Methods and materials for identifying novel pesticide agents

Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of... – Insect cell – per se

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C435S023000

Reexamination Certificate

active

07011975

ABSTRACT:
Materials and methods for identifying novel pesticide agents are disclosed herein. Specifically exemplified is a full length aminopeptidase N isolated fromManduca sexta, insect cells expressing APN, and methods of screening pesticide agents using the same. Also disclosed are methods of identifying novel APN inhibitors.

REFERENCES:
Scoazec, J-Y., et al. (1997) J. Hepatol. 26, 543-553.
Wessels, H. P., et al. (1990) J. Cell Biol. 111, 2923-2930.
Ayres, M.D., et al., “The complete DNA sequence ofAutograph californicanuclear polyhedrosis virus,” Virology (1994), pp. 586-605, vol. 202.
Benbacer, L., et al., “Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition . . . ,” J. Virol. (1997), pp. 734-737, vol. 71.
Chaudhri, M., et al., “Expression of glycosylphosphadylinositol-anchoredTrypanosoma brucei. . . ,” Proc. Natl. Acad. Sci. USA (1994), pp. 6443-6447, vol. 91.
Davies, A., et al., “Expression of the glycosylphosphatidlinositol-linked complement-inhibiting protein . . . ,” Biochemical Journal (1993), pp. 889-896, vol. 295.
Delmas, B., et al., “Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV,” Nature (1992), pp. 417-419, vol. 357.
Denolf, P., et al., “Cloning and characterization ofManduca sextaandPlutella xylostellamidgut aminopeptidase N . . . ” Eur. J. Biochem. (1997), pp. 748-761, vol. 248.
Ferre, J., et al., “Resistance to theBacillus thuringiensisbioinsecticide in a field population . . . ” Proc. Natl. Acad. Sci. USA (1991), pp. 5119-5123, vol. 88.
Fujii, H., et al., “Human melanoma invasion and metastasis enhancement by high expression of aminopeptidase N/CD13.” Clin. Exp. Metast. (1995), pp. 337-344, vol. 13.
Garczynski, S.F., et al., “Bacillus thuringiensisCrylA(c) d-endotoxin binding aminopeptidase in the . . . ,” Insect Biochem. Mol. Biol. (1995), pp. 409-415, vol. 25.
Garczynski, S.F., et al., “Identification of putative brush border membrane binding proteins . . . ,” Appl. Environ. Microbiol. (1991), pp. 2816-2820, vol. 57.
Gill, S., et al., “Identification, isolation, and cloning of aBacillus thuringiensisCrylAc toxin-binding protein . . . ,” J. Biol. Chem. (1995), pp. 27277-27282, vol. 270.
Hua, G., et al., “Molecular cloning of a GPI-anchored aminopeptidase N fromBombyx morimidgut . . . ,” Gene (1998), pp. 177-185, vol. 214.
Kennard, M.L., et al., “Expression of cell surface GPI-anchored human p97 in baculovirus-infected insect cells,” Biotech. Bioeng. (1997), pp. 41-53, vol. 55.
Kenny, A.J., et al., “Cell surface peptidases,” Mammalian Ectoenzymes (1987), pp. 169-210, Elsevier, Amsterdam (A.J. Kenny and A.J. Turner, eds.).
Knight, P.J.K., et al., “The receptor forBacillus thuringiensisCrylA(c) delta-endotoxin in the brush border membrane . . . ,” Mol. Microbiol. (1994), pp. 429-436, vol. 11.
Knight, P.J.K., et al., “Molecular cloning of an insect aminopeptidase N that serves as a receptor . . . ,” J. Biol. Chem. (1995), pp. 17765-17770, vol. 270.
Kolb, A.F., et al., “Characterization of functional domains in the human coronavirus HCV 229E receptor,” J. Gen. Virol. (1996), pp. 2515-2521, vol. 77.
Kozak, M., “An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs,” Nucl. Acids Res. (1987), pp. 8125-8132, vol. 15.
Laemmli, U.K., “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature (1970), pp. 680-685, vol. 227.
Look, A.T. et al., “Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N,” J. Clin. Invest. (1989), pp. 1299-1307, vol. 83.
