Evaluation of mechanisms of azinphos-methyl resistance in the codling moth Cydia pomonella (L.)

Archives of Insect Biochemistry and Physiology
Haim Reuveny, Ephraim Cohen

Abstract

Resistance of the codling moth Cydia pomonella (L.) to azinphos-methyl is not based on enhanced detoxifying enzymes like oxidation mediated by mixed function oxidases or by glutathione S-transferases. Synergism by S,S,S-tributylphosphoro-trithioate was evident, but the overall activity of general esterases using p-nitrophenyl acetate as the substrate was similar in resistant and susceptible insects. In comparison to acetylcholinesterase (AChE) from susceptible adult codling moth, the enzyme of insects resistant to azinphos-methyl has low affinities (higher K(m) values) to the substrates acetylthiocholine (ATCh) and propionylthiocholine. This difference indicates a possible amino acid alteration at the catalytic or anionic binding sites of the resistant enzyme. Inhibition studies revealed no apparent differences in sensitivity of AChE enzymes from resistant and susceptible moths to organophosphorus compounds (OPs), carbamate insecticides and quaternary ammonium ligands. MEPQ (7-Methylethoxyphosphinyloxy)-1-methylquinolinium) is the most powerful OP inhibitor acting at a nM range, while chlopyrifos oxon, azinphos-methyl oxon and paraoxon are less inhibitory by 22.9, 82.3 and 475 fold, respectively. The codling moth AChE is a typi...Continue Reading

References

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Citations

Apr 19, 2008·Pest Management Science·Maritza Reyes, Benoît Sauphanor
Jun 29, 2012·Environmental Toxicology and Chemistry·Timothy A Bargar
Oct 16, 2015·Journal of Economic Entomology·Maritza ReyesEduardo Fuentes-Contreras
Jun 21, 2019·Bulletin of Entomological Research·M A Navarro-RoldánM Siegwart
Aug 28, 2021·Pesticide Biochemistry and Physiology·Di JuXue-Qing Yang

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