| Title: | "Expression, affinity, and binding mode analysis of antennal-binding protein X in the variegated cutworm Peridroma saucia (Hubner)" |
| Author(s): | Dong JF; Sun YL; Wang K; Guo H; Wang SL; |
| Address: | "College of Horticulture and Plant Protection, Henan University of Science and Technology, Luoyang 471000, China. Department of Plant Protection, Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences, Beijing 100081, China. College of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding 071002, China. Electronic address: guohaoinsect@126.com. Department of Plant Protection, Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences, Beijing 100081, China. Electronic address: wangshaoli@caas.cn" |
| DOI: | 10.1016/j.ijbiomac.2023.124671 |
| ISSN/ISBN: | 1879-0003 (Electronic) 0141-8130 (Linking) |
| Abstract: | "The variegated cutworm Peridroma saucia (Hubner) is a worldwide pest that causes serious damage to many crops. Odorant-binding proteins (OBPs) are small soluble proteins involved in the first step of odorant reception. In moths, antennal-binding protein Xs (ABPXs) represent a main subfamily of classic OBPs. However, their functions remain unclear. Here, we cloned the ABPX gene from the antennae of P. saucia. RT-qPCR and western-blot analyses showed that PsauABPX is antenna-predominant and male-biased. Further temporal expression investigation indicated that the expression of PsauABPX started 1 day before eclosion and reached the highest 3 days after eclosion. Next, fluorescence binding assays revealed that recombinant PsauABPX had high binding affinities with P. saucia female sex pheromone components Z11-16: Ac and Z9-14: Ac. Then, molecular docking, molecular dynamics simulation, and site-directed mutagenesis were employed to identify key amino acid residues involved in the binding of PsauABPX to Z11-16: Ac and Z9-14: Ac. The results demonstrated that Val-32, Gln-107 and Tyr-114 are essential for the binding to both sex pheromones. This study not only give us insight into the function and binding mechanism of ABPXs in moths, but could also be used to explore novel strategies to control P. saucia" |
| Keywords: | "Female Male Animals Amino Acid Sequence Molecular Docking Simulation *Moths/genetics Carrier Proteins/chemistry Insect Proteins/metabolism *Receptors, Odorant/chemistry Antennal binding protein X Binding properties Peridroma saucia;" |
| Notes: | "MedlineDong, Jun-Feng Sun, Ya-Lan Wang, Ke Guo, Hao Wang, Shao-Li eng Netherlands 2023/05/04 Int J Biol Macromol. 2023 Jul 1; 242(Pt 1):124671. doi: 10.1016/j.ijbiomac.2023.124671. Epub 2023 May 1" |
