Pyrethroid Esterase(s) May Contribute to Natural Pyrethroid Tolerance of Larvae of the Common Green Lacewing 1

Abstract

Larvae of the common green lacewing, Chrysopa carnea Stephens1, have a remarkable natural tolerance to pyrethroids, providing important selectivity in integrated control programs. A portion of this tolerance is attributable to detoxification by pyrethroid esterase(s). This larval enzyme(s) has unusually high activity and a unique specificity for hydrolyzing cis -permethrin and -cypermethrin two- to three-fold faster than the corresponding trans -isomers. Deltamethrin is also hydrolyzed rapidly. Certain properties of the larval pyrethroid esterase(s) parallel the sensitivity of the larvae to pyrethroid poisoning. Larval pyrethroid esterase(s) increases in activity for hydrolyzing trans -permethrin on larval growth in agreement with the increased tolerance to trans -permethrin poisoning. The relative rates of hydrolysis of deltamethrin and the cis - and trans -isomers of permethrin and cypermethrin by the larval pyrethroid esterase(s) generally coincide with the tolerance of the larvae to these pyrethroids. Phenyl saligenin cyclic phosphonate, a potent inhibitor for larval pyrethroid esterase, synergizes trans -permethrin toxicity by 68-fold from an LD50 of 17,000 μg/g to one of 250 μg/g. Although the involvement of penetration rates, nerve sensitivity, and oxidative detoxification has not been evaluated, it is clear that pyrethroid esterase(s) is a major factor contributing to the natural pyrethroid tolerance of lacewing larvae.