Comparison of an esterase associated with organophosphate resistance in Lucilia cuprina with an orthologue not associated with resistance in Drosophila melanogaster

Pesticide Biochemistry and Physiology

Volumn 55, Issue 2, 1996, Pages 85-99

  Parker, Anthony G ^a,b   Campbell, Peter M ^a   Spackman, Merrin E ^a   Russell, Robyn J ^a   Oakeshott, John G ^a  

^a CSIRO   (Australia)

^b AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

DROSOPHILA MELANOGASTER; FELIS CATUS; LUCILIA CUPRINA; MELANOGASTER;

EID: 0030158104     PISSN: 00483575     EISSN: None     Source Type: Journal    
DOI: 10.1006/pest.1996.0038     Document Type: Article

References (28)

1. 1. W. C. Dauterman, Insect metabolism: Extramicrosomal, in "Comprehensive Insect Physiology, Biochemistry and Pharmacology" (G. A. Kerkut and L. I. Gilbert, Eds.), pp. 713-730, Pergamon, Oxford, 1985.
2. 2. F. J. Oppenoorth, Biochemistry and genetics of insecticide resistance, in "Comprehensive Insect Physiology, Biochemistry and Pharmacology" (G. A. Kerkut and L. I. Gilbert, Eds.), pp. 731-773, Pergamon, Oxford, 1985.
3. 3. A. L. Devonshire, Role of esterases in resistance of insects to insecticides, Biochem. Soc. Trans. 19, 755 (1991).
4. 4. F. J. Oppenoorth and K. van Asperen, Allelic genes in the house fly producing modified enzymes that cause organophosphate resistance, Science 132, 298 (1960).
5. 5. M. G. Townsend and J. R. Busvine, The mechanism of malathion-resistance in the blowfly, Chrysomya putoria, Entomol. Exp. Appl. 12, 243 (1969).
6. 6. P. B. Hughes and D. A. Raftos, Genetics of an esterase associated with resistance to organophosphorous insecticides in the sheep blowfly, Lucilia cuprina (Weidemann) (Diptera: Calliphoridae), Bull. Entomol. Res. 75, 535 (1985).
7. 7. R. W. Beeman and B. A. Schmidt, Biochemical and genetic aspects of malathion-specific resistance in the Indianmeal moth (Lepidoptera: Pyralidae), J. Econ. Entomol. 75, 945 (1982).
8. 8. M. E. Spackman, J. G. Oakeshott, K. A. Smyth, K. M. Medveczky, and R. J. Russell, A cluster of esterase genes on chromosome 3R of Drosophila melanogaster includes homologues of esterase genes conferring insecticide resistance in Lucilia cuprina, Biochem. Genetics 32, 39 (1994).
9. 9. R. J. Russell, G. C. Robin, P. Kastakos, R. D. Newcomb, T. M. Boyce, K. M. Medveczky, and J. G. Oakeshott, Molecular cloning of an a esterase gene cluster on chromosome 3R of Drosophila melanogaster, Insect Biochem. Mol. Biol., 26, 235 (1996).
10. 10. A. G. Parker, R. J. Russell, A. C. Delves, and J. G. Oakeshott, Biochemistry and Physiology of esterases in organophosphate-susceptible and -resistant strains of the Australian sheep blowfly, Lucilia cuprina, Pestic. Biochem. Physiol. 41, 305 (1991).
11. 11. J. A. McKenzie, A. G. Parker, and J. L. Yen, Polygenic and single gene responses to selection for resistance to diazinon in Lucilia cuprina, Genetics 130, 613 (1992).
12. 12. M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248 (1976).
13. 13. U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680 (1970).
14. 14. W. Mastropaolo and J. Yourno, An ultraviolet spectrophotometric assay for α-naphthyl acetate and α-naphthyl butyrate esterases, Anal. Biochem. 115, 188 (1981).
15. 15. G. N. Wilkinson, Statistical estimations in enzyme kinetics, Biochem. J. 80, 324 (1961).
16. 16. M. J. Healy, M. M. Dumancic, and J. G. Oakeshott, Biochemical and physiological studies of soluble esterases from Drosophila melanogaster, Biochem. Genet. 29, 365 (1991).
17. 17. M. A. Gordon, D. E. Carpenter, H. W. Barrett, and I. B. Wilson, Determination of the normality of cholinesterase solutions, Anal. Biochem. 85, 519 (1978).
18. 18. M. Cygler, J. D. Schrag, J. L. Sussman, M. Harel, I. Silman, M. K. Gentry, and B. P. Doctor, Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases and related proteins, Protein Sci. 2, 366 (1993).
19. 19. M. K. Gentry and B. P. Doctor, Amino acid alignment of cholinesterases, esterases, lipases, and related proteins, in "Enzymes of the Cholinesterase Family" (D. M. Quinn, A. S. Balasubramanian, and P. Taylor, Eds.), pp. 493-505, Plenum, New York, 1995.
20. 20. R. D. Newcomb, P. M. Campbell, R. J. Russell, and J. G. Oakeshott, cDNA cloning, baculovirus-expression and kinetic properties of the esterase, E3, involved in organophosphate resistance in Lucilia cuprina, Insect Biochem. Mol. Biol., in press.
21. 21. D. M. Quinn, Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states, Chem. Rev. 87, 955 (1987).
22. 22. G. Gibney, S. Camp, M. Dionne, K. MacPhee-Quigley, and P. Taylor, Mutagenesis of essential functional residues in acetylcholinesterase, Proc. Natl. Acad. Sci. USA 87, 7546 (1990).
23. 23. S. D. Mane, C. S. Tepper, and R. C. Richmond, Studies of esterase 6 in Drosophila melanogaster XIII. Purification and characterization of the two major isozymes, Biochem. Genet. 21, 1019 (1983).
24. 24. M. W. White, S. D. Mane, and R. C. Richmond, Studies of esterase 6 in Drosophila melanogaster. XVIII Biochemical differences between the slow and fast allozymes, Mol. Biol. Evol. 5, 41 (1988).
25. 25. J. Pen, A. Schipper, H. A. H. Rongen, and J. J. Beintema, Differences in specificity and catalytic efficiency between allozymes of esterase-4 from Drosophila mojavensis, Mol. Biol. Evol. 3, 366 (1986).
26. 26. P. M. Campbell, "Characterization of Juvenile Hormone Esterase in Drosophila melanogaster," Ph.D. thesis, Australian National University, Canberra, 1993.
27. 27. K. van Asperen and F. J. Oppenoorth, The interaction between organophosphorus insecticides and esterases in homogenates of organophosphate susceptible and resistant houseflies, Entomol. Exp. Appl. 3, 68 (1960).
28. 28. J. L. Krysan and L. E. Chadwick, Bimolecular rate constants for organophosphorus inhibitors of fly head cholinesterase, Entomol. Exp. Appl. 5, 179 (1962).