摘要
大肠埃希氏菌(Escherichia coli)外膜蛋白OmpC与细菌耐药关系密切,但有关其高表达与大肠埃希氏菌耐药的关系研究尚不清楚.为深入探讨OmpC的耐药功能,将ompC克隆到pET-28a载体上进行诱导表达,采用MALDI-TOF质谱分析证明,重组OmpC能够在外膜上大量表达.以此高表达菌株进行四环素耐药试验发现,ompC-pET-28a-BL21的最低抑菌浓度(MIC)值是对照菌株pET-28a-BL21的64倍.研究结果从蛋白质水平进一步证明OmpC在大肠埃希氏菌耐药中的重要作用.
Outer membrane protein(OmpC) was thought to related to tetracycline resistance in E.coli,but the relationship between the overexpression of OmpC and tetracycline resistance was poorly understood.In the present study,ompC was cloned to pET-28a and MALDI-TOF showed recombined OmpC was highly expressed in the outer membrane of ompC-pET-28a-BL21.The minimum inhibitory concentration(MIC) of tetracycline of ompC-pET-28a-BL21 was 192 μg/mL,64 times higher than pET-28a-BL21.These results confirmed the importance of OmpC in tetracycline resistance in E.coli at protein level directly.
出处
《厦门大学学报(自然科学版)》
CAS
CSCD
北大核心
2010年第6期858-862,共5页
Journal of Xiamen University:Natural Science
基金
国家自然科学基金资助项目(40976080)