83.1 83.1 83.1 83.1 83.1 80.9 IP1B-B21 71.6 71.5 71.8 71.8 99.1 99.1 99.2 99.2 99.2 99, 2 99.2 99.2 96.9 IP1B-B22 70.7 70.4 70.7 71.0 94.7 94.7 94.7 94.7 94.7 94.7 94.8 94.8 97 .6 IP1B-B23 72.5 72.3 72.6 72.3 96.0 96.0 96.2 96.2 96.2 96.2 96.2 96.2 96.0 1P1B-B24 71.6 71.5 71.8 71.8 98.8 98.9 98.9 98.9 98.9 98.9 98.9 98.9 96.6 1P1B-B25 71.8 71.6 71.9 71, 9 99.4 99.4 99.5 99.5 99.5 99.5 99.5 99.5 96.6 IP1B-B26 71.6 71.5 71.8 71.8 99.5 99.2 99 .4 99.4 99.4 99.4 99.4 99.4 96.5 IP1B-B27 71.3 71.2 71.5 71.3 99.2 98.9 99.7 99.5 99.5 99.5 99.2 99.2 96.0 IP1B-B28 71.3 71.2 71.5 71.3 99.1 99.1 99.4 99.2 99.2 99.2 99.5 99, 5 96.3 IP1B-B29 71.3 71.2 71.5 71.3 99.1 99.1 99.4 99.2 99.2 99.2 99.4 99.4 96.3 IP1B-B31 - 99.4 99.1 98.0 71.3 71.6 71.5 71.5 71.5 71.5 71.5 71.5 69.2 IP1B-B32 - - 99.2 98.0 71.2 71.5 71.3 71.3 71.3 71.3 71.3 71.3 69.1 IP1B-B33 - - - 98.0 71.5 71.8 71.6 71.6 71.6 71.6 71, 6 71.6 69.4 IP1B-B34 - - - - 71.5 71.8 71.5 71.5 71.5 71.5 71.5 71.5 69.7 IP1B-B40 - - - - - 99 .7 99.1 99.1 99.1 99.2 99.2 99.4 96.2 IP1B-B41 - - - - - - 99.1 99.1 99.1 99.2 99.2 99.4 96.2 IP1B-B42 - - - - - - - 99.8 99.8 99.7 99.5 99.4 96.2 IP1B-B43 - - - - - - - - 99.8 99.8 99, 5 99.5 96.2 IP1B-B44 - - - - - - - - - 99.7 99.7 99.4 96.2 IP1B-B45 - - - - - - - - - - 99.4 99.7 96.2 c 123 IP1B-B46 ............ 99.7 96.3 IP1B-B47 ............ 96.3 Example 2. Saturation mutagenesis at selected positions of the Cry1B variant polypeptides of MP258 and IP-1B The polynucleotides of sec. with no. of ident.: 48, sec. with no. of ident.: 6, sec. with no. of ident.: 14, and sec. with no. ident. no.: 42 encoding MP258, IP1B-B21, IP1B-B25 and IP1B-B45 (sec. with ident. no.: 47, sec. with ident. no.: 5, sec. with ident. no. .: 13, and SEQ ID NO: 41 respectively) were used as the templates for saturation mutagenesis at selected amino acid positions. A reverse mutagenesis primer and a complementary forward mutagenesis primer were designed to create the amino acid substitution(s) at the site(s) of interest. Typically, the mutagenesis primer was between 30 to 45 bases in length with two or more bases, usually 10 to 15, on either side of the site of interest. To do saturation mutagenesis, degenerate primers covering all possible amino acid residues were used. Mutagenesis reactions were performed using the Agilent QuikChange™ Lightening Site-Directed Mutagenesis Kit. Materials provided in the kit are QuikChange™ Lightening Enzyme, 10X QuikChange™ Lightning Buffer, dNTP mix, QuikSolution™ Reagent, and Don restriction enzyme according to manufacturer's instructions. PCR amplifications were typically performed with the Expand™ High Fidelity PCR System (Roche, Switzerland) in 50 ul containing 50-100 ng templates, 0.4-2 μΜ primer pair, 200 μΜ dNTPs, and 2 Units of DNA polymerase. The mutagenesis reaction was initiated by preheating the reaction mixture to 94 °C for c 124 min, followed by 16 cycles of the following cycle schedule: 94 °C for 1 min, 52 °C for 1 min, and 68 °C for 8, 12, 16, or 24 min depending on insole length. The mutagenesis reaction was terminated by incubation at 68 °C for 1 h. PCR amplification products were evaluated by agarose gel electrophoresis. PCR products were purified by a QIAquick™ PCR purification kit (Qiagen, Germany) and then treated with the restriction enzyme Dpnl. A 1 µl aliquot of the PCR product was typically transformed into BL21(DE3) cells and inoculated onto a Luria-Bertani (LB) plate containing 100 µg / ml ampicillin. Approximately 48 or more colonies were selected for saturation mutagenesis and plasmid DNA isolated for sequencing. Two-step sequencing was used, the first for the specific mutation site(s) with one sequencing primer followed by full sequence confirmation with multiple sequencing primers. After confirming by sequencing all 19 amino acid mutations, the mutant genes progressed to protein expression and purification. In the case of mutations made to cover the entire Domain III of IP1B-B25 spanning T495 to E655, 48 mutant clones from each site were picked and selected for CEW activity, as described in Example 4. To sequence the mutant clones to determine the mutated amino acids, among 151 amino acid residues