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Detection of insecticide resistance by immunological estimation of carboxylesterase activity in Myzus persicae (Sulzer) and cross reaction of the antiserum with Phorodon humuli (Schrank) (Hemiptera: Aphididae)

Published online by Cambridge University Press:  10 July 2009

A. L. Devonshire ,
G. D. Moores  and
R. H. Ffrench-Constant
A. L. Devonshire
Affiliation:
Rothamsted Experimental Station, Harpenden, Herts., UK
G. D. Moores
Affiliation:
Rothamsted Experimental Station, Harpenden, Herts., UK
R. H. Ffrench-Constant
Affiliation:
Rothamsted Experimental Station, Harpenden, Herts., UK
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Abstract

An antiserum was prepared against carboxylesterase E4, the enzyme conferring resistance in Myzus persicae (Sulzer) to a wide range of insecticides, and the immunoglobulin G (IgG) fraction was purified from it by affinity chromotography. Interactions of the antiserum and IgG with aphid homogenates and the purified esterase proteins were studied by immune diffusion, immunoelectrophoresis and enzyme-linked immunosorbent assay (ELISA). In M. persicae, the interactions were specific for E4 and its closely-related mutant form, FE4, and except for Phorodon humuli (Schrank), there was no cross-reaction with homogenates of the nine other aphid species examined. These studies confirmed the quantitative changes in E4 protein previously reported and established that the increased esterase activity in P. humuli also arises from the production of more protein, or proteins, homologous to E4. Resistance of M. persicae could be characterized by immunoelectrophoresis even after preservation of the insects in 30% ethanol. Although ELISA could also be used to identify resistance, a simpler immunoplate assay was developed based on measuring the esterase activity of E4 retained when the enzyme bound to IgG. This assay discriminates well between the three resistant M. persicae variants common in the field in the UK, and its simplicity allows the study of large numbers of insects.

Type
Original Articles
Information
Bulletin of Entomological Research , Volume 76 , Issue 1 , March 1986 , pp. 97 - 107
Copyright
Copyright © Cambridge University Press 1986

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