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Functional study on the mutations in the silkworm (Bombyx mori) acetylcholinesterase type 1 gene (ace1) and its recombinant proteins.(Report)

Byline: Ju-mei Wang (1), Bin-bin Wang (1), Yi Xie (1), Shan-shan Sun (1), Zhi-ya Gu (1), Lie Ma (1), Fan-chi Li (1), Yi-fan Zhao (1), Bin Yang (3), Wei-de Shen (1,2), Bing Li (1,2) Keywords: Bombyx mori; Acetylcholinesterase; Gene mutation Abstract: The acetylcholinesterase of Lepidoptera insects is... Full description

Journal Title: Molecular Biology Reports Jan, 2014, Vol.41(1), p.429(9)
Main Author: Wang, Ju - Mei
Other Authors: Wang, Bin - Bin , Xie, Yi , Sun, Shan - Shan , Gu, Zhi - Ya , Ma, Lie , Li, Fan - Chi , Zhao, Yi - Fan , Yang, Bin , Shen, Wei - De , Li, Bing
Format: Electronic Article Electronic Article
Language: English
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ID: ISSN: 0301-4851
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recordid: gale_ofa354367389
title: Functional study on the mutations in the silkworm (Bombyx mori) acetylcholinesterase type 1 gene (ace1) and its recombinant proteins.(Report)
format: Article
creator:
  • Wang, Ju - Mei
  • Wang, Bin - Bin
  • Xie, Yi
  • Sun, Shan - Shan
  • Gu, Zhi - Ya
  • Ma, Lie
  • Li, Fan - Chi
  • Zhao, Yi - Fan
  • Yang, Bin
  • Shen, Wei - De
  • Li, Bing
subjects:
  • Genetic Research -- Genetic Aspects
  • Pesticide Resistance -- Genetic Aspects
  • Recombinant Proteins -- Genetic Aspects
  • Genes -- Genetic Aspects
  • Gene Mutation -- Genetic Aspects
  • Glycine
ispartof: Molecular Biology Reports, Jan, 2014, Vol.41(1), p.429(9)
description: Byline: Ju-mei Wang (1), Bin-bin Wang (1), Yi Xie (1), Shan-shan Sun (1), Zhi-ya Gu (1), Lie Ma (1), Fan-chi Li (1), Yi-fan Zhao (1), Bin Yang (3), Wei-de Shen (1,2), Bing Li (1,2) Keywords: Bombyx mori; Acetylcholinesterase; Gene mutation Abstract: The acetylcholinesterase of Lepidoptera insects is encoded by two genes, ace1 and ace2. The expression of the ace1 gene is significantly higher than that of the ace2 gene, and mutations in ace1 are one of the major reasons for pesticide resistance in insects. In order to investigate the effects of the mutations in ace1's characteristic sites on pesticide resistance, we generated mutations for three amino acids using site-directed mutagenesis, which were Ala(GCG)303Ser(TCG), Gly(GGA)329Ala(GCA) and Leu (TCT)554Ser(TTC). The Baculovirus expression system was used for the eukaryotic expression of the wild type ace1 (wace1) and the mutant ace1 (mace1). SDS-PAGE and Western blotting were used to detect the targeting proteins with expected sizeof about 76 kDa. The expression products were purified for the determination of AChE activity and the inhibitory effects of physostigmine and phoxim. We observed no significant differences in the overall activity of the wild type and mutant AChEs. However, with 10 min of physostigmine (10 uM) inhibition, the remaining activity of the wild type AChE was significantly lower than that of the mutant AChE. Ten min inhibition with 33.4 uM phoxim also resulted in significantly lower remaining activity of the wild type AChE than that of the mutant AChE. These results indicated that mutations for the three amino acids reduced the sensitivity of AChE to physostigmine and phoxim, which laid the foundation for future in vivo studies on AChE's roles in pesticide resistance. Author Affiliation: (1) School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (2) National Engineering Laboratory for Modern Silk, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (3) Jiangsu Minxing Cocoon Silk Stock Co., Ltd, Dongtai, 224200, Jiangsu, People's Republic of China Article History: Registration Date: 19/11/2013 Received Date: 21/01/2013 Accepted Date: 19/11/2013 Online Date: 10/12/2013 Article note: Ju-mei Wang, Bin-bin Wang and Yi Xie have contributed equally to the study.
