Plant Genetic Systems N.v.

Bayer Bioscience N.v.

Aventis Cropscience Gmbh

Aventis Cropscience, N.v.

Biotalys Nv

Marnix Peferoen

Bart J Lambert

Stefan K Jansens

Katrien Van Audenhove

Jeroen Van Rie

Peter Verheesen

Roel Van Aarssen

Henk Joos

Peter Denolf

Johan Botterman

Inge Elodie Van Daele

Herman Hofte

João Filipe Veloso Vieira

Jan Geerinck

Van RIE;Jeroen

Four novelstrains, which are deposited at the BCCM-LMG under accession nos. LMG P-12592, LMG P-12593, LMG P-12594, and LMG P-13493, produce new crystal proteins during sporulation that are toxic to Lepidoptera, more particularly against Noctuidae such asspp. and, against Pyralidae such as, and against Yponomeutidae such as, and that are encoded by a novel gene. The crystal proteins contain protoxins, which can yield a toxin as trypsin-digestion product. A plant, the genome of which is transformed with a DNA sequence that comes from either one of the strains and that encodes its respective toxin, is resistant to Lepidoptera. Each strain, itself, or its crystals, crystal proteins, protoxin or toxin can be used as the active ingredient in an insecticidal composition for combatting Lepidoptera.

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Four novelstrains, which are deposited at the BCCM-LMG under accession nos. LMG P-12592, LMG P-12593, LMG P-12594, and LMG P-13493, produce new crystal proteins during sporulation that are toxic to, more particularly against Noctuidae such asspp. and, against Pyralidae such as, and against Yponomeutidae such as, and that are encoded by a novel gene. The crystal proteins contain protoxins, which can yield a toxin as trypsin-digestion product. A plant, the genome of which is transformed with a DNA sequence that comes from either one of the strains and that encodes its respective toxin, is resistant to. Each strain, itself, or its crystals, crystal proteins, protoxin or toxin can be used as the active ingredient in an insecticidal composition for combatting

Four novel strains, which are deposited at the BCCM-LMG under accession nos. LMG P-12592, LMG P-12593, LMG P-12594, and LMG P-13493, produce new crystal proteins during sporulation that are toxic to Lepidoptera, more particularly against Noctuidae such as Spodoptera spp. and , against Pyralidae such as , and against Yponomeutidae such as , and that are encoded by a novel gene. The crystal proteins contain protoxins, which can yield a toxin as trypsin-digestion product. A plant, the genome of which is transformed with a DNA sequence that comes from either one of the strains and that encodes its respective toxin, is resistant to Lepidoptera. Each strain, itself, or its crystals, crystal proteins, protoxin or toxin can be used as the active ingredient in an insecticidal composition for combatting Lepidoptera.

Bacillus thuringiensis strains and their insecticidal proteins

The present invention relates to transformed plants and plant cells comprising DNA molecules encoding proteins with insecticidal activity. The invention relates more particularly to transformed plants and plant cells comprising DNA molecules encoding the protease resistant toxins BTS02618Aa or BTS02618Ab, as well as to methods of rendering plants or plant cells resistant to insects using these DNA molecules.

The present invention relates to transformed microrganisms comprising DNA molecules encoding Bacillus thuringiensis proteins with insecticidal activity. The invention relates more particularly to transformed microrganisms comprising DNA molecules encoding the protease resistant toxins BTS02618Aa or BTS02618Ab.

Four novel Bacillus thuringiensis strains, which are deposited at the BCCM-LMG under accession nos. LMG P-12592, LMG P-12593, LMG P-12594, and LMG P-13493, produce new crystal proteins during sporulation that are toxic to Lepidoptera, more particularly against Noctuidae such as spodoptera spp. and Agotis ipsilon, against Pyralidae such as Ostrinia nubilalis, and against Yponomeutidae such as Plutella xylostella, and that are encoded by a novel gene. The crystal proteins contain protoxins, which can yield a toxin as trypsin-digestion product. A plant, the genome of which is transformed with a DNA sequence that comes from either one of the strains nd that encodes its respective toxin, is resistant to Lipidoptera. Each strain, itself, or its crystal, crystal protein, protoxin or toxin can be used as the active ingredient in an insecticidal composition for combating Lepidoptera.

Two new Bacillus thuringiensis strains, which are deposited at the DSM under accession numbers 5870 and 5871, produce new crystal proteins during sporulation that are toxic to Coleoptera and that are encoded by new genes. The crystal proteins contain protoxins, which can yield toxins as trypsin-digestion products. A plant, the genome of which is transformed with a DNA sequence that comes from either one of the strains and encodes an insecticidally effective portion of its respective protoxin or encodes its respective toxin, is resistant to Coleoptera. Each strain, itself, or its crystals, crystal proteins, protoxin, toxin and/or insecticidally effective protoxin portion can be used as the active ingredient in an insecticidal composition for combatting Coleoptera.

Bacillus thuringiensis strains and their genes encoding insecticidal

Two new Bacillus thuringiensis strains, which are deposited at the DSM under accession nos. 5131 and 5132, produce crystal proteins during sporulation that are toxic to Coleoptera. The crystal proteins contain 74 kDa and 129 kDa protoxins, respectively, which can yield 68 and 66 kDa toxins, respectively, as trypsin-digestion products. A plant, the genome of which is transformed with a DNA sequence that comes from either one of the strains and that codes for its respective toxin, is resistant to Coleoptera. Each strain, itself, or its crystals, crystal proteins, protoxin or toxin can be used as the active ingredient in an insecticidal composition for combatting Coleoptera.

Bacillus thuringiensis insecticidal toxins

New modified Cry proteins, particularly modified CryIIIA proteins, having significantly altered toxicity, and DNA sequences encoding these proteins, are designed. Analysis of solvent-accessible amino acid positions in domain II of the CryIIIA protein by alanine-scanning mutagenesis identified individual amino acids involved in corn rootworm toxicity. Random replacement of these amino acids identifies modified proteins with improved toxicity. A combination of all or most thus identified improved amino acids in a single protein yields modified CryIIIA proteins with significantly improved toxicity. Particularly regions protruding from the Cry molecule and located at the apex of the Cry proteins, were identified as involved in toxicity.

Diabrotica toxins

A method to combat or control Ostrinia nubilalis by contacting such insects with a CryIB protein or a combination of a CryIB protein and a CryIAb or CryIAc protein.

Growing community of inventors

Ghent, Belgium

Marnix Peferoen