Amino acid substitution in Ace paralogous acetylcholinesterase accompanied by organophosphate resistance in the spider mite Tetranychus kanzawai
Amino acid substitution in Ace paralogous acetylcholinesterase accompanied by organophosphate resistance in the spider mite Tetranychus kanzawai
复制标题
DOI：
10.1016/j.pestbp.2005.02.004
复制
发表时间：
2005-06-01
影响因子：
4.7
通讯作者：
Kono, Y
中科院分区：
文献类型：
--
作者：
Aiki, Y;Kozaki, T;Kono, Y
具有不敏感乙酰胆碱酯酶（AChE）的kanzawa叶螨（Tetranychus kanzawai）耐杀虫剂菌株在日本各地广泛传播。为了阐明这种不敏感的分子机制，基于荨麻疹叶螨AChE cDNA序列和两种螨的AChE序列比较，测定了耐药菌株的乙酰胆碱酯酶（AChE） cDNA。cDNA编码AChE一级结构的687个氨基酸，与荨麻疹具有较高的同源性。氨基酸同源性表明该乙酰胆碱酯酶是昆虫乙酰胆碱酯酶的一类同源型。两种氨基酸之间仅存在3个氨基酸残基的取代。在耐药菌株的乙酰胆碱酯酶（AChE）中，3个氨基酸替换中有1个是位于酶活性位点酰基袋内的Phe439Trp。鉴于在三带喙库蚊抗性品系中，在Ace类乙酰胆碱酯酶的等效位置发现了相同的取代，推测Phe439Trp取代可能是螨虫乙酰胆碱酯酶不敏感的重要原因。(c) 2005爱思唯尔公司版权所有。
Insecticide resistant strains of the kanzawa spider mite, Tetranychus kanzawai, with insensitive AChE have spread widely throughout Japan. To clarify the molecular mechanism of this insensitivity, acetylcholinesterase (AChE) cDNA of the resistant strains of T. kanzawai was determined based on the AChE cDNA sequence of Tetranychus urticae and the sequences compared between the two spider mite species. The cDNA encoded 687 amino acids of AChE primary structure showing high homology to T. urticae. Amino acid homology indicated that the AChE is an Ace paralogous type of insect AChE. There were only three substitutions of amino acid residues between the AChEs of the two species. In the AChE of the resistant strain of T. kanzawai, one of the three amino acid substitutions was Phe439Trp, which lines the acyl pocket of the enzyme active site. Considering that the same substitution was found at the equivalent position of Ace paralogous AChE in the resistant strain of Culex tritaeniorhynchus, Phe439Trp substitution likely plays an important role in the insecticide insensitivity of the mite AChE. (c) 2005 Elsevier Inc. All rights reserved.