Dual mutations in the whitefly nicotinic acetylcholine receptor β1 subunit confer target-site resistance to multiple neonicotinoid insecticides
文献类型: 外文期刊
第一作者: Yin, Cheng
作者: Yin, Cheng;Liu, Shao-Nan;Du, Tian-Hua;Gong, Pei-Pan;Wei, Xue-Gao;Yang, Jing;Huang, Ming-Jiao;Fu, Bu-Li;Liang, Jin-Jin;Xue, Hu;Hu, Jin-Yu;Ji, Yao;He, Chao;Du, He;Wang, Chao;Zhang, Rong;Lu, Han-Tang;Xie, Wen;Yang, Xin;Zhang, You-Jun;Yin, Cheng;Gui, Lian-You;OReilly, Andrias O.;Zhang, Cheng-Jia;Tan, Qi-Mei;Chu, Dong;Zhou, Xu-Guo;Nauen, Ralf;Bass, Chris
作者机构:
期刊名称:PLOS GENETICS ( 影响因子:4.5; 五年影响因子:5.5 )
ISSN: 1553-7404
年卷期: 2024 年 20 卷 2 期
页码:
收录情况: SCI
摘要: Neonicotinoid insecticides, which target insect nicotinic acetylcholine receptors (nAChRs), have been widely and intensively used to control the whitefly, Bemisia tabaci, a highly damaging, globally distributed, crop pest. This has inevitably led to the emergence of populations with resistance to neonicotinoids. However, to date, there have been no reports of target-site resistance involving mutation of B. tabaci nAChR genes. Here we characterize the nAChR subunit gene family of B. tabaci and identify dual mutations (A58T&R79E) in one of these genes (BT beta 1) that confer resistance to multiple neonicotinoids. Transgenic D. melanogaster, where the native nAChR D beta 1 was replaced with BT beta 1(A58T&R79E), were significantly more resistant to neonicotinoids than flies where D beta 1 were replaced with the wildtype BT beta 1 sequence, demonstrating the causal role of the mutations in resistance. The two mutations identified in this study replace two amino acids that are highly conserved in >200 insect species. Three-dimensional modelling suggests a molecular mechanism for this resistance, whereby A58T forms a hydrogen bond with the R79E side chain, which positions its negatively-charged carboxylate group to electrostatically repulse a neonicotinoid at the orthosteric site. Together these findings describe the first case of target-site resistance to neonicotinoids in B. tabaci and provide insight into the molecular determinants of neonicotinoid binding and selectivity.
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