Carbamate and organophosphate resistance in Culex pipiens L. (Diptera: Culicidae) in southern France and the significance of Est-3A

Abstract

Three French strains of Culex pipiens L. were compared at the fourth larval instar for tolerance to organophosphate and carbamate insecticides, with and without the addition of synergists (the oxidase inhibitors piperonyl butoxide and CGA 84708) (a propynyl compound) and the carboxylesterase inhibitors triphenyl phosphate (TPP) and S,S,S-tributyl phosphorotrithioate (TBPT). The S54 strain was resistant to all the organophosphates tested (chlorpyrifos, malathion, monocrotophos and profenofos) compared to the susceptible LA VIS strain but only slightly tolerant to the two carbamates (carbaryl and naphthyl phenylcarbamate). The MAURIN strain was resistant to all the insecticides, including the carbamates, at a higher level. The action of chlorpyrifos and malathion on S54 was very strongly synergised by TBPT, less strongly by TPP and not at all by piperonyl butoxide. In fact, resistance was enhanced by piperonyl butoxide, as was resistance to monocrotophos and profenofos by CGA 84708. No synergist had much effect on the MAURIN strain, although TPP slightly increased the toxicity of malathion, and piperonyl butoxide and CGA 84708 slightly increased the toxicity of carbaryl. The toxic effect of carbaryl was also increased by the addition of extra acetone. Electrophoretic studies showed that the carboxylesterase enzyme coded by gene Est-2^0.64 (which is in linkage disequilibrium withEst-3^A and acts as a marker for it) was absent from LA VIS but present in the resistant strains; but, whereas S54 was monomorphic for the gene, MAURIN was polymorphic (frequency 0·5). It is concluded that organophosphate resistance in S54 was due to detoxification by carboxylesterase wherease organophosphate and carbamate resistance in MAURIN had a strong non-metabolic component, possibly an insensitive acetylcholinesterase.