Degradation of sex pheromone and plant volatile components by an antennal glutathione S-transferase in the oriental fruit moth,Grapholita molesta Busck (Lepidoptera: Tortricidae).

Abstract

Insect antennae have a primary function of perceiving and discerning odorant molecules including sex pheromones and host plant volatiles. The assumption that genes highly expressed in the antennae may have an olfactory-related role associated with signal transduction. Here, one delta subfamily glutathione S-transferase (GST) gene (GmolGSTD1) was obtained from an antennal transcriptome of Grapholita molesta. Quantitative real-time polymerase chain reaction results revealed that GmolGSTD1 was mainly expressed in antennae and the expression levels were significantly higher in female antennae than in male antennae. The recombinant GmolGSTD1 (rGmolGSTD1) showed glutathione-conjugating activity toward 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. The pH range for optimal rGmolGSTD1 enzyme activity was 6.0-6.5, and rGmolGSTD1 enzyme activity had maximal peaks at 35-40°C. Spectrophotometric analysis indicated that insecticides had weak inhibitory effects on the activity of rGmolGSTD1 with the inhibitory rates of 28.82% for chlorpyrifos, 22.27% for lambda-cyhalothrin, 18.07% for bifenthrin, 20.42% for acetamiprid, 17.57% for thiamethoxam, 25.67% for metaflumizone, 27.43% for abamectin, and 7.24% for chlorbenzuron. rGmolGSTD1 exhibited high degradation activity to the sex pheromone component (Z)-8-dodecenyl alcohol and the host plant volatile butyl hexanoate with the degradation efficiency of 75.01% and 48.54%, respectively. We speculate that GmolGSTD1 works in inactivating odorant molecules and maintaining sensitivity to olfactory communication of G. molesta.