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Organophosphorus insecticide interacts with the pheromone-binding proteins of Athetis lepigone: Implication for olfactory dysfunction

文献类型： 外文期刊

作者： Zhang, Ya-Nan 1 ; Xu, Ji-Wei 1 ; Zhang, Xiao-Chun 1 ; Zhang, Xiao-Qing 1 ; Li, Lu-Lu 1 ; Yuan, Xiaohui 2 ; Mang, Ding- 1 ;

作者机构： 1.Huaibei Normal Univ, Coll Life Sci, Anhui Prov Key Lab Pollutant Sensit Mat & Environ, Huaibei, Peoples R China

2.Jinan Univ, Inst Biomed, Guangzhou, Peoples R China

3.Zhuhai Trinomab Biotechnol Co Ltd, Zhuhai, Peoples R China

4.Tokyo Univ Agr & Technol, Grad Sch Bioapplicat & Syst Engn, Tokyo, Japan

5.Shandong Normal Univ, Coll Life Sci, Key Lab Anim Resistance Res, Jinan, Peoples R China

6.Agr Res Ctr, Bioassay Res Dept, Cent Agr Pesticide Lab, Sabahia Plant Protect Res Stn, Alexandria, Egypt

7.Jiangsu Acad Agr Sci, Inst Plant Protect, Key Lab Food Qual & Safety Jiangsu Prov, State Key Lab Breeding Base, Nanjing, Peoples R China

关键词： Pheromone binding protein; Phoxim; Fluorescence competitive binding assay; Computational simulation; Site-directed mutagenesis

期刊名称：JOURNAL OF HAZARDOUS MATERIALS （ 影响因子：10.588； 五年影响因子：10.129 ）

ISSN： 0304-3894

年卷期： 2020 年 397 卷

页码：

收录情况： SCI

摘要： Athetis lepigone is one of the most severe polyphagous pests, and it has developed resistance to different chemical insecticides. Insects primarily rely on the olfactory system to recognize various environmental chemicals, including xenobiotics such as insecticides. Here, we expressed two A. lepigone pheromone-binding proteins (AlepPBP2 and AlepPBP3), and observed they had higher binding affinities to phoxim than other insecticides, with Ki was 3.30 +/- 0.38 mu M and 3.27 +/- 0.10 mu M, respectively. Molecular dynamics simulation, binding mode analysis, and computational alanine scanning showed that six residues (Phe15, Phe39, Ile55, Leu65, Ile97, and Phe122) of AlepPBP2 and three residues (Phe12, Ile52, and Ile134) of AlepPBP3 maybe as potential residues that can change protein ability to bind an organophosphorus insecticide phoxim. Then, we used site-directed mutagenesis assay to mutate these residues into alanine, respectively. Subsequently, the binding assays displayed that Phe15, Phe39, and Ile97 of AlepPBP2, Phe12 and Ile134 of AlepPBP3 caused a significant decrease of AlepPBPs binding ability to phoxim, suggesting they should play crucial roles in the AlepPBPs/phoxim interactions. Our findings could further advance in using PBPs as unique targets to design and develop precise and environmentally-friendly pest control agents with high insecticidal potential using a computer-aided drug design (CADD) approach.

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