Mutations of acetylcholinesterase1 contribute to prothiofos-resistance in Plutella xylostella (L.).

@article{Lee2007MutationsOA,
  title={Mutations of acetylcholinesterase1 contribute to prothiofos-resistance in Plutella xylostella (L.).},
  author={Dae-Weon Lee and J. Choi and W. Kim and Y. Je and J. Song and B. Chung and K. Boo and Y. Koh},
  journal={Biochemical and biophysical research communications},
  year={2007},
  volume={353 3},
  pages={
          591-7
        }
}
Insensitive acetylcholinesterase (AChE) is involved in the resistance of organophosphorous and carbamate insecticides. We cloned a novel full-length AChE cDNA encoding ace1 gene from adult heads of the diamondback moth (DBM, Plutella xylostella). The ace1 gene encoding 679 amino acids has conserved motifs including catalytic triad, choline-binding site and acyl pocket. Northern blot analysis revealed that the ace1 gene was expressed much higher than the ace2 in all examined body parts. The… Expand
Amino acid substitutions and intron polymorphism of acetylcholinesterase1 associated with mevinphos resistance in diamondback moth, Plutella xylostella (L.).
TLDR
Results imply that amino acid substitutions in AChE1 of SHMTCN strain are associated with mevinphos resistance in this insect pest, and this finding is important for insecticide resistance management of P. xylostella in the field. Expand
Characterization of acephate resistance in the diamondback moth Plutella xylostella
TLDR
expression of GST genes available in P. xylostella to date was examined using the resistant and susceptible strains, revealing no significant correlation between the expression and resistance levels, suggesting that other factors such as GSTs are involved in acephate resistance. Expand
Mutation in ace1 associated with an insecticide resistant population of Plutella xylostella
TLDR
Findings suggest that the A298S mutation, along with reported G324A mutation, can be important in the development of organophosphate resistance and could be a good candidate for a molecular diagnosis marker for resistance monitoring. Expand
Insecticide-resistance mechanism of Plutella xylostella (L.) associated with amino acid substitutions in acetylcholinesterase-1: A molecular docking and molecular dynamics investigation
TLDR
In the present study, the wild-type and mutant AChE1 structures were constructed and their structural stabilities, residual flexibilities were investigated through molecular dynamics simulations, and the structural and energetic changes responsible for the insecticide-resistance in A ChE1 were analyzed using molecular docking. Expand
Acetylcholinesterases of the cat flea Ctenocephalides felis: identification of two distinct genes and biochemical characterization of recombinant and in vivo enzyme activities.
TLDR
Comparison of substrate specificities and inhibitor sensitivities of both recombinant enzymes with those of AChE activities extracted from adult fleas suggest that CfAChE1, and not CfAchE2, is the dominant activity in C. felis imagoes. Expand
Mechanisms of resistance to malathion in the medfly Ceratitis capitata.
TLDR
The coding sequence for acetylcholinesterase (AChE) gene (Ccace) of C. capitata is obtained and it is shown that target site insensitivity is one of the factors of malathion resistance. Expand
Acetylcholinesterase Genes in the Glanville Fritillary Butterfly (Melitaea cinxia, Lepidoptera: Nymphalidae)
TLDR
Compared the amino acids at the sites where substitution may result in insecticide resistance between McACHEs and the earlier reported AChEs, it is found that no amino acid substitution related to insecticides resistance occurs in either McAChE1 or McA cholinesterase. Expand
Biochemistry and molecular characterisation of chlorpyrifos resistance in field strains of the white‐backed planthopper Sogatella furcifera (Hemiptera: Delphacidae)
TLDR
Cloned the full‐length cDNA of AChE type 1 and type 2 genes from S. furcifera and found that SfAChE1 is more highly expressed than Sf aChE2, and both genes were most highly expressed during the first instar nymph stage, and then expressed at a decreasing rate until the end of the fifth instarNymph stage. Expand
Molecular characterization and inhibition analysis of the acetylcholinesterase gene from the silkworm maggot, Exorista sorbillans.
