Genotyping of acetylcholinesterase in insects

Li, B.; Wang, Y.H.; Liu, H.T.; Xu, Yong; Wei, Zhenguo; Chen, Y.H.; Shen, Wei

doi:10.1016/j.pestbp.2010.04.004

Cited by 16 publications

(9 citation statements)

References 16 publications

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“…Acetylcholinesterase is the important target enzyme of organophosphate and carbamate pesticides (Bacioa et al 2008;Li et al 2010;Lai et al 2013). The variation o f ace tylcholinesterase in the enzyme system can weaken the inhibitory effect of pesticides and enhance resistance.…”

Section: Discussionmentioning

confidence: 99%

Synergistic effect of imidacloprid combined with synergistic agents (Beichuang, Jiexiaoli) onMyzus persicae(Hemiptera: Aphididae)

Chen

Zhang

et al. 2014

International Journal of Pest Management

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Myzus persicae is a well known aphid pest, which can transport plant viruses to plants of the nightshade/potato family, namely the Solanaceae, and other food crops. Our aim was to explore the effects of imidacloprid combined with synergistic agents (Beichuang and Jiexiaoli) on Myzus persicae. Different concentrations of imidacloprid combined with synergistic agents were used to treat M. persicae. Biological activity of M. persicae was analyzed under indoor conditions, and the control efficiency of the admixture was determined through field experiments. The penetration rate of the admixture on tobacco leaf and M. persicae was analyzed, and the liquid surface tension and contact angle was measured. Imidacloprid combined with Beichuang and Jiexiaoli showed significant synergistic effects with high control efficacy. Beichuang and Jiexiaoli significantly improved the penetration of imidacloprid into the cuticle of tobacco leaves and the insect body wall. The surface tension and contact angles were abated by synergists. The combination of imidacloprid with Beichuang and Jiexiaoli showed a significant synergistic effect, which can be used for decreasing the dosage of imidacloprid and improving its long-term control efficacy.

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Section: Discussionmentioning

confidence: 99%

Synergistic effect of imidacloprid combined with synergistic agents (Beichuang, Jiexiaoli) onMyzus persicae(Hemiptera: Aphididae)

Chen

Zhang

et al. 2014

International Journal of Pest Management

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“…According to Dunn (1989), this type of inhibition probably occurs because this compound irreversibly binds to the hydroxyl side chain of the serine residue, impeding the enzymatic catalysis. This class of esterase is commonly found in insects (see Krejci et al 1991, Anthony et al 1995, Hinton and Hammock 2003, Coutinho-Abreu et al 2007, Yu et al 2009, and Li et al 2010 as examples). However, in some insects, they were not detected.…”

Section: Effect Of Chemicals On the Est-4 Activitymentioning

confidence: 99%

Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution

et al. 2014

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Background: After duplication, one copy of an original gene can become redundant and decay toward a pseudogene status or functionally diverge. Here, we performed the purification and biochemical characterization of EST-4 (a late larval β-esterase) from two Drosophila repleta group species, Drosophila mulleri and Drosophila arizonae, in order to establish comparative parameters between these enzymes in these species and to contribute to better understand their evolution. Results: In D. mulleri, EST-4 had an optimal activity in temperatures ranging from 40°to 45°C and at pH 7.5, maintaining stability in alkaline pH (8.0 to 10.0). It was classified as serine esterase as its activity was inhibited by PMSF. No ion negatively modulated EST-4 activity, and iron had the most positive modulating effect. In D. arizonae, it showed similar optimum temperature (40°C), pH (8.0), and was also classified as a serine esterase, but the enzymatic stability was maintained in an acidic pH (5.5 to 6.5). Fe +2 had the opposite effect found in D. mulleri, that is, negative modulation. Al +3 almost totally inhibited the EST-4 activity, and Na + and Cu +2 had a positive modulation effect. Kinetic studies, using ρ-nitrophenyl acetate as substrate, showed that EST-4 from D. mulleri had higher affinity, while in D. arizonae, it showed higher V max and catalytic efficiency in optimal reaction conditions. Conclusions: EST-4 from D. mulleri and D. arizonae are very closely related and still maintain several similar features; however, they show some degree of differentiation. Considering that EST-4 from D. mulleri has more conspicuous gel mobility difference among all EST-4 studied so far and a lower catalytic efficiency was observed here, we proposed that after duplication, this new copy of the original gene became redundant and started to decay toward a pseudogene status in this species, which probably is not occurring in D. arizonae.

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“…() reported that Plutella xylostella three mutations in ace 1 (Ala201Ser, Gly227Ala, Ala441Gly) may account for OP resistance. The Leu452Gly mutation is uniquely present in P. xylostella , suggesting that this site is related to pesticide resistance (Li et al., ).…”

Section: Introductionmentioning

confidence: 99%

“…() reported that Bmace 1 has higher expression level than Bmace 2 and is OP inducible. To investigate the relationship between Bmace 1 mutations and pesticide resistance, we used mutations at Ala (GCG) 303 Ser (TCG), Gly (GGA) 329 Ala (GCA), and Leu (TCT) 554 Ser (TTC) based on the resistance‐related sites in P. xylostella and predicted resistance sites (Baek et al., ; Li et al., ) to begin preliminary study, the relationship between mutations and enzyme activity (Wang et al., ).…”

Section: Introductionmentioning

confidence: 99%

EXPRESSION AND EFFECTS OF MUTANT Bombyx mori ACETYLCHOLINESTRASE1 IN BmN CELLS

Wang

Xie

et al. 2016

Arch Insect Biochem Physiol

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The main mechanism of toxicity of organophosphate (OP) and carbamate (CB) insecticides is their irreversible binding and inhibition of acetylcholinestrase (AChE), encoded by ace1 (acetylcholinestrase gene 1), leading to eventual death of insects. Mutations in AChE may significantly reduce insects susceptibility to these pesticides. Bombyx mori is an important beneficial insect, and no OP- or CB-resistant strains have been generated. In this study, wild-type ace1 (wace1) and mutant ace1 (mace1) were introduced into BmN cells, confirmed by screening and identification. The expression of wace1 and mace1 in the cells was confirmed by Western blot and their expression levels were about 21-fold higher than the endogenous ace1 level. The activities of AChE in wace1 and mace1 transgenic cells were 10.6 and 20.2% higher compared to control cells, respectively. mace1 transgenic cells had higher remaining activity than wace1 transgenic cells under the treatment of physostigmine (a reversible cholinesterase inhibitor) and phoxim (an OP acaricide). The results showed that ace1 transgene can significantly improve ace1 expression, and ace1 mutation at a specific site can reduce the sensitivity to AChE inhibitors. Our study provides a new direction for the exploration of the relationship between AChE mutations and drug resistance.

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Genotyping of acetylcholinesterase in insects

Cited by 16 publications

References 16 publications

Synergistic effect of imidacloprid combined with synergistic agents (Beichuang, Jiexiaoli) onMyzus persicae(Hemiptera: Aphididae)

Synergistic effect of imidacloprid combined with synergistic agents (Beichuang, Jiexiaoli) onMyzus persicae(Hemiptera: Aphididae)

Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution

EXPRESSION AND EFFECTS OF MUTANT Bombyx mori ACETYLCHOLINESTRASE1 IN BmN CELLS

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