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

Two major classes of target site insensitivity mutations confer resistance to organophosphate and carbamate insecticides
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DOI:
10.1016/j.pestbp.2004.03.002
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发表时间:
2004-07-01
影响因子:
4.7
通讯作者:
Oakeshott, JG
Oakeshott, JG
中科院分区:
农林科学1区
文献类型:
--
作者:
Russell, RJ;Claudianos, C;Oakeshott, JG

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生物测定和生化数据的种间比较表明,靶点对氨基甲酸盐和有机磷酸盐的抗性有两种主要模式。I型抗药性通常对氨基甲酸酯类更有效,在两个亚种蚊子中已被证明是由于它们的两种乙酰胆碱酯酶活性位点之一的氧阴离子孔中有一种特殊的Gly-Ser突变。有趣的是,在其他一些物种中,在等效位点上的不同取代赋予了其他酯酶对有机磷酸酯酶的水解能力,这些酯酶负责代谢抗性。以桃蚜为例,I型抗性是由于乙酰胆碱酯酶酰基袋附近的Ser-Phe突变。II型耐药至少对有机磷酸盐和氨基甲酸酯一样有效,在某些情况下甚至可能只对有机磷酸盐有效。对三种高等双翅目昆虫这种抗性模式的分子研究表明,这是由于乙酰胆碱酯酶活性位点峡谷收缩的变化,限制了杀虫剂与峡谷底部催化残基的结合。三带喙库蚊的一例II型耐药涉及到与桃姬蚊的I型耐药位点不同的乙酰胆碱酯酶酰基袋附近的同一位点。(C) 2004爱思唯尔公司版权所有。
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.