Purification and characterization of a carboxylesterase involved in malathion-specific resistance from Tribolium castaneum (Coleoptera: Tenebrionidae).

Specific resistance to malathion in a strain of Tribolium castaneum is due to a 44-fold increase in malathion carboxylesterase (MCE) activity relative to a susceptible strain, whereas non-specific esterase levels are slightly lower. Unlike the overproduced esterase of some mosquito and aphid species, MCE in Tribolium castaneum accounts for only a small fraction (0.033-0.045%) of the total extractable protein respectively in resistant and susceptible strains. The enzyme was purified to apparent homogeneity from these two strains and has a similar molecular weight of 62,000. However, preparative isoelectricfocusing indicated that resistant insects possess one MCE with pI of 7.3, while susceptible insects possess a MCE with a pI of 6.6. Purified MCE from both populations had different K(m) and V(m) values for hydrolysis of malathion as well as for alpha-naphthyl acetate. The kinetic analysis suggests that MCE of resistant insects hydrolyses malathion faster than the purified carboxylesterase from susceptible beetles and that this enzyme has greater affinity for malathion than for naphthyl esters. Malathion-specific resistance is due to the presence of a qualitatively different esterase in the resistant strain.

Larvicidal properties of decomposed leaf litter in the subalpine mosquito breeding sites.

The larvicidal properties of the dietary leaf litter originating from the vegetation surrounding the subalpine mosquito breeding sites were investigated by using 10-month decomposed alder leaf litter against different field collections of culicine taxa of various ecological origin (Aedes cantans, Aedes caspius, Aedes cataphylla, Aedes detritus, Aedes punctor, Aedes pullatus, Aedes rusticus, Anopheles claviger, Culex hortensis, Culex pipiens, Culiseta morsitans). Larvae originating from sites with polyphenol-poor vegetation appeared more sensitive to ingested leaf litter than those originating from sites with polyphenol-rich vegetation. Within a given taxon (e.g., A. rusticus, A. cataphylla, C. hortensis), the overall levels of cytochrome P450 monooxygenase and esterase activities appeared higher in larvae able to feed on leaf litter than in pupae and adults unable to feed on leaf litter. This suggests the involvement of these enzymes in the detoxification mechanisms responsible for larval tolerance to polyphenols of the dietary leaf litter. Such a tolerance of the larval stage thus appears as fundamental in the ecotoxicological adaptation of mosquito taxa to the polyphenolic profiles of the riparian vegetation.