生物技术通报 ›› 2013, Vol. 0 ›› Issue (3): 155-159.

• 研究报告 • 上一篇    下一篇

抗生素耐药性大肠杆菌外膜蛋白mOmpAN端序列分析

赵志平,聂鑫,李再新,丁杰,张智,谢万如   

  1. 四川理工学院化学与制药工程学院,自贡 643000
  • 收稿日期:2012-08-24 修回日期:2013-03-21 出版日期:2013-03-20 发布日期:2013-03-21
  • 作者简介:赵志平,博士,讲师,研究方向:大肠杆菌耐药机制、光合细菌的综合开发和应用;E-mail :zhipingzhao@suse.edu.cn
  • 基金资助:
    国家自然科学基金项目(31100089),四川省教育厅项目(11ZB102),四川理工学院人才引进项目(2011RC12)

Sequence Analysis of Amino Terminus of mOmpA from Antibiotic Resistant Escherichia coli

Zhao Zhiping, Nie Xin, Li Zaixin, Ding Jie, Zhang Zhi, Xie Wanru   

  1. School of Chemistry and Pharmaceutical Engineering,Sichuan University of Science & Engineering,Zigong 643000)
  • Received:2012-08-24 Revised:2013-03-21 Published:2013-03-20 Online:2013-03-21

摘要: 从抗生素耐药大肠杆菌中克隆了mOmpA(突变OmpA)并构建表达载体pET32a-mOmpA。序列比对分析表明, mOmpA N 端与OmpA N端DNA 序列同源性为79.93%,氨基酸同源性为81.17%。Swiss-Model 蛋白结构预测表明,mOmpA loop 环的 方向发生了显著变化。研究结果有助于进一步了解大肠杆菌OmpA 的结构和功能以及大肠杆菌耐药机制。

关键词: 抗生素耐药, 外膜蛋白, OmpA, 大肠杆菌, 突变

Abstract: In the present study, we amplified the mOmpA from an isolated antibiotic resistant E. coli strain and subsequently constructed the expression vector pET32a-mOmpA. DNA sequence alignment analysis indicated that the amino terminus of the mOmpA shared 79.93% homology with the OmpA. The mOmpA amino terminus was 81.17% identical to that of the OmpA. Protein structure predication analysis through Swiss-Model suggested that the loops orientation of mOmpA N-termunus was dramatically changed compared with OmpA. Our present study promotes to better understand the structure and functions of E. coli OmpA and E. coli antibiotic resistance mechanisms.

Key words: Antibiotic resistance, Outer membrane protein, OmpA E. coli, Mutation