Resistance-associated point mutations in insecticide-insensitive acetylcholinesterase

Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):5922-6. doi: 10.1073/pnas.91.13.5922.

Abstract

Extensive utilization of pesticides against insects provides us with a good model for studying the adaptation of a eukaryotic genome to a strong selective pressure. One mechanism of resistance is the alteration of acetylcholinesterase (EC 3.1.1.7), the molecular target for organophosphates and carbamates. Here, we report the sequence analysis of the Ace gene in several resistant field strains of Drosophila melanogaster. This analysis resulted in the identification of five point mutations associated with reduced sensitivities to insecticides. In some cases, several of these mutations were found to be combined in the same protein, leading to different resistance patterns. Our results suggest that recombination between resistant alleles preexisting in natural populations is a mechanism by which insects rapidly adapt to new selective pressures.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Acetylcholinesterase / genetics*
  • Acetylcholinesterase / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carbaryl / pharmacology
  • Cloning, Molecular
  • Drosophila melanogaster / drug effects
  • Drosophila melanogaster / enzymology
  • Drosophila melanogaster / genetics*
  • Female
  • Insecticide Resistance / genetics*
  • Insecticides / pharmacology
  • Insecticides / toxicity*
  • Kinetics
  • Malathion / analogs & derivatives
  • Malathion / pharmacology
  • Models, Molecular
  • Oocytes / physiology
  • Paraoxon / pharmacology*
  • Point Mutation*
  • Propoxur / pharmacology
  • Protein Structure, Secondary*
  • Torpedo
  • Xenopus

Substances

  • Insecticides
  • malaoxon
  • Propoxur
  • Acetylcholinesterase
  • Paraoxon
  • Carbaryl
  • Malathion