Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2008-07-08
2008-07-08
Kubelik, Anne (Department: 1638)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C800S279000
Reexamination Certificate
active
07396813
ABSTRACT:
The subject invention pertains to the use of peptide fragments of cadherins (including cadherin-like proteins). The subject invention includes a cell (and use thereof) comprising a polynucleotide that expresses the peptide fragment. The subject invention includes methods of feeding the peptides to insects. In preferred embodiments, the peptides are fed to target insects together with one or more insecticidal proteins, preferably (but not limited to)B.t. Cry proteins. When used in this manner, the peptide fragment can not only enhance the apparent toxin activity of the Cry protein against the insect species that was the source of the receptor but also against other insect species. Preferably, the cadherin is aBacillus thuringiensis(B.t.) insecticidal crystal protein (Cry) toxin receptor. Preferably, the peptide fragment is a binding domain of the receptor. In some preferred embodiments, the peptide is the binding domain nearest to the membrane proximal ectodomain. Corresponding domains are identifiable in a variety ofB.t. toxin receptors.
REFERENCES:
patent: 5712248 (1998-01-01), Kalman et al.
patent: 6423502 (2002-07-01), Bulla
patent: 6455266 (2002-09-01), Bulla
patent: WO 01/34807 (2001-05-01), None
Lazar et al, 1988, Mol. Cell. Biol. 8:1247-1252.
Hill et al, 1998, Biochem. Biophys. Res. Comm. 244:573-577.
Guo et al, 2004, Proc. Natl. Acad. Sci. USA 101: 9205-9210.
Abdullah, M.A.F., et al., “Enhancement of Cry19Aa mosquitocidal activity againstAedes aegyptiby mutations . . . ,” Appl. Environ. Microbiol. (2004), pp. 3769-3771, vol. 70.
Abdullah, M.A.F., et al., “Introduction of Culex toxicity intoBacillus thuringiensisCry4Ba by protein engineering,” Appl. Environ. Microbiol. (2003), pp. 5343-5353, vol. 69.
Dorsch, J.A., et al., “Cry1A toxins ofBacillus thuringiensisbind specifically to a region adjacent . . . ,” Insect Biochem. Molec. Biol. (2002), pp. 1025-1036, vol. 32.
Francis, B.R., et al., “Further characterization of BT-R1, the cadherin-like receptor for Cry1Ab toxin . . . ,” Insect Biochem. Molec. Biol. (1997), pp. 541-550, vol. 27.
Gahan, L.J., et al., “Identification of a gene associated with B.t. resistance inHeliothis virescens,” Science (2001), pp. 857-860, vol. 293.
Gomez, B., et al., “Hydropathic complementarity determines interaction of epitope (869) HITDTNNK(876) inManduca sexta. . . ,” J. Biol. Chem. (2002), pp. 30137-30143, vol. 277.
Gomez, I., et al., “Molecular basis forBacillus thuringiensisCry1Ab toxin specificity: two structural determinants . . . ,” Biochem. (2003), pp. 10482-10489, vol. 42.
Gomez, I., et al., “Mapping the epitope in cadherin-like receptors involved inBacillus thuringiensisCry1A toxin . . . ,” J. Biol. Chem. (2001), pp. 28906-28912, vol. 276.
Gomez, I., et al., “Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer . . . ,” FEBS Lett. (2002), pp. 242-246, vol. 513.
Hara, H., et al., “A cadherin-like protein functions as a receptor forBacillus thuringiensisCry1Aa and Cry1Ac toxins on midgut . . . ,” FEBS Lett. (2003), pp. 29-34, vol. 538.
Hua, G., et al., “Fluorescent-based assays establish Manduca sexta Bt-R1a cadherin as a receptor for multiple . . . ,” Insect Biochem. Molec. Biol. (2004), pp. 193-202, vol. 34.
Keeton, T.P. et al., “Ligand specificity and affinity of BT-R1, theBacillus thuringiensistoxin receptor from . . . ,” Appl. Environ. Microbiol. (1997), pp. 3419-3425, vol. 63.
Morin, S. et al., “Three cadherin alleles associated with resistance toBacillus thuringiensisin pink bollworm,” Proc. Natl. Acad. Sci. U.S.A. (2003), pp. 5004-5009, vol. 100.
Nagamatsu, Y., et al., “Identification of Bombyx mori midgut receptor forBacillus thuringiensisinsecticidal . . . ,” Biosci. Biotechnol. Biochem. (1998), pp. 718-726, vol. 62.
Nagamatsu, Y., et al., “The cadherin-like protein is essential to specificity determination and cytotoxic action of the Bacillus . . . ,” FEBS Lett. (1999), pp. 385-390, vol. 460.
Tsuda, Y., et al., “Cytotoxic activity ofBacillus thuringiensisCry proteins on mammalian cells transfected with cadherin-like . . . ,” Biochem. J. (2003), pp. 697-703, vol. 369.
Vadlamudi, R.K., et al., “A specific binding protein from Manduca sexta for the insecticidal toxin of Bacillus . . . ,” J. Biol. Chem. (1993), pp. 12334-12340, vol. 268.
Vadlamudi, R.K., et al., “Cloning and expression of a receptor for an insecticidal toxin ofBacillus thuringiensis,” J. Biol. Chem. (1995), pp. 5490-5494, vol. 270.
Xie, R., et al., “Single amino acid mutations in the cadherin receptor from H.v. affects its toxin binding ability to Cry1A . . . ,” J. Biol. Chem. (2005), pp. 8416-8425, vol. 280.
Abdullah Mohd Amir Fursan
Adang Michael J.
Chen Jiang
Hua Gang
Kubelik Anne
Saliwanchik Lloyd & Saliwanchik
University of Georgia Research Foundation Inc.
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