Involvement of Chemosensory Protein BodoCSP1 in Perception of Host Plant Volatiles in Bradysia odoriphaga

Chemosensory proteins (CSPs) can bind and transport odorant molecules and play important roles in insect chemoreception. In this study, we focused on the roles of a chemosensory protein (BodoCSP1) in perception of host plant volatiles in Bradysia odoriphaga. The expression of BodoCSP1 was significantly higher in adults than in larvae and pupae, without a significant difference between male and female adults. Recombinant protein BodoCSP1 exhibited relatively high binding affinities to 9 out of 10 tested ligands (K-i < 10 mu M). Behavioral assays revealed that adults of B. odoriphaga showed a significant preference for five compounds. The predicted three-dimensional (3D) structure of BodoCSP1 has the typical six alpha-helices that form the hydrophobic ligand-binding pocket. Molecular docking and site-directed mutagenesis combined with ligand-binding assays indicated that Val48 and Thr66 may be the key binding site in BodoCSP1 for host plant volatiles. RNAi results indicated that dsBodoCSP1-treated adults showed significant reductions in response to diallyl disulfide, dipropyl disulfide, and allyl methyl disulfide. These results indicated that BodoCSP1 plays essential functions in the perception of host plant volatiles in B. odoriphaga.

Automated summary

Chemosensory protein BodoCSP1 plays essential roles in host plant volatile perception in Bradysia odoriphaga, with higher expression in adults. The predicted three-dimensional structure of BodoCSP1 features six alpha-helices forming a hydrophobic ligand-binding pocket.