Characterization of the chemosensory protein EforCSP3 and its potential involvement in host location by Encarsia formosa

Abstract

Chemosensory proteins (CSPs) perform several functions in insects. This study performed the gene expression, ligand-binding, and molecular docking assays on the EforCSP3 identified in the parasitoid wasp Encarsia formosa, to determine whether EforCSP3 functions in olfaction, especially in host location and host preference. The results showed that EforCSP3 was highly expressed in the female head, and its relative expression was much higher in adults than in other developmental stages. The fluorescence binding assays suggested that the EforCSP3 exhibited high binding affinities to a wide range of host-related volatiles, among which dibutyl phthalate, 1-octene, β-elemene, and tridecane had the strongest binding affinity with EforCSP3, besides α-humulene and β-myrcene, and should be assessed as potential attractants. Protein structure modeling and molecular docking predicted the amino acid residues of EforCSP3 possibly involved in volatile binding. α-Humulene and β-myrcene attracted E. formosa in a previous study and exhibited strong binding affinities with EforCSP3 in the current study. In conclusion, EforCSP3 may be involved in semiochemical reception by E. formosa.

Keywords

• Encarsia formosa
• chemosensory protein
• expression profiles
• fluorescence binding assay
• molecular docking