4.7 Article

Functional disparity of four pheromone-binding proteins from the plum fruit moth Grapholita funebrana Treitscheke in detection of sex pheromone components

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 225, Issue -, Pages 1267-1279

Publisher

ELSEVIER
DOI: 10.1016/j.ijbiomac.2022.11.186

Keywords

Grapholita funebrana; Chemoreception; Pheromone binding proteins; Fluorescence binding assay; Tissue expression; Molecular docking

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This study identified four pheromone-binding proteins (PBPs) in Grapholita funebrana, determined their preferred ligands, and investigated the molecular forces maintaining the PBP-pheromone complexes. The results showed high expression of these PBPs in the antennae, with different preferences for different pheromones. Hydrophobic forces, including van der Waals forces and hydrogen bonds, were found to play a crucial role in maintaining the PBP-pheromone complexes. This study enhances our understanding of the sex pheromone recognition mechanisms in G. funebrana and will facilitate the development of novel control strategies.
Grapholita funebrana, also known as the plum fruit moth, is an oligophagous pest species that causes enormous economic losses of the fruits of Rosaceae. An eco-friendly method for the control of G. funebrana besides chemical control has not yet been developed. The sex pheromone communication system plays an important role in moth courtship and mating, in which pheromone-binding proteins (PBPs) are critical. In this research, we identified four PBPs, namely, GfunPBP1.1, GfunPBP1.2, GfunPBP2, and GfunPBP3, from the antennae of G. funebrana. The results of real-time quantitative PCR (RT-qPCR) showed that all four GfunPBPs were overwhelmingly expressed in the antennae and that GfunPBP1.2 and GfunPBP2 showed male-biased expression patterns, whereas GfunPBP1.1 and GfunPBP3 were equally expressed between sexes. The results of ligand-binding assays illustrated that although all four recombinant GfunPBPs (rGfunPBPs) had binding activity with the tested sex pheromone compounds, their preferred ligands were significantly different. rGfunPBP2 had the strongest binding affinity to Z8-12:Ac and Z8-12:OH; rGfunPBP1.1 preferred to bind Z8-14:Ac, Z10-14:Ac, and 12:OH more than to the other three GfunPBPs; and rGfunPBP1.2 exhibited stronger binding affinity to E8-12:Ac than to the other rGfunPBPs. Molecular docking results demonstrated that hydrophobic forces, especially van der Waals forces and hydrogen bonds, were the most important forces that maintained GfunPBP-pheromone ligand complexes. This study will improve our understanding of the sex pheromone recognition mechanisms of G. funebrana and pro-mote the development of novel strategies for controlling G. funebrana.

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