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Insecticidal Proteins and Methods for Their Use Insektizidproteine Und Verfahren Zu Deren Verwendung Protéines Insecticides Et Leurs Procédés D’Utilisation

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Insecticidal Proteins and Methods for Their Use Insektizidproteine Und Verfahren Zu Deren Verwendung Protéines Insecticides Et Leurs Procédés D’Utilisation (19) *EP003102684B1* (11) EP 3 102 684 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) Int Cl.: of the grant of the patent: C12N 15/82 (2006.01) C07K 14/415 (2006.01) 06.05.2020 Bulletin 2020/19 (86) International application number: (21) Application number: 15708059.9 PCT/US2015/014816 (22) Date of filing: 06.02.2015 (87) International publication number: WO 2015/120270 (13.08.2015 Gazette 2015/32) (54) INSECTICIDAL PROTEINS AND METHODS FOR THEIR USE INSEKTIZIDPROTEINE UND VERFAHREN ZU DEREN VERWENDUNG PROTÉINES INSECTICIDES ET LEURS PROCÉDÉS D’UTILISATION (84) Designated Contracting States: (74) Representative: J A Kemp LLP AL AT BE BG CH CY CZ DE DK EE ES FI FR GB 14 South Square GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO Gray’s Inn PL PT RO RS SE SI SK SM TR London WC1R 5JJ (GB) (30) Priority: 07.02.2014 US 201461937288 P (56) References cited: WO-A2-2013/098858 (43) Date of publication of application: 14.12.2016 Bulletin 2016/50 • H. K. ABICHT ET AL: "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic (73) Proprietors: Sulfate-Reducing Bacterium from Copper Mining • Pioneer Hi-Bred International, Inc. Waste in Norilsk, Northern Siberia", JOURNAL Johnston, Iowa 50131-1014 (US) OF BACTERIOLOGY, vol. 193, no. 21, 1 November • E. I. du Pont de Nemours and Company 2011 (2011-11-01), pages 6104-6105, Wilmington, DE 19805 (US) XP055196331, ISSN: 0021-9193, DOI: 10.1128/JB.06018-11 -& DATABASE UniProt (72) Inventors: [Online] 16 November 2011 (2011-11-16), • BARRY, Jennifer "SubName: Full=Uncharacterized protein Ames, Iowa 50014 (US) {ECO:0000313|EMBL:EGW36042.1};", • HAYES, Kevin XP002741068, retrieved from EBI accession no. Urbandale, Iowa 50323 (US) UNIPROT:G2G258 Database accession no. •LIU, Lu G2G258 Palo Alto, California 94301 (US) • TAMURA SAKI ET AL: "Purification, • SCHEPERS, Eric characterization and cDNA cloning of two Port Deposit, Maryland 21904 (US) natterin-like toxins from the skin secretion of • YALPANI, Nasser oriental catfish Plotosus lineatus", TOXICON, vol. Johnston, Iowa 50131 (US) 58, no. 5, October 2011 (2011-10), pages 430-438, XP28314820, ISSN: 0041-0101 Note: Within nine months of the publication of the mention of the grant of the European patent in the European Patent Bulletin, any person may give notice to the European Patent Office of opposition to that patent, in accordance with the Implementing Regulations. Notice of opposition shall not be deemed to have been filed until the opposition fee has been paid. (Art. 99(1) European Patent Convention). EP 3 102 684 B1 Printed by Jouve, 75001 PARIS (FR) EP 3 102 684 B1 Description FIELD 5 [0001] This disclosure relates to the field of molecular biology. Provided are novel genes that encode pesticidal proteins. These pesticidal proteins and the nucleic acid sequences that encode them are useful in preparing pesticidal formulations and in the production of transgenic pest-resistant plants. BACKGROUND 10 [0002] Biological control of insect pests of agricultural significance using a microbial agent, such as fungi, bacteria or another species of insect affords an environmentally friendly and commercially attractive alternative to synthetic chemical pesticides. Generally speaking, the use of biopesticides presents a lower risk of pollution and environmental hazards and biopesticides provide greater target specificity than is characteristic of traditional broad-spectrum chemical insecti- 15 cides. In addition, biopesticides often cost less to produce and thus improve economic yield for a wide variety of crops. [0003] Certain species of microorganisms of the genus Bacillus are known to possess pesticidal activity against a range of insect pests including Lepidoptera, Diptera, Coleoptera, Hemiptera and others. Bacillus thuringiensis (Bt) and Bacillus popilliae 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 and B. cereus. Microbial insecticides, particularly 20 those obtained from Bacillus strains, have played an important role in agriculture as alternatives to chemical pest control. [0004] Crop plants have been developed with enhanced insect resistance by genetically engineering crop plants to produce pesticidal proteins from Bacillus. For example, corn and cotton plants have been genetically engineered to produce pesticidal proteins isolated from strains of Bt. These genetically engineered crops are now widely used in agriculture and have provided the farmer with an environmentally friendly alternative to traditional insect-control methods. 