ABC  Vol.3 No.1 , February 2013
Amino terminus mutant OmpA from an isolated antibiotic resistant Escherichia coli still possess resistance to environmental stresses
ABSTRACT

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 β- 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 β-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.


Cite this paper
Zhao, Z. , Nie, X. , Li, Z. , Zhang, Z. , Ding, J. and Xie, W. (2013) Amino terminus mutant OmpA from an isolated antibiotic resistant Escherichia coli still possess resistance to environmental stresses. Advances in Biological Chemistry, 3, 108-113. doi: 10.4236/abc.2013.31014.
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