Insect glutathione transferases and insecticide resistance

Authors


Dr Hilary Ranson, Vector Research Group, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK. Tel.: +44 (0)151 7053310; fax: +44 (0)151 3053369; e-mail: hranson@liv.ac.uk

Abstract

Glutathione transferases (GSTs) are a diverse family of enzymes found ubiquitously in aerobic organisms. They play a central role in the detoxification of both endogenous and xenobiotic compounds and are also involved in intracellular transport, biosynthesis of hormones and protection against oxidative stress. Interest in insect GSTs has primarily focused on their role in insecticide resistance. GSTs can metabolize insecticides by facilitating their reductive dehydrochlorination or by conjugation reactions with reduced glutathione, to produce water-soluble metabolites that are more readily excreted. In addition, they contribute to the removal of toxic oxygen free radical species produced through the action of pesticides. Annotation of the Anopheles gambiae and Drosophila melanogaster genomes has revealed the full extent of this enzyme family in insects. This mini review describes the insect GST enzyme family, focusing specifically on their role in conferring insecticide resistance.

Ancillary