A review on the structure and mechanism of cytosolic Glutathione S transferases in mosquitoes

Abstract

Glutathione S transferases are functionally diverse enzymes that have a consensus structure. These enzymes play a vital role in detoxification, protecting cells from oxidative cells and insecticide resistance in mosquitoes. This review includes the structure and function of various GSTs isolated from Anopheles gambiae and Aedes aegypti. The mosquito GSTs have a canonical fold that is made of a thioredoxin-like N-terminal domain and an alpha helical C-terminal domain. The enzyme has a conserved glutathione binding domain and a relatively variable substrate binding site that is hydrophobic in nature. Differences within the enzymes reveal adaptation to various ecological and chemical pressures. In addition to their role in developing insecticide resistance- the enzymes can also be used in biosensing. This review highlights the importance of mosquito GSTs both as a tool and target for insect physiology, chemical ecology and public health.