Functional characterization of a novel λ-cyhalothrin metabolizing glutathione S-transferase, CpGSTe3, from the codling moth Cydia pomonella

BACKGROUND Recent work has shown that two codling moth ( Cydia pomonella ) glutathione S -transferase genes (GSTs), CpGSTd1 and CpGSTd3 , can metabolize λ-cyhalothrin, one of the recommended insecticides for C. pomonella control worldwide. However, systematical characterization of delta and epsilon GSTs, especially their potential contributions in the metabolism of λ-cyhalothrin, is currently still lacking in C. pomonella . RESULTS In this study, a total of nine cDNA sequences were identified in C. pomonella , including four in the delta and five in the epsilon subclasses. RT-qPCR showed that seven GSTs were ubiquitously expressed at all developmental stages, and CpGSTe2 , CpGSTe3 , and CpGSTe4 were mainly expressed in larvae. The mRNA levels of CpGSTd2 , CpGSTd4 , and CpGSTe5 were significantly higher in male than in female adults. Tissue-specific expression analysis revealed that the CpGSTe2 , CpGSTe3 , and CpGSTe4 were highly expressed in the midgut while CpGSTd2 and CpGSTd4 were predominantly expressed in the Malpighian tubules. The transcripts of these GSTs (except CpGSTe1 ) were co-expressed following exposure to LD 10 of λ-cyhalothrin for 3 h. Recombinant CpGSTd4, CpGSTe2, and CpGSTe3 proteins expressed in Escherichia coli displayed glutathione-conjugating activity toward 1-chloro-2,4-dinitrobenzene. In addition, λ-cyhalothrin could inhibit the activity of recombinant CpGSTd4, CpGSTe2, and CpGSTe3 enzymes, but only recombinant CpGSTe3 showed λ-cyhalothrin metabolic capacity, with 21.88 ± 1.09% of parental compound being depleted within 1 h. CONCLUSION These data show that CpGSTe3 is a third GST gene, encoding an enzyme that metabolizes λ-cyhalothrin in C. pomonella . © 2019 Society of Chemical Industry