LAUSR

Insects are highly reliant on their active olfactory system in which odorant binding proteins play a role to selectivity and sensitivity during odour perception and processing. This study sets out to determine whether and to which extent the antennal loaded SaveOBP10 in English grain aphid Sitobion avenae, contributes in olfactory processing during host selection. To understand this possible relationship, we purified the SaveOBP10 recombinant protein and performed fluorescence ligand binding tests, molecular docking, RNA interference (RNAi) and behavioural trials. The results showed that SaveOBP10 had strong binding affinities (Ki ≤5 μM) with most of wheat plant volatiles at pH 5.0 as compared to pH 7.4. In Y‐tube olfactometer bioassays, the S. avenae was attracted behaviourally towards pentadecane, butylated hydroxytoluene, tetradecane and β‐caryophyllene however repelled by naphthalene. After RNAi of SaveOBP10, the aphid showed nonattraction towards β‐caryophyllene and nonsignificant behavioural response to pentadecane, butylated hydroxytoluene and tetradecane. Furthermore, the three‐dimensional structure modelling and molecular docking of SaveOBP10 were performed to the volatiles with high binding abilities. Together these findings indicate that SaveOBP10 can bind more strongly to the volatiles that involved in S. avenae behaviour regulation and possibly will contribute effectively in S. avenae integrated pest management.