language: English
source:
identifier: ISSN: 0301-4851
fulltext: fulltext
issn:
  • 0301-4851
  • 03014851
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titleFunctional study on the mutations in the silkworm (Bombyx mori) acetylcholinesterase type 1 gene (ace1) and its recombinant proteins.(Report)
creatorWang, Ju - Mei ; Wang, Bin - Bin ; Xie, Yi ; Sun, Shan - Shan ; Gu, Zhi - Ya ; Ma, Lie ; Li, Fan - Chi ; Zhao, Yi - Fan ; Yang, Bin ; Shen, Wei - De ; Li, Bing
ispartofMolecular Biology Reports, Jan, 2014, Vol.41(1), p.429(9)
identifierISSN: 0301-4851
subjectGenetic Research -- Genetic Aspects ; Pesticide Resistance -- Genetic Aspects ; Recombinant Proteins -- Genetic Aspects ; Genes -- Genetic Aspects ; Gene Mutation -- Genetic Aspects ; Glycine
descriptionByline: Ju-mei Wang (1), Bin-bin Wang (1), Yi Xie (1), Shan-shan Sun (1), Zhi-ya Gu (1), Lie Ma (1), Fan-chi Li (1), Yi-fan Zhao (1), Bin Yang (3), Wei-de Shen (1,2), Bing Li (1,2) Keywords: Bombyx mori; Acetylcholinesterase; Gene mutation Abstract: The acetylcholinesterase of Lepidoptera insects is encoded by two genes, ace1 and ace2. The expression of the ace1 gene is significantly higher than that of the ace2 gene, and mutations in ace1 are one of the major reasons for pesticide resistance in insects. In order to investigate the effects of the mutations in ace1's characteristic sites on pesticide resistance, we generated mutations for three amino acids using site-directed mutagenesis, which were Ala(GCG)303Ser(TCG), Gly(GGA)329Ala(GCA) and Leu (TCT)554Ser(TTC). The Baculovirus expression system was used for the eukaryotic expression of the wild type ace1 (wace1) and the mutant ace1 (mace1). SDS-PAGE and Western blotting were used to detect the targeting proteins with expected sizeof about 76 kDa. The expression products were purified for the determination of AChE activity and the inhibitory effects of physostigmine and phoxim. We observed no significant differences in the overall activity of the wild type and mutant AChEs. However, with 10 min of physostigmine (10 uM) inhibition, the remaining activity of the wild type AChE was significantly lower than that of the mutant AChE. Ten min inhibition with 33.4 uM phoxim also resulted in significantly lower remaining activity of the wild type AChE than that of the mutant AChE. These results indicated that mutations for the three amino acids reduced the sensitivity of AChE to physostigmine and phoxim, which laid the foundation for future in vivo studies on AChE's roles in pesticide resistance. Author Affiliation: (1) School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (2) National Engineering Laboratory for Modern Silk, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (3) Jiangsu Minxing Cocoon Silk Stock Co., Ltd, Dongtai, 224200, Jiangsu, People's Republic of China Article History: Registration Date: 19/11/2013 Received Date: 21/01/2013 Accepted Date: 19/11/2013 Online Date: 10/12/2013 Article note: Ju-mei Wang, Bin-bin Wang and Yi Xie have contributed equally to the study.
