| Title: | Functional Disparity of Three Pheromone-Binding Proteins to Different Sex Pheromone Components in Hyphantria cunea (Drury) |
| Author(s): | Zhang XQ; Mang DZ; Liao H; Ye J; Qian JL; Dong SL; Zhang YN; He P; Zhang QH; Purba ER; Zhang LW; |
| Address: | "Anhui Provincial Key Laboratory of Microbial Control, Engineering Research Center of Fungal Biotechnology, Ministry of Education School of Forestry & Landscape Architecture, Anhui Agricultural University, Hefei 230036, China. Education Ministry, Key Laboratory of Integrated Management of Crop Diseases and Pests, College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei 2-24-16, Tokyo 184-8588, Japan. College of Life Sciences, Huaibei Normal University, Huaibei 235000, China. State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Huaxi District, Guiyang 550025, China. Sterling International, Inc., Spokane, Washington 99216, United States. Structural Cellular Biology Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa 904-0495, Japan" |
| ISSN/ISBN: | 1520-5118 (Electronic) 0021-8561 (Linking) |
| Abstract: | "Hyphantria cunea (Drury) is a destructive invasive pest species in China that uses type II sex pheromone components. To date, however, the binding mechanisms of its sex pheromone components to their respective pheromone-binding proteins (HcunPBPs 1/2/3) have not been explored. In the current study, all three HcunPBPs were expressed in the antennae of both sexes. The prokaryotic expression and ligand binding assays were employed to study the binding of the moth's four sex pheromone components, including two aldehydes and two epoxides, and 24 plant volatiles to the HcunPBPs. Our results showed that the abilities of these HcunPBPs to bind to the aldehydes were significantly different from binding to the epoxides. These three HcunPBPs also selectively bind to some of the plant volatiles tested. Our molecular docking results indicated that some crucial hydrophobic residues might play a role in the binding of HcunPBPs to their sex pheromone components. Three HcunPBPs have different selectivities for pheromone components with both major and minor structural differences. Our study provides a fundamental insight into the olfactory mechanism of moths at the molecular level, especially for moth species that use various type II pheromone components" |
| Keywords: | Aldehydes/chemistry/metabolism Animals Carrier Proteins/chemistry/*metabolism Epoxy Compounds/chemistry/metabolism Female Insect Proteins/chemistry/*metabolism Male Molecular Docking Simulation Moths/chemistry/metabolism Protein Binding Sex Attractants/ch; |
| Notes: | "MedlineZhang, Xiao-Qing Mang, Ding-Ze Liao, Hui Ye, Jia Qian, Jia-Li Dong, Shuang-Lin Zhang, Ya-Nan He, Peng Zhang, Qing-He Purba, Endang R Zhang, Long-Wa eng 2020/12/29 J Agric Food Chem. 2021 Jan 13; 69(1):55-66. doi: 10.1021/acs.jafc.0c04476. Epub 2020 Dec 27" |
