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Two single mutations commonly cause qualitative change of nonspecific carboxylesterases in insects

Publication Type  Journal Article
Year of Publication  2011
Authors  Cui, F.; Lin, Z.; Wang, H.; Liu, S.; Chang, H.; Reeck, G.; Qiao, C.; Raymond, M.; Kang, L.
Journal Title  Insect Biochemistry and Molecular Biology
Volume  41
Issue  1
Pages  1-8
Abstract  

Carboxylesterases provide key mechanisms of resistance to insecticides, particularly organophosphates (OPs), in insects. One resistance mechanism is a qualitative change in the properties of a carboxylesterase. Two mutant forms, G151D and W271L, have been observed, mostly in dipteran species, to affect substrate specificity of enzymes. But whether these two single mutations can commonly change character of insect carboxylesterases is unknown. In our study carboxylesterase genes from seven insects distributed among four orders were cloned, mutated at position 151 or 271 and expressed in Escherichia coli. The kinetics of the purified recombinant proteins was examined towards an artificial carboxylester and two OP insecticides. The G/A151D and W271L mutation significantly reduced carboxylesterase activity in 87.5% and 100% cases, respectively, and at the same time conferred OP hydrolase activities in 62.5% and 87.5% cases, respectively. Thus, the change at position 271 is more effective to influence substrate specificity than that at position 151. These results may suggest that these two mutations have the potential to cause insecticide resistance broadly in insects.

Full Text  

Two single mutations commonly cause qualitative change of nonspecific carboxylesterases in insects

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