Host: The Japanese Society of Toxicology
Glutathione transferases (GSTs) for insects can influence their sensitivity in insecticides, and as the Lepidoptera comprises major agricultural pests, it is important to study lepidopteran GSTs. We report herein the characterization of a novel GST (GSTU2) in the silkworm, Bombyx mori.
A GSTU2 mRNA was induced in a silkworm strain exhibiting diazinon resistance. The diazinon and GSH conjugation caused by GSTU2 were involved in a substitution of the phosphothioester moiety of diazinon by glutathione. Since this moiety of diazinon is important part for binding to AChE, GSTU2 could play a crucial role in detoxification of diazinon.
