%0 Journal Article %T Amino terminus mutant OmpA from an isolated antibiotic resistant <i>Escherichia</i> <i>coli</i> still possess resistance to environmental stresses %A Zhiping Zhao %A Xin Nie %A Zaixin Li %A Zhi Zhang %A Jie Ding %A Wanru Xie %J Advances in Biological Chemistry %P 108-113 %@ 2162-2191 %D 2013 %I Scientific Research Publishing %R 10.4236/abc.2013.31014 %X

Antibiotic resistant Escherichia coli strains are becoming more common recently. OmpA is a very important antigen protein of E. coli, which consists of two separate domains, N-terminal and C-terminal domain. The N-terminal domain contains eight ¦Ā- barrel regions that plays important roles in the multifaceted functions of OmpA. In the present study, we cloned a mutant OmpA gene from a multi-antibiotic resistant E. coli strain. Sequence analysis indicated that the N-terminal DNA sequence of the mutant OmpA shared 81.05% homology with the modeled OmpA from E. coli K12 and the N-terminal amino acid sequence of the mutant OmpA was 81.22% identical to that of the E. coli K12 OmpA. Moreover, several amino acids located in the ¦Ā-barrel region were mutated. The mutant OmpA was expressed in BL21 suggested by SDS-PAGE. Resistance to environmental stress assay indicated that the N-terminus mutant OmpA still possessed excellent activities in pH, temperature and osmotic pressure resistance. Our pre- sent study may supply insights into better and deeper understand the relationships between OmpA N-terminal regions and its functions in environmental stress conditions and the mechanisms on antibiotic resistance of E. coli.

%K Antibiotic Resistance %K OmpA %K Environmental Stress %K < %K i> %K E.< %K /i> %K < %K i> %K coli< %K /i> %U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=28130