The insect olfactory system serves as a critical detection mechanism, where odorant-binding proteins (OBPs) mediate recognition by binding odor molecules, thereby regulating behavioral responses. Here, we functionally characterized three male antennal-enriched OBPs (BodoOBP2, BodoOBP4, and BodoOBP8) from Bradysia odoriphaga. Fluorescence binding assays showed that these OBPs had significantly higher affinity for three sex pheromones than for five host plant volatiles, with BodoOBP8's affinity for linolenic acid particularly outstanding (Ki = 0.44 μΜ, pH = 5.0). Molecular docking attributed these profiles to key pocket residues. RNA interference showed that dsRNA-treated males had significantly impaired female recognition. Furthermore, host-plant attraction assays showed a reduced Chinese chive orientation in dsBodoOBP2- and dsBodoOBP4-silenced adults. Our findings suggest that BodoOBP2 and BodoOBP4 mediate both pheromone communication and host-plant detection, while BodoOBP8 mainly transports pheromones. These results advance our understanding of olfactory mechanisms in Diptera and provide molecular targets for olfactory-based management of this pest.
Jin et al. (Sat,) studied this question.
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