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Associations between acetylcholinesterase-1 mutations and chlorpyrifos resistance in beet armyworm, Spodoptera exigua

文献类型： 外文期刊

作者： Teng, Haiyuan 1 ; Zuo, Yayun 1 ; Jin, Zeng 1 ; Wu, Yidong 1 ; Yang, Yihua 1 ;

作者机构： 1.Nanjing Agr Univ, Coll Plant Protect, Nanjing 210095, Peoples R China

2.Northwest A&F Univ, Coll Plant Protect, Inst Pesticide Sci, Yangling 712100, Shaanxi, Peoples R China

3.Shanghai Acad Agr Sci, Inst Ecoenvironm & Plant Protect, Shanghai 201403, Peoples R China

关键词： Acetylcholinesterase; Point mutation; Chlorpyrifos resistance; Beet armyworm; Organophosphate

期刊名称：PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：4.966； 五年影响因子：4.591 ）

ISSN： 0048-3575

年卷期： 2022 年 184 卷

页码：

收录情况： SCI

摘要： Control of the beet armyworm, Spodoptera exigua depends heavily on chemical insecticides. Chlorpyrifos, an acetylcholinesterase (AChE) inhibitor, has been used in beet armyworm control for many years in China. Here we describe high level resistance to chlorpyrifos in a S. exigua strain, FX19-R, which was developed from a field-collected Chinese strain (FX) by selection with chlorpyrifos in the laboratory. FX19-R showed 1001-fold resistance to chlorpyrifos compared with the laboratory reference strain WH-S. The esterase inhibitor triphenyl phosphate (TPP) provided significant but small synergism (only 3.5-fold) for chlorpyrifos and neither of the glutathione s-transferase depletor diethyl maleate and the cytochrome P450s inhibitor piperonyl butoxide provided any detectable synergism, indicating that AChE insensitivity may play the major role in the resistance in FX19-R. Consistent with this, an amino acid substitution, F443Y (F331Y in standard Torpedo californica numbering) in AChE1 was identified in the FX19-R strain and shown to be tightly linked to chlorpyrifos resistance. Precisely homologous substitutions have been associated with organophosphate resistance in other pest species. A novel amino acid substitution, G311S (or G198S in standard numbering), was also identified in the reference strain WH-S. Recombinantly expressed AChE1 proteins carrying the G311S and F443Y substitutions were about 4.2-fold and 210-fold less sensitive to inhibition by chlorpyrifos oxon than wild-type AChE1, respectively. These results enhance our understanding of the mechanisms of chlorpyrifos resistance and provide a basis for resistance management based on monitoring the F443Y and G311S substitutions.

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