Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2007-10-02
2007-10-02
Carlson, Karen Cochrane (Department: 1656)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Reexamination Certificate
active
11294220
ABSTRACT:
Compositions and methods for controlling plant pests are disclosed. In particular, novel nucleic acid sequences encoding modified Cry3A toxins having increased toxicity to corn rootworm are provided. By inserting a protease recognition site, such as cathepsin G, that is recognized by a gut protease of a target insect in at least one position of a Cry3A toxin a modified Cry3A toxin having significantly greater toxicity, particularly to western and northern corn rootworm is designed. Further, a method of making the modified Cry3A toxins and methods of using the modified cry3A nucleic acid sequences, for example in microorganisms to control insects or in transgenic plants to confer protection from insect damage, and a method of using the modified Cry3A toxins, and compositions and formulations comprising the modified Cry3A toxins, for example applying the modified Cry3A toxins or compositions or formulations to insect-infested areas, or to prophylactically treat insect-susceptible areas or plants to confer protection against the insect pests are disclosed.
REFERENCES:
patent: 5659123 (1997-08-01), Van Rie et al.
patent: 5763241 (1998-06-01), Fischhoff et al.
patent: 6063597 (2000-05-01), Walters et al.
patent: 7030295 (2006-04-01), Chen et al.
patent: WO99/00407 (1999-01-01), None
patent: WO99/31248 (1999-06-01), None
Adang et al, The reconstruction and expression of aBacillus thuringiensiscryIIIA gene in protoplasts and potato plantsPlant Molecular Biology, vol. 21 (1993), pp. 1131-1145.
Carroll et al, Proteolytic processing of a coleopteran-specific δ-endotoxin produced byBacillus thuringiensisvar.tenebrionis Biochemical Journal, vol. 26 (1989), pp. 99-105.
Carroll et al., Intramolecular Proteolytic Cleavage ofBacillus thuringiensisCry3A δ-Endotoxin May Facilitate Its Coleopteran ToxicityJournal of Invertebrate Pathology, vol. 70 (1997) pp. 41-49.
Gazit et al, The structure and organization within the membrane of the helices composing the pore-forming domain ofBacillus thuringiensisδ-endotoxin are consistent with an “umbrella-like” structure of the poreProceedings of the National Academy of Sciences, USA, vol. 95 (Oct. 1998), pp. 12289-12294.
Gazit, E. and Shai, Y., The Assembly and Organization of the α5 and α7 Helices from the Pore-forming Domain ofBacillus thuringiensisδ-endotoxinThe Journal of Biological Chemistry, vol. 270, No. 6 (Feb. 10, 1995), pp. 2571-2578.
Gillikin et al, Partial Characterization of Digestive Tract Proteinases from Western Corn Rootworm Larvae,Diabrotica virgifera Archives of Insect Biochemistry and Physiology, vol. 19 (1992), pp. 285-298.
Li et al, Crystal structure of insecticidal δ-endotoxin fromBacillus thuringiensisat 2.5 Å resolutionNature, vol. 353 (Oct. 31, 1991), pp. 815-821.
Martinez-Ramirez, A.C. and Real M.D., Proteolytic Processing ofBacillus thuringiensisCryIIIA Toxin and Specific Binding to Brush-Border Membrane Vesicles ofLeptinotarsa decemlineata(Colorado Potato Beetle)Pesticide Biochemistry and Physiology, vol. 54 (1996), pp. 115-122, Article, No. 0015.
McPherson et al, Characterization of the Cleopteran-Specific Protein Gene ofBacillus thuringiensisvar.tenebrionis Bio/Technology, vol. 6 (1988), pp. 61-66.
Oppert, B., Protease Interactions WithBacillus thuringiensisInsecticidal ToxinsArchives of Insect Biochemistry and Physiology, vol. 42 (1999), pp. 1-12.
Sekar et al., Molecular cloning and characterization of the insecticidal crystal protein gene ofBacillus thuringiensisvar.tenebrionis Proceedings of the National Academy of Sciences, USA, vol. 84 (Oct. 1987), pp. 7036-7040.
Slaney et al, Mode of Action ofBacillus thuringiensisToxin CryIIIA: An Analysis of Toxicity inLeptinotarsa decemlineata(Say) andDiabrotica undecimpunctataHowardi BarberInsect Biochemistry Molecular Biology, vol. 22, No. 1 (1992), pp. 9-18.
Sutton et al, Synthetic cryIIIA gene formBacillus thuringiensisimproved for high expression in plantsTransgenic Research, vol. 1 (1992), pp. 228-236.
Wu, S.J., Dean, D.H., Functional Significance of Loops in The Receptor Binding Domain ofBacillus thuringiensisCryIIIA δ-EndotoxinJournal of Molecular Biology, vol. 255 (1996), pp. 628-640.
Wu et al, Enhanced toxicity ofBacillus thuringiensisCry3A δ-Endotoxin on coleopterans by mutagenesis in a receptor binding loopFederation of European Biochemical Societies Letters, vol. 473 (2000), pp. 227-232.
Haider et al, Specificity ofBacillus thuringiensisvar.colmeriInsecticidal Delta-Endotoxin in Determined by Differential Proteolytic Processing of the Protoxin by Larval Gut ProteasesEuropean Journal of Biochemistry, vol. 156, No. 3 (May 1, 1986), pp. 531-540.
Smedley et al, Mutagenesis of three surface-exposed loops of aBacillus thuringiensisinsecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertionSociety for General Microbiology, vol. 142, No. Part 7 (Jul. 1996), vol. 1617-1624.
Chen Eric
Stacy Cheryl
Carlson Karen Cochrane
Syngenta Participations (AG)
Warren Gregory W.
LandOfFree
Modified Cry3A toxins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Modified Cry3A toxins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Modified Cry3A toxins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3824798