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Genetics of an esterase associated with resistance to organophosphorus insecticides in the sheep blowfly, Lucilia cuprina (Wiedemann) (Diptera: Calliphoridae)

Published online by Cambridge University Press:  10 July 2009

P. B. Hughes  and
D. A. Raftos
P. B. Hughes
Affiliation:
Biological and Chemical Research Institute, Department of Agriculture, New South Wales, P.M.B. 10, P.O., Rydalmere, N.S.W. 2116, Australia
D. A. Raftos
Affiliation:
Biological and Chemical Research Institute, Department of Agriculture, New South Wales, P.M.B. 10, P.O., Rydalmere, N.S.W. 2116, Australia
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Abstract

Electrophoresis was used to characterize the esterases in Lucilia cuprina (Wiedemann). Of the 16 esterase bands visualized, only one was associated with resistance to organophosphorus insecticides. In laboratory reference strains, the esterase E3 was consistently found in both susceptible and heterozygously resistant flies, but was absent from homozygously resistant flies. It was postulated that resistant flies possessed a non-staining form of E3, designated E3null. Genetic analyses mapped the locus for E3null to a position in the same region as the gene for organophosphorus resistance. No recombinants between the genes for resistance and E3null were detected. In field populations of L. cuprina from several areas in Australia, a close association was found between the frequency of E (0·97) and the proportion of flies resistant to organophosphorus insecticide (0·967). This association suggests that E3null represents the product of a major resistance gene in terms of the ‘mutant ali-esterase’ theory. E3 as found in susceptible blowflies, represents the ‘original’ ali-esterase, the gene for which mutated to one coding for E3null. This mutant enzyme can hydrolyse organophosphates more efficiently than E3 but has lost the ability to hydrolyse 1- and 2-naphthyl acetate (the substrates used to visualize the esterases after electrophoresis).

Type
Original Articles
Information
Bulletin of Entomological Research , Volume 75 , Issue 3 , September 1985 , pp. 535 - 544
Copyright
Copyright © Cambridge University Press 1985

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