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Sci Rep

Title:		Key site residues of pheromone-binding protein 1 involved in interacting with sex pheromone components of Helicoverpa armigera
Author(s):		Dong K; Duan HX; Liu JT; Sun L; Gu SH; Yang RN; Dhiloo KH; Gao XW; Zhang YJ; Guo YY;
Address:		"State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China. Department of Entomology, China Agricultural University, Beijing, 100193, China. College of Science, China Agricultural University, Beijing, 100193, China. Key Laboratory of Tea Biology and Resources Utilization, Ministry of Agriculture, Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, 310008, China. Department of Entomology, Faculty of Crop Protection, Sindh Agriculture University Tandojam, Tandojam, Pakistan. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China. yjzhang@ippcaas.cn"
Journal Title:		Sci Rep
Year:		2017
Volume:		20171204
Issue:		1
Page Number:		16859 -
DOI:		10.1038/s41598-017-17050-5
ISSN/ISBN:		2045-2322 (Electronic) 2045-2322 (Linking)
Abstract:		"Pheromone binding proteins (PBPs) are widely distributed in insect antennae, and play important roles in the perception of sex pheromones. However, the detail mechanism of interaction between PBPs and odorants remains in a black box. Here, a predicted 3D structure of PBP1 of the serious agricultural pest, Helicoverpa armigera (HarmPBP1) was constructed, and the key residues that contribute to binding with the major sex pheromone components of this pest, (Z)-11- hexadecenal (Z11-16:Ald) and (Z)-9- hexadecenal (Z9-16:Ald), were predicted by molecular docking. The results of molecular simulation suggest that hydrophobic interactions are the main linkage between HarmPBP1 and the two aldehydes, and four residues in the binding pocket (Phe12, Phe36, Trp37, and Phe119) may participate in binding with these two ligands. Then site-directed mutagenesis and fluorescence binding assays were performed, and significant decrease of the binding ability to both Z11-16:Ald and Z9-16:Ald was observed in three mutants of HarmPBP1 (F12A, W37A, and F119A). These results revealed that Phe12, Trp37, and Phe119 are the key residues of HarmPBP1 in binding with the Z11-16:Ald and Z9-16:Ald. This study provides new insights into the interactions between pheromone and PBP, and may serve as a foundation for better understanding of the pheromone recognition in moths"
Keywords:		"Aldehydes/chemistry/metabolism Amino Acid Sequence Animals Binding Sites Insect Proteins/chemistry/genetics/*metabolism Molecular Docking Simulation Moths/*metabolism Mutagenesis, Site-Directed Protein Binding Protein Structure, Tertiary Recombinant Prote;"
Notes:		"MedlineDong, Kun Duan, Hong-Xia Liu, Jing-Tao Sun, Liang Gu, Shao-Hua Yang, Ruo-Nan Dhiloo, Khalid Hussain Gao, Xi-Wu Zhang, Yong-Jun Guo, Yu-Yuan eng Research Support, Non-U.S. Gov't England 2017/12/06 Sci Rep. 2017 Dec 4; 7(1):16859. doi: 10.1038/s41598-017-17050-5"