GLUTATHIONE TRANSFERASE ISOZYMES INVOLVED IN INSECTICIDE RESISTANCE OF DIAMONDBACK MOTH LARVAE

In addition to the three glutathione transferase (GST) isozymes already identified in diamondback moth larvae, Phutella xylostella (L.), a fourth one, GST-4, was purified from a teflubenzuron (TFB)-resistant strain. This GST isozyme was similar to GST-3 in terms of biochemical and toxicological properties. GST-4, a homodimer with a subunit molecular mass of 26.6 kDa and a pI of ca. 8.9, displayed even stronger substrate preference than GST-3 for 1,2-dichloro-4-nitrobenzene and several organophosphorus insecticides, i.e., parathion, methyl parathion, and paraoxon. These two proteins were highly immunorelated and shared at least the first eight amino acids at the N-terminus. Immunoblotting analysis indicated that polyclonal antiserum raised against GST-3 cross-reacted with GST-1 and GST-2 at least 40-fold less intensely than with the antigen. Using this antiserum as probe, higher amounts and greater Variations of GST-3/GST-4 were observed in larvae of a methyl parathion- and a TFB-resistant strain compared with a susceptible and a fenvalerate-resistant strain. Among the six lepidopterous insects examined, only Spodoptera exigua larvae clearly had proteins immunorelated to GST-3/GST-4 of diamondback moth. No such cross-reactivity was observed in Musca domestica, Drosophila melanogaster, and Aedes aegypti. (C) 1994 Academic Press, Inc.