BACKGROUND: Pheromone-binding proteins (PBPs) are responsible for transporting sex pheromones and general odorantbinding proteins (GOBPs) have been proposed to transport host-plant volatiles. A large number of OBPs have been identified from Lepidoptera species. However, olfactory molecular biology and physiology studies on PBP and GOBP in sugarcane pests are limited. Chilo infuscatellus is one of the most widely distributed pests in sugarcane-producing areas. RESULTS: Three PBPs (CinfPBP1, CinfPBP2 and CinfPBP3) and two GOBPs (CinfGOBP1 and CinfGOBP2) were identified, and five olfactory gene transcripts were abundantly expressed in antennae of C. infuscatellus. Binding assays showed that CinfPBP1-3 exhibited strong binding affinity for the sex pheromone components Z11-16:OH and 16:OH of C. infuscatellus. Meanwhile, Cinf-GOBP1-2 had high binding affinity with host-plant volatiles from sugarcane (Saccharum officinarum). Field-trapping results suggested that four volatile components, octadecane, (Z)-3-hexen-1-ol, ⊍-terpineol and hexadecane from host plants and sex pheromone mixed baits have synergistic roles in attracting C. infuscatellus adult moths. CONCLUSION: Functional characterization of CinfPBPs and CinfGOBPs in C. infuscatellus could help us find new environmentally friendly alternatives to conventional pest control using pesticides in sugarcane fields.

Insect olfaction system plays a key role in the foraging food, pollination, mating, oviposition, reproduction and other insect physiological behavior. Odorant binding protein are widely found in the various olfactory sensilla of different insect antennae and involved in chemical signals discrimination from natural environment. In this study, a novel OBP gene, MvitOBP3 is identified from the legume pod borer, Maruca vitrata, which it mainly harms important legume vegetables including cowpea, soybean and lablab bean. Real-time PCR results demonstrated that MvitOBP3 gene was abundantly expressed in the antennal tissue of M. vitrata, while low levels were distributed in the head, thorax, abdomen, leg and wing of adult moths. The recombinant OBP3 protein was purified using the prokaryotic expression and affinity chromatography system. Fluorescence competitive binding experiments indicated that that MvitOBP3 protein exhibited greater binding affinities with host-plant flower volatiles including Butanoic acid butyl ester, Limonene, 1H-indol-4-ol and 2-methyl-3-phenylpropanal, highlighting they may have attractant activities for the oviposition of female moths on the legume vegetables. Moreover, protein homology modeling and molecular docking analysis revealed that there are six amino acid sites of MvitOBP3 involved in the binding of the host-plant volatiles. These findings will further promote to understand the key role of odorant binding protein during host perception and oviposition of M. vitrata moths, which improve the efficiency of semiochemical-based prevention and monitoring for this pest in the legume vegetables field.

Insect olfaction system plays a key role in the foraging food, pollination, mating, oviposition, reproduction and other insect physiological behavior. Odorant binding protein are widely found in the various olfactory sensilla of different insect antennae and involved in chemical signals discrimination from natural environment. In this study, a novel OBP gene, MvitOBP3 is identified from the legume pod borer, Maruca vitrata, which it mainly harms important legume vegetables including cowpea, soybean and lablab bean. Real-time PCR results demonstrated that MvitOBP3 gene was abundantly expressed in the antennal tissue of M. vitrata, while low levels were distributed in the head, thorax, abdomen, leg and wing of adult moths. The recombinant OBP3 protein was purified using the prokaryotic expression and affinity chromatography system. Fluorescence competitive binding experiments indicated that that MvitOBP3 protein exhibited greater binding affinities with host-plant flower volatiles including Butanoic acid butyl ester, Limonene, 1H-indol-4-ol and 2-methyl-3-phenylpropanal, highlighting they may have attractant activities for the oviposition of female moths on the legume vegetables. Moreover, protein homology modeling and molecular docking analysis revealed that there are six amino acid sites of MvitOBP3 involved in the binding of the host-plant volatiles. These findings will further promote to understand the key role of odorant binding protein during host perception and oviposition of M. vitrata moths, which improve the efficiency of semiochemical-based prevention and monitoring for this pest in the legume vegetables field.