Esterase-mediated bifenthrin resistance in a multiresistant strain of the two-spotted spider mite, Tetranychus urticae.
A field-collected multiresistant strain of Tetranychus urticae Koch exhibiting high resistance to bifenthrin was investigated in comparison with a susceptible laboratory strain. The esterase inhibitor S,S,S-tributyl-phosphorotrithioate ( DEF) was able strongly to synergise bifenthrin toxicity in the resistant strain. Optimal conditions for determining esterase activities in T. urticae were determined, and a higher esterase activity towards several artificial substrates was found in this resistant strain, which had a preference for hydrolysing 4-nitrophenyl butyrate. Bifenthrin was able to bind the active centres of T. urticae esterases in vitro, as was determined after competition experiments by a Dixon plot, revealing a higher affinity of bifenthrin in the resistant strain. Bifenthrin-hydrolysing activity in the resistant and susceptible strains was examined in vitro and quantified with gas chromatography. A 7.2-fold higher metabolising rate was found in the resistant strain. Copyright (c) 2006 Society of Chemical Industry.[1]References
- Esterase-mediated bifenthrin resistance in a multiresistant strain of the two-spotted spider mite, Tetranychus urticae. Van Leeuwen, T., Tirry, L. Pest Manag. Sci. (2007) [Pubmed]
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