The amino acid Ser223 acts as a key site for the binding of Thrips palmi α1 nicotinic acetylcholine receptor to neonicotinoid insecticides

文献类型： 外文期刊

第一作者： Zhang, Kun

作者： Zhang, Kun;Chen, Jianwen;Huang, Huixiu;Wen, Huiqi;Geng, Junjie;Wu, Shaoying;Zhang, Kun;Chen, Jianwen;Huang, Huixiu;Wen, Huiqi;Geng, Junjie;Wu, Shaoying;Yang, Jingfang;Yang, Jingfang

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关键词： Thrips palmi; Nicotinic acetylcholine receptors; Neonicotinoids; Heterologous expression; Computer simulation

期刊名称：PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：4.0； 五年影响因子：4.5 ）

ISSN： 0048-3575

年卷期： 2025 年 213 卷

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收录情况： SCI

摘要： Thrips palmi (Karny) is a devastating pest on melons and vegetables worldwide. Neonicotinoids, which act on nicotinic acetylcholine receptors (nAChRs), are among the most effective insecticides for thrips control. For the high neonicotinoids resistance in T. palmi, it is urgent to clarify the main target subunits of neonicotinoid action and the molecular mechanism of subunits binding insecticides. In this study, we cloned two alpha subunits (alpha 1 and alpha 2) of T. palmi. T. palmi alpha 1/ Rattus norregicus beta 2 and T. palmi alpha 2/ R. norregicus beta 2 nAChR subtypes were successfully heterologous expressed in Xenopus laevis oocytes, respectively. After stimulation of the two receptor subtypes by each of the three neonicotinoids (imidacloprid, clothianidin and dinotefuran), for Tp alpha 1/r beta 2, dinotefuran showed the highest agonist affinity (pEC50) and efficacy (Imax), whereas for Tp alpha 2/r beta 2, dinotefuran showed the lowest agonist affinity, and the highest agonist efficacy was clothianidin. Overall, the agonist affinity and efficacy of Tp alpha 1/r beta 2 were greater than that of Tp alpha 2/r beta 2, which proved that alpha 1 subunit of T. palmi is the main target of neonicotinoids. Computer simulation and electrophysiological experiment results showed the different responses of the same neonicotinoid to two nAChR subtypes were mainly due to the difference between Lys220/ Ser223 in Tp alpha 1 and Arg223/Pro226 in Tp alpha 2, with Ser223 identified as the key binding site. This study revealed that the nAChR subunit of T. palmi binds to the key amino acid residues of neonicotinoid insecticides, which provides the basis for the subsequent design and synthesis of green and efficient specific insecticides.

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