Lu, Y., et al., “Conversion ofBacillus thuringiensisCrylAc-binding aminopeptidase to a soluble form . . . ,” Insect Biochem. Molec. Biol. (1996), pp. 33-40, vol. 26.
Luo, K., et al., “A 106 kDa form of aminopeptidase is a receptor forBacillus thuringiensisCrylC . . . ,” Insect Biochem. Mol. Biol. (1996), pp. 783-791, vol. 26.
Luo, K., et al., “TheHeliothis virescens170-kDa aminopeptidase functions as ‘Receptor A’. . . ,” Insect Biochem. Mol. Biol. (1997a), pp. 735-743, vol. 27 (8/9).
Luo, K., et al., “Binding ofBacillus thuringiensisCry1Ac toxin to aminopeptidase in susceptible and resistant . . . ,” Appl. Environ. Microbiol. (1997b), pp. 1024-1027, vol. 63.
Luo, K., et al., “Expression of a glycosylphosphatidylinositol-linkedManduca sextaaminopeptidase N . . . ,” Protein Expression and Purification (1999), pp. 113-122, vol. 17.
Masson, L., et al., “The CrylA(c) receptor purified fromManduca sextadisplays multiple specificities,” J. Biol. Chem. (1995), pp. 20309-20315, vol. 270.
McConville, M.J., et al., “The structure, biosynthesis and function of glycosylated phosphatidylinositols . . . ,” Biochemical Journal (1993), pp. 305-324, vol. 294.
McLaughlin, S., et al., “The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions,” TIBS (1995), pp. 272-276, vol. 20.
Morris, T.D., et al., “Promoter influence on baculovirus-mediated gene expression in permissive and non-permissive insect cell lines,” J. Virol. (1992), pp. 7397-7405, vol. 66.
Plakidou-Dymock, S., et al., “A role for aminopeptidase N in Na +- dependent amino acid transport in bovine renal brush-border . . . ,” Biochem. J. (1993), pp. 59-65, vol. 290.
Richardson, M.A., et al., “Native and baculovirus-expressed forms of the Immunoprotective protein BM86 from . . . ,” Insect Mol. Biol. (1993), pp. 139-147, vol. 1.
Sangadala, S., et al., “A mixture ofManduca sextaaminopeptidase and alkaline phosphatase enhancesBacillus. . . ,” J. Biol. Chem. (1994), pp. 10088-10092, vol. 269.
Schwartz, J.-L., et al., “Ion channels formed in planar lipid bilayers byBacillus thuringiensistoxins in the presence of . . . ,” FEBS Lett. (1997), pp. 270-276, vol. 412.
Takasaki, S., et al., “N-linked neutral sugar chains of aminopeptidase N purified from rat small intestinal brush-border membrane,” Biochem. (1991), pp. 9102-9110, vol. 30.
Tomita, M., et al., “Purification of glycosylphosphatidylinositol-anchoring aminopeptidase N from the plasma . . . ,” Int. J. Biochem. (1994), pp. 977-986, vol. 26.
Towbin, H., et al., “Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets . . . ,” Proc. Natl. Acad. Sci. USA (1979), pp. 4350-4354, vol. 76.
Tresnan, N.B., et al., “Feline aminopeptidase N serve as a receptor for feline, canine, porcine, and human coronaviruses . . . ,” J. Virol. (1996), pp. 8669-8674, vol. 70.
Valaitis, A., et al., “Brush border membrane aminopeptidase-N in the midgut of the gypsy moth serves as . . . ,” Insect Biochem. Molec. Biol. (1995), pp. 1143-1151, vol. 25.
Vaughn, J.L., et al., “The establishment of two insect cell lines from the insectSpodoptera frugiperda. . . ,” In Vitro Cell. Dev. Biol. (1977), pp. 213-217, vol. 13.
Wolfersberger, M.G., et al., “Preparation and partial characterization of amino acid transporting brush border . . . ,” Comp. Biochem. Physiol. (1987), pp. 301-308, vol. 86A.
Yaoi, K., et al., “Aminopeptidase N fromBombyx morias a candidate for the receptor ofBacillus thuringiensisCry1Aa toxin,” Eur. J. Biochem. (1997), pp. 652-657, vol. 246.
Yeager, C.L., et al., “Human aminopeptidase N is a receptor for human coronavirus 229E,” Nature (1992), pp. 420-422, vol. 357.

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