Biochemical and physiological differences in the malathion carboxylesterase activities of malathion-susceptible and -resistant lines of the sheep blowfly, Lucilia cuprina

Pesticide Biochemistry and Physiology

Volumn 54, Issue 1, 1996, Pages 48-55

  Smyth, Kerrie Ann ^a,b,d   Walker, Virginia K ^c   Russell, Robyn J ^a   Oakeshott, John G ^a  

^a CSIRO   (Australia)

^b AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

^c QUEEN S UNIVERSITY   (Canada)

^d SYRACUSE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0029801257     PISSN: 00483575     EISSN: None     Source Type: Journal    
DOI: 10.1006/pest.1996.0008     Document Type: Article

References (33)

1. 1. A. L. Devonshire and G. D. Moores, A carboxylesterase with broad substrate specificity causes organophosphorus, carbamate and pyrethroid resistance in peach-potato aphids (Myzus persicae), Pestic. Biochem. Physiol. 18, 235 (1982).
2. 2. C. Mouchès, N. Pasteur, J. B. Berge, O. Hyrien, M. Raymond, B. R. de Saint Vincent, M. de Silvestri, and G. P. Georghiou, Amplification of an esterase gene is responsible for insecticide resistance in a California Culex mosquito, Science 233, 778 (1986).
3. 3. L. M. Field, A. L. Devonshire, and B. G. Forde, Molecular evidence that insecticide resistance in peach-potato aphids (Myzus persicae Sulz.) results from amplification of an esterase gene, Biochem. J. 251, 309 (1988).
4. 4. F. J. Oppenoorth and K. van Asperen, Allelic genes in the housefly producing modified enzymes that cause organophosphate resistance, Science 132, 298 (1960).
5. 5. P. B. Hughes and D. A. Raftos, Genetics of an esterase associated with resistance to organophosphorus insecticides in the sheep blowfly, Lucilia cuprina (Wiedemann) (Diptera: Calliphoridae), Bull. Entomol. Res. 75, 535 (1985).
6. 6. M. Eto, "Organophosphorus Insecticides: Organic and Biological Chemistry," CRC Press, Cleveland, 1974.
7. 7. C. E. Dyte and D. G. Rowlands, The metabolism and synergism of malathion in resistant and susceptible strains of Tribolium castaneum (Herbst) (Coleoptera, Tenebrionidae), J. Stored Prod. Res. 4, 157 (1968).
8. 8. M. G. Townsend and J. R. Busvine, The mechanism of malathion resistance in the blowfly Chrysomyia putoria, Entomol. Exp. Appl. 12, 243 (1969).
9. 9. W. Welling and P. T. Blaakmeer, Metabolism of malathion in a resistant and susceptible strain of house-flies, in "International IUPAC Congress of Pesticide Chemistry" (A. S. Tahori, Ed.), pp. 61-75, Gordon and Breach Science, New York, 1971.
10. 10. M. I. Picollo de Villar, L. J. T. Van Der Pas, H. R. Smissaert, and F. J. Oppenoorth, An unusual type of malathion-carboxylesterase in a Japanese strain of house fly, Pestic. Biochem. Physiol. 19, 60 (1983).
11. 11. T. Shono, Linkage group analysis of carboxylesterase in a malathion resistant strain of the housefly, Musca domestica L. (Diptera: Muscidae), Appl. Entomol. Zool. 18, 407 (1983).
12. 12. 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).
13. 13. W. R. Halliday, Tissue specific esterase and malathion carboxylesterase activity in larvae of malathion-resistant Plodia interpunctella (Huber) (Lepidoptera: Pyralidae), J. Stored Prod. Res. 24, 91 (1988).
14. 14. J. Hemingway, The biochemical nature of malathion resistance in Anopheles stephensi from Pakistan, Pestic. Biochem. Physiol. 17, 149 (1982).
