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: The whitefly, Bemisia  tabaci , is an important invasive economic pest of agricultural crops worldwide. β-ionone has a significant oviposition repellent effect against B.  tabaci , but the olfactory molecular mechanism of this insect for recognizing β-ionone is unclear. To clarify the binding properties of odorant-binding proteins (OBPs) with β-ionone, we performed gene cloning, evolution analysis, bacterial expression, fluorescence competitive binding assay, and molecular docking to study the binding function of OBP1 and OBP4 on β-ionone. The results showed that after the OBP1 and OBP4 proteins were recombined, the compound β-ionone exhibited a reduction in the fluorescence binding affinity to &lt;50%, with a dissociation constant of 5.15 and 3.62 μM for OBP1 and OBP4, respectively. Our data indicate that β-ionone has high affinity for OBP1 and OBP4, which play a crucial role in the identification of oviposition sites in B.  tabaci . The findings of this study suggest that whiteflies employ β-ionone compound in the selection of the suitable egg-laying sites on host plants during the oviposition behavior.

Discrimination of Oviposition Deterrent Volatile β-Ionone by Odorant-Binding Proteins 1 and 4 in the Whitefly Bemisia tabaci