Binding affinity characterization of an antennae-enriched chemosensory protein from the white-backed planthopper, Sogatella furcifera (Horváth), with host plant volatiles.

The white-backed planthopper (WBPH) Sogatella furcifera is a notorious rice pest in Asia. Olfaction is crucial for the WBPH to seek and locate rice plants. However, its mechanism is still not fully understood. Chemosensory proteins (CSPs) are some of the important olfactory-related proteins. In this study, we first used a bacterial system to successfully express the recombinant, antennae-enriched protein SfurCSP5. Further, competitive fluorescence binding assays with 86 candidate ligands, including some known rice plant volatiles, showed that SfurCSP5 has high affinities for 2-tridecanone, 2-pentadecanone, and β-ionone, which are known to be present in volatile mixtures that can attract rice planthoppers, and produced Ki values of 4.89, 4.09, and 1.39 μmol/L, respectively. Additionally, homology modeling of the protein structure of SfurCSP5 showed that it possesses five α-helixes (α-1, α-2, α-3, α-4, and α-5), which is a non-typical feature of the insect CSPs. Finally, ligand docking results revealed that Leu-44, Ile-64, Phe-90, Trp-98, and Phe-101 are five hydrophobic residues that interact with all of the ligands, indicating their key involvement in the binding of SfurCSP5. Our study lays the foundation for an understanding of the olfaction mechanism of rice planthoppers.