TLDR
Insight is given of the mechanism that some OP insecticides can selectively kills Es while without distinct effect on its host, B. mori, by comparison of the I(50) values of eserine, dichlorvos, Chlorpyrifos and omethoate of recombinant Es A ChEs with its host (Bombyx mori) AChEs. Expand
Molecular and functional properties of two Spodoptera exigua acetylcholinesterase genes.
  • J. Zhao, D. Hao, +4 authors K. Wang
  • Biology, Medicine
  • Archives of insect biochemistry and physiology
  • 2019
TLDR
The biological functions of the two Ace genes (SeAce1 and SeAce2), providing novel insights into the development of strategies for controlling insect pests, are revealed. Expand
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References

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Identification and characterization of ace1-type acetylcholinesterase likely associated with organophosphate resistance in Plutella xylostella
Abstract Insensitive acetylcholinesterase (AChE) was determined to be primarily involved in a prothiofos-resistant (PR) strain of diamondback moth (DBM, Plutella xylostella L.), as judged by the AChEExpand
Molecular characterization of two acetylcholinesterase genes from the oriental tobacco budworm, Helicoverpa assulta (Guenée).
TLDR
Cloned cDNAs encoding two ace genes, designated as Ha-ACE1 and Ha-ace2 by a combined degenerate PCR and RACE strategy from adult heads of the oriental tobacco budworm, Helicoverpa assulta, demonstrated that two Ha-AChEs were expressed in vivo. Expand
Identification and characterization of mutations in housefly (Musca domestica) acetylcholinesterase involved in insecticide resistance.
TLDR
The baculovirus expression of wild-type and mutated housefly AChE proteins has confirmed that the mutations each confer relatively modest levels of insecticide insensitivity except the novel Gly-262-->Val mutation, which results in much stronger resistance (up to 100-fold) to certain compounds. Expand
Absence of protein polymorphism attributable to insecticide-insensitivity of acetylcholinesterase in the green rice leafhopper, Nephotettix cincticeps.
TLDR
The cDNA sequence of acetylcholinesterase (AChE) from the green rice leafhopper was amplified, based on conserved peptide sequences of AChEs, showing the most similarity to that of A ChE in the Colorado potato beetle. Expand
An amino acid substitution attributable to insecticide-insensitivity of acetylcholinesterase in a Japanese encephalitis vector mosquito, Culex tritaeniorhynchus.
TLDR
The F455W replacement in the Ace2 gene is solely responsible for the insecticide-insensitivity of AChE in TYM mosquitoes. Expand
Acetylcholinesterase mutation in an insecticide-resistant population of the codling moth Cydia pomonella (L.).
TLDR
Two strains of Cydia pomonella (L.) (Lepidoptera: Tortricidae) were selected in the lab by exposure to increasing concentrations of diflubenzuron (Rdfb strain) or azinphos-methyl (Raz strain) and a target site resistance mechanism was suggested by the inhibition of acetylcholinesterase (AChE) activity. Expand
Identification of mutations conferring insecticide‐insensitive AChE in the cotton‐melon aphid, Aphis gossypii Glover
TLDR
Two mutations in the ace1 gene of Aphis gossypii are associated with insensitivity of acetylcholinesterase (AChE) to carbamate and organophosphate insecticides, providing a molecular explanation of why pirimicarb has a specific aphicidal action. Expand
Mutations of acetylcholinesterase which confer insecticide resistance in Drosophila melanogaster populations
TLDR
It is confirmed here that mutations are found either isolated or in combination in the same protein and it is shown that most natural populations are heterogeneous, composed of a mixture of different alleles. Expand
Fenitroxon insensitive acetylcholinesterases of the housefly, Musca domestica associated with point mutations.
TLDR
The cDNA of AChE in the housefly, Musca domestica, was sequenced and individual flies were genotyped by this gene in an inhibition assay of A ChE activity with an organophaspate, fenitroxon, and mutations at Gly and Tyr were associated with the insensitivity. Expand
Mechanisms of monocrotophos resistance in cotton bollworm, Helicoverpa armigera (Hübner).
TLDR
After comparing analysis of the entire AChE gene sequence from 5 resistant and 6 susceptible cotton bollworm individuals, nine mutations were identified and one of them, the Ala/Thr mutation, is likely to be responsible for the A ChE insensitivity to monocrotophos. Expand
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