Molecular and Functional Characterization of pheromone binding protein 1 from the Oriental Fruit Moth, Grapholita molesta (Busck)

Abstract

Pheromone binding protein (PBP) is thought primarily to bind and transport the sex pheromone in moths. The accumulated studies suggest that three PBPs were identified in moth species. In Grapholita molesta, the functions of GmolPBP2 and GmolPBP3 have been previously studied. However, the function of GmolPBP1 is still unclear. Furthermore, the Cydia pomonella sex pheromone Codlemone can act as a sex pheromone synergist of G. molesta. In C. pomonella, CpomPBP1 specifically bind the Codlemone. CpomPBP1 displays high identity with GmolPBP1 (70%), indicating that the two PBPs may share a similar 3D structure thus can bind the similar or same ligands. In this study, we explored the molecular and functional characterization of GmolPBP1. GmolPBP1, bearing the typical characteristics of Lepidopteran odorant binding proteins, was closest phylogenetically to CpomPBP1. Binding studies demonstrated that GmolPBP1 exhibited strong binding affinities with (Z)-8-dodecenyl alcohol, 1-dodecanol and Codlemone. Molecular docking showed that GmolPBP1 has different ligand recognition mechanism for the three ligands. Our results suggest that GmolPBP1 functions as recognizer of (Z)-8-dodecenyl alcohol and 1-dodecanol of the female sex pheromone blend, and may be the potential transporter of Codlemone, which contributes to the synergism of the pheromone response of G. molesta by Codlemone.

Structural insights into the discrepant synergistic activity of Codlemone and (Z)‐8‐dodecenol towards Grapholita molesta pheromones

“…Just like 1-dodecanol, a minor pheromone component released by female OFM, 31 it was assumed to be sensed by C. pomonella pheromone binding protein 2 (CpomPBP2) to enhance the attractivity of Codlemone to C. pomonella. 32,33 As a prominent transporter of OFM sex pheromones, 34,35 GmolPBP2 was speculated as the olfactory protein that can sense Cod and Dod in the antennal sensilla of OFM due to its high affinity to the two synergists. 22,34 The information altogether makes GmolPBP2 be an appropriate molecular target for the binding mode analysis of Cod and Dod.…”

Degradation of sex pheromone and plant volatile components by an antennal glutathione S‐transferase in the oriental fruit moth,Grapholita molesta Busck (Lepidoptera: Tortricidae)

“…The adult insects exhibit seasonal host transfer behavior, and its sensitive olfactory system plays an important role in mating, host location and selection of oviposition sites (Rajapakse, Walter, Moore, Hull, & Cribb, ). In recent years, many studies have been conducted on the selective sensation, identification, and transportation of odor molecules in G. molesta (X. L. Chen, Su, Li, Li, & Wu, ; G. Zhang, Chen, Yu, Tian, & Wu, ). A large number of olfactory genes were identified by the sequencing of antenna transcriptome (G. Li, Du, Li, & Wu, ; G. H. Zhang, Li, Xu, Chen, & Wu, ), confirming the binding properties of various OBPs and CSPs to main host plant volatiles (G. W. Li, Zhang, Li, Wu, & Xu, ; Song, Dong, Qiao, & Wu, ).…”

Mating‐based regulation and ligand binding of an odorant‐binding protein support the inverse sexual communication of the greater wax moth, Galleria mellonella (Lepidoptera: Pyralidae)

“…In that sense, both PBPs and GOBPs are considered pheromone carriers with broad binding selectivity in some cases. For example, PBP1 and PBP2 from tortricid moths (eg Grapholita molesta and Cydia pomonella) possess high binding specificity towards alcohol-or acetate-based pheromone components with 12-14 carbon atoms (Tian et al, 2016;Zhang et al, 2018a). By contrast, the orthologous GOBP2 of the moths Loxostege sticticalis, S. litura and Ch.…”