subjected to mutagenesis, 103 sites were sequenced based on the number of activating mutations and inhibitory mutations. Sites containing mutants that did not show significant changes in activity were not sequenced. Example 3. Purification of cry1B variant insecticidal proteins 125 The cry1 B variant insecticidal protein genes were expressed in a modified pMAL vector (cat. no. E8000S from New England Biolabs) as a fusion with MBP (maltose binding protein). The pMAL vector was modified to attach a 6X His tag to the N-terminus of the MBP following the methionine at position 1. The plasmid containing the insecticidal protein gene was cloned in E. coli BL21(DE3). BL21 cells were grown in MagicMedia™ (Life Technologies) in 96-deep-well plates or flasks on a shaker operating at 250 rpm at 37°C for 8h followed by 16°C for 64h. During incubation at 16 °C, the MBP-toxin fusion protein accumulated in the BL21 cell as a soluble protein. To purify the fusion protein, E. coli cells were harvested by centrifugation and treated in a lysozyme solution consisting of 2 mg / mL lysozyme in 50 mL pH8 sodium phosphate buffer containing 300 mM NaCl. , 2 U / ml endonuclease (Epicentre) and 5 mM MaCI2 for 3 h at 37 °C with gentle shaking. Then, lysozyme-treated E. coli cells were disrupted with 1% Triton X100 and clarified lysate containing IP-1B proteins was prepared by centrifugation at 4000 rpm, 30 min (96-well plates) or 9000 rpm ( samples produced in vials). His-tagged MBP-toxin proteins were purified from the clarified lysate by affinity chromatography using Qiagen™ NiNTA agarose according to the manufacturer's standard procedure. For clarified lysate samples prepared in 96-well plates, Pall Corporation™ (25 Harbor Park Drive Port Washington, NY 11050) deep 96-well filter plates were used as affinity chromatography columns. Purified toxin proteins eluted from NiNTA agarose were passed through Sephadex G25 to change the phosphate buffer to 25 mM HEPES-NaOH, pH8 and used in an insect bioassay. 126 to determine the insecticidal activity. MBP was digested with 1 / 100 (w / w) Factor Xa (New England Biolabs) at 25 °C overnight and separated from IP-1B proteins by Superdex 200 column chromatography using the difference in sizes and the weak affinity of MBP for Superdex. Protein concentrations were determined by capillary electrophoresis with the LabChip™ GXII device (Caliper LifeSciences). The protein analysis was repeated at least 3 times until the final concentrations were considered reliable within the predetermined deviation, less than 10%. Example 4. Determination of the insecticidal activity of IP-1B variant proteins The activity of Cry1B polypeptide variants against the major maize pests, the European corn borer (ECB, Ostrinia nubilalis), ear bollworm (ECW, Helicoverpa zea), and fall armyworm (FAW, Spodoptera frugiperda), was determined by feeding trial as described in Cong, R., et al. Proceedings of the 4th Pacific Rim Conferences on Biotechnology of Bacillus thuringiensis and its environmental impact, pp. 118-123, ed. by R. J. Akhurst, C. E. Beard and P. Hughes, published 2002, Canberra, Australia. Briefly, the feeding trials were conducted on an artificial diet containing the insecticidal proteins. Insecticidal proteins were prepared as described in Example 1, and 10 pL of the protein samples were mixed with 40 pL of molten (40-50 °C) artificial insect diet prepared on the basis of insect-formulated Southland premix. lepidoptera (Southland Products, Lake Village, AR) with low melting temperature agarose. The diet-protein insecticide mixture was placed in each well of a 96-well microtiter plate. One or more newly hatched larvae of the 127 insects were placed in each well to feed for 4 days for CEW and FAW and 5 days for ECB at 28 °C. Alternatively, insect eggs or larvae were sorted by large particle flow cytometry using COPAS™ (Complex Object Parametric Sorter and Analyzer) obtained from Union Biometrica (Holliston, MA) to place one egg or larva per well. in a 96-well microtiter plate containing solidified insect artificial diet. When eggs were used to lay on test plates, only those wells containing larvae that hatched after 16 