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Odorant binding proteins play a crucial role in transporting semiochemicals across the sensillum lymph to olfactory receptors within the insect antennal sensilla. In this study, the general odorant binding protein 2 gene was cloned from the antennae of  Loxostege sticticalis , using reverse transcription PCR and rapid amplification of cDNA ends. Recombinant  Lsti GOBP2 was expressed in  Escherichia coli  and purified by Ni ion affinity chromatography. Real-time PCR assays indicated that  Lsti GOBP2 mRNA is expressed mainly in adult antennae, with expression levels differing with developmental age. Ligand-binding experiments using N-phenyl-naphthylamine (1-NPN) as a fluorescent probe demonstrated that the  Lsti GOBP2 protein has binding affinity to a broad range of odorants. Most importantly,  trans -11-tetradecen-1-yl acetate, the pheromone component of  Loxostege sticticalis , and  trans -2-hexenal and  cis -3-hexen-1-ol, the most abundant plant volatiles in essential oils extracted from host plants, had high binding affinities to  Lsti GOBP2 and elicited strong electrophysiological responses from the antennae of adults.

Functional Analysis of General Odorant Binding Protein 2 from the Meadow Moth, Loxostege sticticalis L. (Lepidoptera: Pyralidae)