Two major classes of target site insensitivity mutations confer resistance to organophosphate and carbamate insecticides

Russell, RJ, Claudianos, C, Campbell, PM, Horne, I, Sutherland, TD and Oakeshott, JG (2004) Two major classes of target site insensitivity mutations confer resistance to organophosphate and carbamate insecticides. Pesticide Biochemistry And Physiology, 79 3: 84-93. doi:10.1016/j.pestbp.2004.03.002


Author Russell, RJ
Claudianos, C
Campbell, PM
Horne, I
Sutherland, TD
Oakeshott, JG
Title Two major classes of target site insensitivity mutations confer resistance to organophosphate and carbamate insecticides
Journal name Pesticide Biochemistry And Physiology   Check publisher's open access policy
ISSN 0048-3575
Publication date 2004-01-01
Sub-type Article (original research)
DOI 10.1016/j.pestbp.2004.03.002
Open Access Status DOI
Volume 79
Issue 3
Start page 84
End page 93
Total pages 10
Place of publication San Diego
Publisher Academic Press Inc Elsevier Science
Language eng
Abstract Interspecific comparisons of bioassay and biochemical data suggest two major patterns of target site resistance to carbamates and organophosphates. Pattern I resistance, which is generally more effective for carbamates, has been shown in two sub-species of mosquitoes to be due to a particular Gly-Ser mutation in the oxyanion hole within the active site of one of their two acetylcholinesterase enzymes. Intriguingly, different substitutions at the equivalent site confer organophosphate hydrolytic ability on other esterases responsible for metabolic resistance in some other species. In the case of the aphid, Myzus persicae, Pattern I resistance is due to a Ser-Phe mutation in the vicinity of the acyl pocket of acetylcholinesterase. Pattern II resistance is at least as effective for organophosphates as it is for carbamates and may even be specific to organophosphates in some cases. Molecular studies on this pattern of resistance in three higher Diptera show that it is due to changes that constrict the acetylcholinesterase active site gorge and limit binding of the insecticide to the catalytic residues at the base of the gorge. One case of Pattern II resistance in the mosquito, Culex tritaeniorhynchus, involves the same site near the acyl pocket of acetylcholinesterase, albeit a different substitution, as that involved in Pattern I resistance in M. persicae. (C) 2004 Elsevier Inc. All rights reserved.
Keyword Biochemistry & Molecular Biology
Entomology
Physiology
acetylcholinesterase
insects
carbamates
organophosphates
target site resistance
Amino-acid Substitution
Aphis-gossypii Glover
Encoding Acetylcholinesterase
Nephotettix-cincticeps
Anopheles-sacharovi
Reduced Sensitivity
Mosquito Vectors
Lucilia-cuprina
Point Mutations
Myzus-persicae
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Queensland Brain Institute Publications
 
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Created: Wed, 17 Oct 2007, 23:00:25 EST