Mutations of acetylcholinesterase which confer insecticide resistance in insect populations.
Resistance-modified acetylcholinesterases have been described in many insect species and sequencing of their genes has allowed several point mutations to be described. Most mutations line the active site gorge. Each mutation provides a specific resistance pattern: it confers resistance to one insecticide but may increase sensitivity to another. Most mutations alter hydrolysis of the substrate by decreasing the rate of enzyme deacetylation and by diminishing the stability of the enzyme. Mutations are often found in combination in the same protein. This has several consequences: it increases the level of resistance, it enlarges the spectrum of resistance and it may restore the catalytic efficiency of the enzyme. Natural populations are heterogeneous, composed of a mixture of different alleles.
Fournier
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IPBS, Biotechnologie des Proteines, 205 route de Narbonne, 31077 Toulouse, France. fournier@ipbs.fr
D000110:Acetylcholinesterase / Q000235:genetics* / Q000378:metabolism*; D000483:Alleles; D000818:Animals; D001483:Base Sequence; D004252:DNA Mutational Analysis; D004795:Enzyme Stability / Q000187:drug effects; D006868:Hydrolysis; D007313:Insecta / Q000187:drug effects* / Q000201:enzymology* / Q000235:genetics; D007305:Insecticide Resistance / Q000235:genetics*; D007306:Insecticides / Q000494:pharmacology*; D009154:Mutation / Q000235:genetics*; D011156:Population Density; D013379:Substrate Specificity
D007306:Insecticides; D000110:Acetylcholinesterase