hours were used for test data collection. Usually, occlusion rates of 90 to 95% were obtained due to the efficient classification of COPAS. After certain feeding periods, the insects' response to protein was scored using a 0-3 numerical scoring system based on the size and mortality of the larvae in each well. If no response (or normal growth) was observed, a score of 0 was given. When growth was slightly retarded, a score of 1 was given. A score of 2 means that the larvae were severely retarded in growth (close to the size of the larvae). new born). A score of 3 means the death of all larvae in the well. The percent response (response) for each treatment was calculated by dividing the total score, a sum of the scores of the replicate wells for each treatment by the highest possible total scores. For example, if a treatment (one sample, one dose) had 6 replicate wells, the highest possible total score would be 3X6 = 18. To identify variant Cry1B polypeptides that have increased levels of activity towards these maize pests, significantly greater than the activity of the reference such as the wild-type reference protein, it is not 128 mutated (eg MP258 sec. ID no.: 47). Variant polypeptides at certain concentrations were assayed along with 4 doses of the reference protein within a 96 well assay plate. The concentrations of the insecticidal proteins were within the concentrations of the 4 doses of the reference protein, preferably around the midpoint of the concentrations of the 4 doses. Each sample plate contained the reference protein in a significant number of wells such as 16 wells at 4 different doses. In addition, up to 80 mutant proteins were included in each plate for comparison of activity with the reference protein. From a sample plate, 10 ul of samples from each well were collected by multichannel pipettor and dispensed into an assay plate containing 40 ul of molten diet in each well and mixed on a shaker. This process to produce the test plate was repeated up to 6 times or more to produce a desired number of test plates. After the diet had solidified and cooled to 4°C, the newly hatched insect larvae were placed in each well, sealed with perforated Mylar film, and incubated in a 28°C constant temperature incubator. After a certain feeding period, the responses of the insects were scored under a magnifying glass. Sigmoidal dose-response values ​​(responses) were converted to probit linear dose-response values ​​using SAS-JMP®, Generalized Linear Model, Binomial Response, Probit). The response for each protein in the replicates was summed and compared to the dose-response probit line of the reference protein's activity, creating a new number called the lead FAE (rapid activity assessment) number. For example, if a mutant protein showed a certain probit value at 40 ppm and the actual dose with the same probit value for the reference protein was 100 ppm; then the FAE value is 2.5 (100 / 40). This 129 means that the mutant protein is 2.5 times more potent than the reference protein. This assay was performed with 2 different doses of mutant proteins at the same time and repeated 3 times generating 6 lead AED number data points for each mutant. The average guide FAE number was called the FAE index. For each protein, a two-sided t-test was performed to compare the 6 guideline AED numbers. Bonferroni correction was used to assess p-values ​​(number of new proteins / alpha) to determine if the FAE index was statistically significant. The other screening method used in this patent application is the High Dose Assay (HDA). In this method, test proteins at high concentrations (above EC50) were plated in insect assay plates as described above, along with a similar concentration of one or more reference proteins with a known level of activity. This HDA was often used in stepwise selection to rapidly eliminate proteins of little or no activity. Yet another selection method used was the High Productivity Functional Assay (HFA). This trial was similar to the AED but only used one dose instead of 2 doses. Otherwise the HFA, especially in the way of calculating the index, was identical to the FAE. Therefore, the HFA index has the same importance as the FAE index. The predicted point with 50% response on the scoring scheme is called the ILC50 as it is a combination of the growth inhibition or feeding and lethal responses. To determine ILC50 values, each treatment (one dose) was repeated 6 or more, usually 24, times. The insecticidal activity of the Cry1B variants is shown in Table 3. Table 4 shows insecticidal activity against earworm for amino acid substitutions having increased activity. 