15. 15. S. Whyard, A. E. R. Downe, and V. K. Walker, Characterization of a novel esterase conferring insecticide resistance in the mosquito, Culex tarsalis, Arch. Insect Biochem. Physiol., in press.
16. 16. P. B. Hughes, P. E. Green, and K. G. Reichmann, Specific resistance to malathion in laboratory and field populations of the Australian sheep blowfly, Lucilia cuprina (Diptera: Calliphoridae), J. Econ. Entomol. 77, 1400 (1984).
17. 17. D. A. Raftos and P. B. Hughes, Genetic basis of a specific resistance to malathion in the Australian sheep blowfly, Lucilia cuprina (Diptera: Calliphoridae), J. Econ. Entomol. 79, 553 (1986).
18. 18. S. Whyard, R. J. Russell, J. G. Oakeshott, and V. K. Walker, Insecticide resistance and malathion carboxylesterase in the sheep blowfly, Lucilia cuprina, Biochem. Genet. 32, 9 (1994).
19. 19. K. A. Smyth, R. J. Russell, and J. G. Oakeshott, A cluster of at least three esterase genes in Lucilia cuprina includes malathion carboxylesterase and two other esterase genes implicated in resistance to organophosphates, Biochem. Genet. 32, 437 (1994).
20. 20. S. Whyard and V. K. Walker, Characterization of malathion carboxylesterase in the sheep blowfly, Lucilia cuprina, Pestic. Biochem. Physiol. 50, 198 (1994).
21. 21. G. G. Foster, M. J. Whitten, C. Konovalvov, J. T. A. Arnold, and G. Maffi, Autosomal genetic maps of the Australian sheep blowfly, Lucilia cuprina dorsalis R-D. (Diptera: Calliphoridae) and possible correlations with the linkage maps of Musca domestica L. and Drosophila melanogaster (Mg.), Genet. Res. Cambridge 37, 55 (1981).
22. 22. R. S. Ziegler, S. Whyard, A. E. R. Downe, G. R. Wyatt, and V. K. Walker, General esterase, malathion carboxylesterase, and malathion resistance in Culex tarsalis, Pestic. Biochem. Physiol. 28, 279 (1987).
23. 23. 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).
24. 24. D. B. Roberts, "Drosophila: A Practical Approach, " pp. 35, IRL Press, Oxford, 1986.
25. 25. B. D. Hammock, Y. A. I. Abdel-Aal, C. A. Mullin, T. N. Hanzlik, and R. M. Roe, Substituted thiotriflouropropanones as potent selective inhibitors of juvenile hormone esterase, Pestic. Biochem. Physiol. 22, 209 (1984).
26. 26. P. M. Campbell, M. J. Healy, and J. G. Oakeshott, Characterisation of juvenile hormone esterase in Drosophila melanogaster, Insect Biochem. Mol. Biol. 22, 665 (1992).
27. 27. S. Whyard, A. E. R. Downe, and V. K. Walker, Isolation of an esterase conferring insecticide resistance in the mosquito Culex tarsalis, Insect Biochem. Mol. Biol. 24, 819 (1994).
28. 28. V. B. Wigglesworth, "The Principles of Insect Physiology," Chapman and Hall, London, 1972.
29. 29. N. W. Aldridge, The esterases: Perspectives and problems, Chem.-Biol. Interact. 87, 5 (1993).
30. 30. 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).
31. 31. F. W. Plapp, Jr. and G. W. Eddy, Synergism of malathion against resistant insects, Science 334, 2043 (1961).
32. 32. F. W. Plapp, Jr., W. S. Bigley, G. A. Chapman, and G. W. Eddy, Synergism of malathion against resistant house flies and mosquitoes, J. Econ. Entomol. 56, 643 (1963).
33. 33. D. A. Raftos, The biochemical basis of malathion resistance in the sheep blowfly, Lucilia cuprina, Pestic. Biochem. Physiol. 26, 302 (1986).