ArticleProceedings of the National Academy of Sciences of the United States of America1997
A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 382 citations in OpenAlex.
- Structural and evolutionary constraints of organophosphate resistance in dipteran carboxylesterases.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Single Amino Acid Polymorphisms in thePathogens (Basel, Switzerland) · 2023Article
- Review
- Ultrahigh-Throughput Directed Evolution of a Metal-Free α/β-Hydrolase with a Cys-His-Asp Triad into an Efficient Phosphotriesterase.Journal of the American Chemical Society · 2023Article
- Immunoglobulin heavy constant gamma gene evolution is modulated by both the divergent and birth-and-death evolutionary models.Primates; journal of primatology · 2022Article
- Pathogenicity ofInsects · 2022Article
- Genomic analysis of the carboxylesterase family in the salmon louse (Lepeophtheirus salmonis).Comparative biochemistry and physiology. Toxicology & pharmacology : CBP · 2021Article
- Resistance in the GenusInsects · 2021Review
- High-resolution genetic mapping reveals cis-regulatory and copy number variation in loci associated with cytochrome P450-mediated detoxification in a generalist arthropod pest.PLoS genetics · 2021Article
- Peroxiredoxin alleviates the fitness costs of imidacloprid resistance in an insect pest of rice.PLoS biology · 2021Article
- Aedes aegypti miRNA-33 modulates permethrin induced toxicity by regulating VGSC transcripts.Scientific reports · 2021Article
- Molecular basis of resistance to organophosphate insecticides in the New World screw-worm fly.Parasites & vectors · 2020Article
- Article
- Overcoming insecticide resistance through computational inhibitor design.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Exome-wide association of deltamethrin resistance in Aedes aegypti from Mexico.Insect molecular biology · 2019Article
- Article
- Signatures of Insecticide Selection in the Genome ofG3 (Bethesda, Md.) · 2018Article
- Predicting Evolution of the Transcription Regulatory Network in a Bacteriophage.Genome biology and evolution · 2018Article
- Association of detoxification enzymes with butene-fipronil in larvae and adults of Drosophila melanogaster.Environmental science and pollution research international · 2018Article
- Differential gene expression in the evolution of sex pheromone communication in New Zealand's endemic leafroller moths of the genera Ctenopseustis and Planotortrix.BMC genomics · 2018Article
15 more citing papers are in PubMed but not listed here.
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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance to organophosphorus (OP) insecticides is associated with decreased carboxylesterase activity in several insect species. It has been proposed that the resistance may be the result of a mutation in a carboxylesterase that simultaneously reduces its carboxylesterase activity and confers an OP hydrolase activity (the "mutant ali-esterase hypothesis"). In the sheep blowfly, Lucilia cuprina, the association is due to a change in a specific esterase isozyme, E3, which, in resistant flies, has a null phenotype on gels stained using standard carboxylesterase substrates. Here we show that an OP-resistant allele of the gene that encodes E3 differs at five amino acid replacement sites from a previously described OP-susceptible allele. Knowledge of the structure of a related enzyme (acetylcholinesterase) suggests that one of these substitutions (Gly137 --> Asp) lies within the active site of the enzyme. The occurrence of this substitution is completely correlated with resistance across 15 isogenic strains. In vitro expression of two natural and two synthetic chimeric alleles shows that the Asp137 substitution alone is responsible for both the loss of E3's carboxylesterase activity and the acquisition of a novel OP hydrolase activity. Modeling of Asp137 in the homologous position in acetylcholinesterase suggests that Asp137 may act as a base to orientate a water molecule in the appropriate position for hydrolysis of the phosphorylated enzyme intermediate.
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