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titleFunctional study on the mutations in the silkworm (Bombyx mori) acetylcholinesterase type 1 gene (ace1) and its recombinant proteins.(Report)
descriptionByline: Ju-mei Wang (1), Bin-bin Wang (1), Yi Xie (1), Shan-shan Sun (1), Zhi-ya Gu (1), Lie Ma (1), Fan-chi Li (1), Yi-fan Zhao (1), Bin Yang (3), Wei-de Shen (1,2), Bing Li (1,2) Keywords: Bombyx mori; Acetylcholinesterase; Gene mutation Abstract: The acetylcholinesterase of Lepidoptera insects is encoded by two genes, ace1 and ace2. The expression of the ace1 gene is significantly higher than that of the ace2 gene, and mutations in ace1 are one of the major reasons for pesticide resistance in insects. In order to investigate the effects of the mutations in ace1's characteristic sites on pesticide resistance, we generated mutations for three amino acids using site-directed mutagenesis, which were Ala(GCG)303Ser(TCG), Gly(GGA)329Ala(GCA) and Leu (TCT)554Ser(TTC). The Baculovirus expression system was used for the eukaryotic expression of the wild type ace1 (wace1) and the mutant ace1 (mace1). SDS-PAGE and Western blotting were used to detect the targeting proteins with expected sizeof about 76 kDa. The expression products were purified for the determination of AChE activity and the inhibitory effects of physostigmine and phoxim. We observed no significant differences in the overall activity of the wild type and mutant AChEs. However, with 10 min of physostigmine (10 uM) inhibition, the remaining activity of the wild type AChE was significantly lower than that of the mutant AChE. Ten min inhibition with 33.4 uM phoxim also resulted in significantly lower remaining activity of the wild type AChE than that of the mutant AChE. These results indicated that mutations for the three amino acids reduced the sensitivity of AChE to physostigmine and phoxim, which laid the foundation for future in vivo studies on AChE's roles in pesticide resistance. Author Affiliation: (1) School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (2) National Engineering Laboratory for Modern Silk, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (3) Jiangsu Minxing Cocoon Silk Stock Co., Ltd, Dongtai, 224200, Jiangsu, People's Republic of China Article History: Registration Date: 19/11/2013 Received Date: 21/01/2013 Accepted Date: 19/11/2013 Online Date: 10/12/2013 Article note: Ju-mei Wang, Bin-bin Wang and Yi Xie have contributed equally to the study.
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titleFunctional study on the mutations in the silkworm (Bombyx mori) acetylcholinesterase type 1 gene (ace1) and its recombinant proteins.(Report)
authorWang, Ju - Mei ; Wang, Bin - Bin ; Xie, Yi ; Sun, Shan - Shan ; Gu, Zhi - Ya ; Ma, Lie ; Li, Fan - Chi ; Zhao, Yi - Fan ; Yang, Bin ; Shen, Wei - De ; Li, Bing
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abstractByline: Ju-mei Wang (1), Bin-bin Wang (1), Yi Xie (1), Shan-shan Sun (1), Zhi-ya Gu (1), Lie Ma (1), Fan-chi Li (1), Yi-fan Zhao (1), Bin Yang (3), Wei-de Shen (1,2), Bing Li (1,2) Keywords: Bombyx mori; Acetylcholinesterase; Gene mutation Abstract: The acetylcholinesterase of Lepidoptera insects is encoded by two genes, ace1 and ace2. The expression of the ace1 gene is significantly higher than that of the ace2 gene, and mutations in ace1 are one of the major reasons for pesticide resistance in insects. In order to investigate the effects of the mutations in ace1's characteristic sites on pesticide resistance, we generated mutations for three amino acids using site-directed mutagenesis, which were Ala(GCG)303Ser(TCG), Gly(GGA)329Ala(GCA) and Leu (TCT)554Ser(TTC). The Baculovirus expression system was used for the eukaryotic expression of the wild type ace1 (wace1) and the mutant ace1 (mace1). SDS-PAGE and Western blotting were used to detect the targeting proteins with expected sizeof about 76 kDa. The expression products were purified for the determination of AChE activity and the inhibitory effects of physostigmine and phoxim. We observed no significant differences in the overall activity of the wild type and mutant AChEs. However, with 10 min of physostigmine (10 uM) inhibition, the remaining activity of the wild type AChE was significantly lower than that of the mutant AChE. Ten min inhibition with 33.4 uM phoxim also resulted in significantly lower remaining activity of the wild type AChE than that of the mutant AChE. These results indicated that mutations for the three amino acids reduced the sensitivity of AChE to physostigmine and phoxim, which laid the foundation for future in vivo studies on AChE's roles in pesticide resistance. Author Affiliation: (1) School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (2) National Engineering Laboratory for Modern Silk, Soochow University, Suzhou, 215123, Jiangsu, People's Republic of China (3) Jiangsu Minxing Cocoon Silk Stock Co., Ltd, Dongtai, 224200, Jiangsu, People's Republic of China Article History: Registration Date: 19/11/2013 Received Date: 21/01/2013 Accepted Date: 19/11/2013 Online Date: 10/12/2013 Article note: Ju-mei Wang, Bin-bin Wang and Yi Xie have contributed equally to the study.
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