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The oriental fruit fly, Bactrocera dorsalis, is a damaging insect pest for many vegetable and fruit crops that has evolved severe chemical insecticide resistance, including organophosphorus, neonicotinoid, pyrethroid, and macrolides. Hence, it is important to elucidate its detoxification mechanism to improve its management and mitigate resource destruction. Glutathione S-transferase (GST) is a critical secondary phase enzyme that plays multiple detoxification functions against xenobiotics. In this study, we identified several BdGSTs by characterizing their potential relationships with five insecticides using inducible and tissue-specific expression pattern analyses. We found that an antenna-abundant BdGSTd8responded to four different classes of insecticides. Subsequently, our immunohistochemical and immunogold staining analysis further confirmed that BdGSTd8 was primarily located in the antenna. Our investigations also confirmed that BdGSTd8 possesses the capability to enhance cell viability by directly interacting with malathion and chlorpyrifos, which clarified the function of antenna-abundant GST in B. dorsalis. Altogether, these findings enrich our understanding of GST molecular characteristics in B. dorsalisand provide new insights into the detoxification of superfluous xenobiotics in the insect antenna.

Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that mediate the fast action of acetylcholine in synaptic cholinergic transmissions. Insect nAChRs are the target of several classes of insecticides. Here, the full-length cDNA encoding a nAChR beta1 subunit (Bdorβ1) was identified and characterized from a destructive pest, Bactrocera dorsalis. The amino acid sequence of Bdorβ1 shows high identities to other insect nAChRs β1 subunits. Double injection of dsBdorβ1reduced the expression of Bdorβ1and in turn significantly decreased susceptibility to oxa-bridged trans- instead of cis-nitromethylene neonicotinoids. Our results support the involvement of Bdorβ1in the susceptibility of B. dorsalisto oxa-bridged trans- instead of cis-nitromethylene neonicotinoids and imply that these two classes of neonicotinoids might be acting at different nAChR subtypes.