Abstract
Insects recognize odorous compounds using sensory neurons organized in olfactory sensilla. The process odor detection in insects requires an ensemble of proteins, including odorant binding proteins, olfactory receptors, and odor degrading enzymes; each of them are encoded by multigene families. Most functional proteins seem to be broadly tuned, responding to multiple chemical compounds with different, but mostly quite similar structures. Based on the hypothesis that insects recognize host volatiles by means of general odorant binding proteins (GOBPs), the current study aimed to characterize GOBPs of the yellow peach moth, Conogethes punctiferalis (Guenée). In oviposition preference tests, it was found that the yellow peach moth preferred volatiles from Prunus persica (peach) in finding their host plant. Exposure of the moth to volatiles from peaches affected the expression level of GOBP genes. Binding affinity of GOBPs from yellow peach moth was assessed for 16 host plant volatiles and 2 sex pheromones. The fluorescence ligand-binding assays revealed highest affinities for hexadecanal, farnesol, and limonene with K(D) values of 0.55 ± 0.08, 0.35 ± 0.04, and 1.54 ± 0.39, respectively. The binding sites of GOBPs from yellow peach moth were predicted using homology modeling and characterized using molecular docking approaches. The results indicated the best binding affinity of both GOBP1 and GOBP2 for farnesol, with scores of -7.4 and -8.5 kcal/mol. Thus, GOBPs may play an important role in the process of finding host plants.