25 While they have proven to be very successful commercially, these genetically engineered, insect-resistant crop plants provide resistance to only a narrow range of the economically important insect pests. In some cases, insects can develop resistance to different insecticidal compounds, which raises the need to identify alternative biological control agents for pest control. [0005] Accordingly, there remains a need for new pesticidal proteins with different ranges of insecticidal activity against 30 insect pests, e.g., insecticidal proteins which are active against a variety of insects in the order Lepidoptera and the order Coleoptera including but not limited to insect pests that have developed resistance to existing insecticides. [0006] WO2013/098858 A2 discloses a novel insecticidal chitinase protein, its encoding nucleotide and application thereof. 35 SUMMARY [0007] Compositions and methods for conferring pesticidal activity to bacteria, plants, plant cells, tissues and seeds are provided. Compositions include nucleic acid molecules encoding sequences for pesticidal and insecticidal polypep- tides, vectors comprising those nucleic acid molecules, and host cells comprising the vectors. Compositions also include 40 the pesticidal polypeptide sequences and antibodies to those polypeptides. The nucleic acid sequences can be used in DNA constructs or expression cassettes for transformation and expression in organisms, including microorganisms and plants. The nucleotide or amino acid sequences may be synthetic sequences that have been designed for expression in an organism including, but not limited to, a microorganism or a plant. Compositions also comprise transformed bacteria, plants, plant cells, tissues and seeds. 45 [0008] The invention provides a recombinant PtIP-50 polypeptide, wherein the amino acid sequence of the PtIP-50 polypeptide has: a) at least 80% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-50Aa as shown in Figures 10a-10o; 50 b) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-50Aa, PtIP-50Ba, PtIP-50Bb, PtIP-50Bc, or PtIP-50Bd as shown in Figures 10a-10o; c) at least 70% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-50Fb, PtIP-50Fs, PtIP-50Fo, PtIP-50Fk, PtIP-50Fe, PtIP-50FI, PtIP-50Fn, or PtIP-50Ft as shown in Figures 10a-10o; 55 d) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-50Fd, PtIP-50Fm, PtIP-50Fr, PtIP-50Fg, or PtIP-50Fh as shown in Figures 10a-10o; e) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-50Ga, PtIP-50Gb, PtIP-50Gc, or PtIP-50Gd as shown in Figures 10a-10o; or 2 EP 3 102 684 B1 f) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-50Fa, PtIP-50Ff, PtIP-50Fq, PtIP-50Fi, or PtIP-50Fj as shown in Figures 10a-10o; wherein the PtIP-50 polypeptide has insecticidal activity in combination with a PtIP-65 polypeptide as defined below. 5 [0009] The invention further provides a recombinant PtIP-65 polypeptide, wherein the amino acid sequence of the PtIP-65 polypeptide has: a) at least 80% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-65Aa as shown in Figures 17a-17k; 10 b) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-65Aa, PtIP-65Ba, PtIP-65Bb, or PtIP-65Ca as shown in Figures 17a-17k; c) at least 70% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-65Fa or PtIP-65Fb as shown in Figures 17a-17k; d) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid 15 sequence PtIP-65Ga, PtIP-65Gb, PtIP-65Gc, PtIP-65Ha, PtIP-65Gd, or PtIP-65Ge as shown in Figures 17a-17k; e) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-65Hh or PtIP-65Hg as shown in Figures 17a-17k; f) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-65Hb, PtIP-65Hc, PtIP-65Hd, PtIP-65He, or PtIP-65Hf as shown in Figures 17a-17k; or 20 g) at least 75% sequence identity, across the entire length of the amino acid sequence, compared to the amino acid sequence PtIP-65Hj or PtIP-65Hk as shown in Figures 17a-17k; wherein the PtIP-65 polypeptide has insecticidal activity in combination with a PtIP-50 polypeptide as defined above. [0010] Yet further provided by the invention is a polynucleotide encoding the PtIP-50 polypeptide or the PtIP-65 25 polypeptide as defined above. [0011] The invention further provides a composition comprising the PtIP-50 polypeptide as defined above and the PtIP-65 polypeptide as defined above. [0012] Yet further provided by the invention is a fusion protein comprising: 30 a) the PtIP-50 polypeptide as defined above; b) the PtIP-65 polypeptide as defined above; or c) the PtIP-50 polypeptide as defined above and the PtIP-65 polypeptide as defined above.
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