An omega‐class glutathione S‐transferase in the brown planthopper Nilaparvata lugens exhibits glutathione transferase and dehydroascorbate reductase activities

Abstract

A complementary DNA that encodes an omega-class glutathione S-transferase (GST) of the brown planthopper, Nilaparvata lugens (nlGSTO), was isolated by reverse transcriptase polymerase chain reaction. A recombinant protein (nlGSTO) was obtained via overexpression in the Escherichia coli cells and purified. nlGSTO catalyzes the biotransformation of glutathione with 1-chloro-2,4-dinitrobenzene, a general substrate for GST, as well as with dehydroascorbate to synthesize ascorbate. Mutation experiments revealed that putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, were important for glutathione transferase and dehydroascorbate reductase activities. As ascorbate is a reducing agent, nlGSTO may participate in antioxidant resistance.

The diverse functions of Mu-class Glutathione S-transferase HrGSTm1 during the development of Hyalomma rufipes with a focus on the detoxification metabolism of cyhalothrin

“…Previous studies have found that drug stress can induce or inhibit the expression of GSTs [ 24 ]. For example, the expression of Nilaparvata lugens NLGSTE decreased by 36% after exposure to 0.1 mM aldicarb [ 34 ]; the expression of SLGSTe2 and SLGSTe3 of Spodoptera litura was slightly upregulated after exposure to carbaryl, DDT and deltamethrin, but neither of these could be induced after exposure to malathion [ 35 ]; and the expression of Dugesia japonica GSTs was significantly inhibited after exposure to high concentration of glyphosate for 5 days [ 36 ]. In the present study, the expression of HrGSTm1 in the Malpighian tubules was higher than that in the midgut.…”