The N-terminal and central domain of colicin A enables phage lysin to lyse Escherichia coli extracellularly
作者: Guangmou YanJianfang LiuQiang MaRining ZhuZhimin GuoChencheng GaoShuang WangLing YuJingmin GuDongliang HuWenyu HanRui DuJunling YangLiancheng Lei
作者单位: 1Jilin University
2The Second Hospital of Jilin University
3Kitasato University School of Veterinary Medicine
4Jilin Agricultural University
刊名: Antonie van Leeuwenhoek, 2017, Vol.110 (12), pp.1627-1635
来源数据库: Springer Nature Journal
DOI: 10.1007/s10482-017-0912-9
关键词: BacteriophageBacteriophage lysinEscherichia coliGram-negative bacteriaAntimicrobial resistance
英文摘要: Multidrug-resistant Escherichia coli has seriously threatened antibiotic resources and international public health. Bacteriophage lysin preparations have been widely considered as valid agents for solving multidrug resistances. Many lysins have been derived to treat diseases caused by Gram-positive bacteria, but only a few lysin preparations have been found that successively treat diseases caused by Gram-negative bacteria. The outer membrane of Gram-negative bacteria effectively blocks the interactions between peptidoglycan in the periplasmic space and bacteriophage lysins, which therefore hampers the antimicrobial effects of bacteriophage lysins. In this study, a new fusion protein (Colicin-Lysep3) was constructed by fusing the translocation and receptor binding domains of colicin A with...
原始语种摘要: Multidrug-resistant Escherichia coli has seriously threatened antibiotic resources and international public health. Bacteriophage lysin preparations have been widely considered as valid agents for solving multidrug resistances. Many lysins have been derived to treat diseases caused by Gram-positive bacteria, but only a few lysin preparations have been found that successively treat diseases caused by Gram-negative bacteria. The outer membrane of Gram-negative bacteria effectively blocks the interactions between peptidoglycan in the periplasmic space and bacteriophage lysins, which therefore hampers the antimicrobial effects of bacteriophage lysins. In this study, a new fusion protein (Colicin-Lysep3) was constructed by fusing the translocation and receptor binding domains of colicin A with...
全文获取路径: Springer Nature  (合作)
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影响因子:2.072 (2012)

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关键词翻译
关键词翻译
  • colicin 大肠菌素
  • lysin 细胞溶素
  • Escherichia 埃希氏菌属
  • bacteriophage 噬菌体
  • negative 负象
  • demonstrated 探明的储量
  • bacteria 细菌
  • peptidoglycan 肽聚糖
  • widely 广泛地
  • mouse 小鼠