130 (FAE score z 1.2) compared to reference MP258 polypeptide (SEQ ID NO: 47), IP1B-B21 (SEQ ID NO: 5), IP1B-B25 ( sec. with ident. no.: 13), or IP1B-B45 (sec. with ident. no.: 41). Table 4 indicates the position number and amino acids corresponding to positions 50-651 of MP258 (SEQ ID NO: 47); the predicted secondary structure and its assignment; solvent exposure score; an alignment of the amino acid sequence of MP258 (SEQ ID NO: 47); IP1B-B21 (Section ID No.: 5), IP1B-B25 (Section ID No.: 13), IP1B-B45 (Section ID No.: 41), IP1B- B21 (SEQ ID NO: 5), CrylBd (SEQ ID NO: 1), CrylBh (SEQ ID NO: 52), and CryIBi (SEQ ID NO: 52). ID: 54); the polypeptide backbone on which the variant was made; the amino acid substitution variant (eg L50R); and earworm insecticidal FAE score compared to the corresponding polypeptide backbone (MP258 - sec id no: 47, IP1B-B21 - sec id no: 5, IP1B-B25 - part with ID No.: 13, or IP1B-B45 - part with ID No.: 41). Table 3 ident. of the Polypeptide of sec. with ECB CEW FAW clone no. of Ident. CrylBd Sec. with no. ID: 1 ILC50 = 1 ppm ILC50 = >1000 ppm ILC50 = ~ 400 ppm IP1B-B1 Sec. with no. of Ident.: 3 ILC50 = 1.3 ppm ILC50 = 21 ppm ILC50 = 34.3 ppm IP1B-B21 Sec. with no. ID: 5 ILC50 = 22.4 ppm IP1B-B22 Sec. with no. ID: 7 ILC50 = 27.1 ppm IP1B-B23 Sec. with no. ID: 9 ILC50 = 29.2 ppm IP1B-B24 Sec. with no. of Ident.: 11 ILC50 = 12.6 ppm IP1B-B25 Sec. with no. of Ident.: 13 ILC5O= 11.91 ppm IP1B-B26 The sec. with no. ID: 15 ILC50 = 8.36 ppm IP1B-B27 Sec. with no. ID: 17 ILC50 = 7.99 ppm IP1B-B28 Sec. with no. ID: 19 ILC50 = 7.74 ppm IP1B-B29 Sec. with no. ID: 21 ILC50 = 8.45 ppm 131 IP1B-B31 Sec. with no. ID: 23 ILC50 = 2.8 ppm IP1B-B32 Sec. with no. ID: 25 ILC50 = 2.9 ppm IP1B-B33 Sec. with no. ID: 27 ILC50 = 3.0 ppm IP1B-B34 Sec. with no. ID: 29 ILC50 = 2.9 ppm IP1B-B40 Sec. with no. ID: 31 ILC50 = 5.78 ppm IP1B-B41 Sec. with no. ID: 33 ILC50 = 4.54 ppm IP1B-B42 Sec. with no. ID: 35 ILC50 = 6.2 ppm IP1B-B43 Sec. with no. ID: 37 ILC50 = 6.7 ppm IP1B-B44 Sec. with no. ID: 39 ILC50 = 6.9 ppm IP1B-B45 Sec. with no. ID: 41 ILC50 = 5.7 ppm IP1B-B46 Sec. with no. ID: 43 ILC50 = 8 ppm IP1B-B47 Sec. with no. ID: 45 ILC50 = 6.1 ppm MP258 Sec. with no. code: 47 ILC50 = 4 ppm ILC50 = 24ppm ILC50 = 62 ppm Table 5 shows the insecticidal activity against earworm for amino acid substitutions having an FAE score < 1.2 compared to the MP258 (SEQ ID NO: 47) polypeptide backbone. IP1B-B21 (Section ID No.: 5), ltP1B-B25 (Section ID No.: 13), or IP1B-B45 (Section ID No.: 41). Table 5 indicates the position number and amino acids corresponding to positions 50651 of MP258 (SEQ ID NO: 47); the polypeptide backbone on which the variant was made; the amino acid substitution variant (eg L50R); and ia earworm insecticidal FAE score compared to the corresponding polypeptide backbone (MP258 seq id no: 47, IP1B-B21 - sec id no: 5, IP1B -B25 section with ID No.: 13, or IP1B-B45 - section with ID No.: 41. 3Vd CM •M* or CM 'M; CM CM- LO cm X CL 0 bjububa O 0 o LO co LO co LO MLO _l —1 < < 0 3Vd co r*» LO co co co~ CM_ co_ co h» σ co io 132 M-_cg -What with < > X LLI < ajueiJBA o LO O LO CO LO CO LO s _J < < co 3VJ eiueuBA 3V3 LO_ 00 CO K LO CM o> CO- Q LL X. O 0 O O co co LO LO IO LO LO _1 < < 0 CM oo CM LO co r- co — 0 > σ SJUUBA o LO O LO co 0 0 0 3 _1 < < co 3VJ CM r*. 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Claims

1. An isolated Cry1B variant polypeptide molecule characterized in that it comprises an amino acid sequence selected from SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, or SEQ ID NO: 29, and wherein the polypeptide molecule exhibits insecticidal activity against Spodoptera frugiperda (fall armyworm). Four claims follow.