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J Hazard Mater


Title:Organophosphorus insecticide interacts with the pheromone-binding proteins of Athetis lepigone: Implication for olfactory dysfunction
Author(s):Zhang YN; Xu JW; Zhang XC; Zhang XQ; Li LL; Yuan X; Mang DZ; Zhu XY; Zhang F; Dewer Y; Xu L; Wu XM;
Address:"Anhui Province Key Laboratory of Pollutant Sensitive Materials and Environmental Remediation, College of Life Sciences, Huaibei Normal University, Huaibei, China. Electronic address: ynzhang_insect@163.com. Anhui Province Key Laboratory of Pollutant Sensitive Materials and Environmental Remediation, College of Life Sciences, Huaibei Normal University, Huaibei, China. Institute of Biomedicine, Jinan University, Guangzhou, China; Zhuhai Trinomab Biotechnology Co., Ltd., Zhuhai, China. Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Tokyo, Japan. Key Laboratory of Animal Resistance Research, College of Life Science, Shandong Normal University, Jinan, China. Bioassay Research Department, Central Agricultural Pesticide Laboratory, Sabahia Plant Protection Research Station, Agricultural Research Center, Alexandria, Egypt. Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Lab of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, China. Electronic address: xulupesticide@163.com. Anhui Province Key Laboratory of Pollutant Sensitive Materials and Environmental Remediation, College of Life Sciences, Huaibei Normal University, Huaibei, China. Electronic address: dolphin1009@sina.com"
Journal Title:J Hazard Mater
Year:2020
Volume:20200421
Issue:
Page Number:122777 -
DOI: 10.1016/j.jhazmat.2020.122777
ISSN/ISBN:1873-3336 (Electronic) 0304-3894 (Linking)
Abstract:"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?ª++/-?ª+0.38?ª+muM and 3.27?ª++/-?ª+0.10?ª+muM, 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"
Keywords:Animals Carrier Proteins Insect Proteins/genetics/metabolism *Insecticides/toxicity *Olfaction Disorders Pheromones Computational simulation Fluorescence competitive binding assay Pheromone binding protein Phoxim Site-directed mutagenesis;
Notes:"MedlineZhang, Ya-Nan Xu, Ji-Wei Zhang, Xiao-Chun Zhang, Xiao-Qing Li, Lu-Lu Yuan, Xiaohui Mang, Ding-Ze Zhu, Xiu-Yun Zhang, Fan Dewer, Youssef Xu, Lu Wu, Xiao-Min eng Research Support, Non-U.S. Gov't Netherlands 2020/05/11 J Hazard Mater. 2020 Oct 5; 397:122777. doi: 10.1016/j.jhazmat.2020.122777. Epub 2020 Apr 21"

 
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