The Sequence Characteristics and Binding Properties of the Odorant-Binding Protein SvelOBP1 from (Coleoptera: Curculionidae) to Jujube Volatiles.

(Chevrolat) (Coleoptera: Curculionidae) has caused serious damage on jujube trees ( Mill) in northern China. Semiochemicals emerging from the host are essential in the process of insects identifying and localizing the host. The highly expressed odorant-binding protein 1 of (SvelOBP1) was assumed to play a possible role in the recognition of host volatiles. In this study, 1 was cloned based on the antennal transcriptome of . The recombinant SvelOBP1 protein was expressed in and purified by Ni-NTA resin. The predicted protein SvelOBP1 belonged to a classic OBP subfamily. The expression patterns revealed that 1 was mainly expressed in the antennae of both males and females, whereas the expression of SvelOBP1 in other body parts could be neglected. The fluorescence binding assay indicated that SvelOBP1 displayed very strong binding affinities to dibutyl benzene-1,2-dicarboxylate and ()-hex-3-en-1-ol (K = 6.66 ± 0.03 and 7.98 ± 0.06 μM). The molecular docking results showed that residues Trp114, Phe115 and Asp110 may be involved in binding to both dibutyl benzene-1,2-dicarboxylate and ()-hex-3-en-1-ol and may have a great impact on odorant recognition of . Our results provide evidence that SvelOBP1 might participate in the olfactory molecular perception of and would promote the development of pest attractants for control.