抗生素耐药性大肠杆菌外膜蛋白mOmpA N端序列分析

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

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。

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 orE. coli OmpA and E. coli antibiotic resistance mechanisms.