Structural Basis and Recognition Mechanism of Host-Derived Volatiles by Olfactory Proteins in the Agricultural Pest <i>Bactrocera correcta</i> (Diptera: Tephritidae)

Host-derived volatiles play a critical role in mediating plant-insect interactions. <i>Bactrocera correcta</i> is a destructive pest of fruit crops. In this study, we investigated the recognition mechanisms of three key volatiles─β-caryophyllene, ethyl decanoate, and hexyl hexanoate─derived from the host fruits of <i>B. correcta</i>. Using transcriptomic analysis, fluorescence binding assays, molecular docking, and molecular dynamics simulations, we identified BcorOBP19d-2 as a key odorant-binding protein that binds multiple volatiles and facilitates their stabilization and transport. Odorant receptors (BcorOR7a-13, BcorOR74a-3, and BcorOR7a-3) selectively recognize these volatiles, with hydrophobic interactions as the primary driving force for binding. β-Caryophyllene exhibited the highest binding specificity with BcorOR7a-13, ethyl decanoate demonstrated the strongest binding affinity with BcorOR74a-3, and hexyl hexanoate showed moderate stability with BcorOR7a-3. These findings provide structural insights into volatile recognition in polyphagous insects and offer a basis for developing attractants or repellents for pest management.