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<b>:</b><b> </b>The whitefly,<b> </b><i>Bemisia</i><i> </i><i>tabaci</i>, is an important invasive economic pest of agricultural crops worldwide. &#946;-ionone has a significant oviposition repellent effect against <i>B.</i><i> </i><i>tabaci</i>, but the olfactory molecular mechanism of this insect for recognizing &#946;-ionone is unclear. To clarify the binding properties of odorant-binding proteins (OBPs) with &#946;-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 &#946;-ionone. The results showed that after the OBP1 and OBP4 proteins were recombined, the compound &#946;-ionone exhibited a reduction in the fluorescence binding affinity to &lt;50%, with a dissociation constant of 5.15 and 3.62 &#956;M for OBP1 and OBP4, respectively. Our data indicate that &#946;-ionone has high affinity for OBP1 and OBP4, which play a crucial role in the identification of oviposition sites in <i>B.</i><i> </i><i>tabaci</i>. The findings of this study suggest that whiteflies employ &#946;-ionone compound in the selection of the suitable egg-laying sites on host plants during the oviposition behavior.