作者
Barbara Woebking, Galya Reuter, Richard A Shilling, Saroj Velamakanni, Sanjay Shahi, Henrietta Venter, Lekshmy Balakrishnan, Hendrik W van Veen
发表日期
2005/9/15
期刊
Journal of bacteriology
卷号
187
期号
18
页码范围
6363-6369
出版商
American Society for Microbiology
简介
MsbA is an essential ATP-binding cassette half-transporter in the cytoplasmic membrane of the gram-negative Escherichia coli and is required for the export of lipopolysaccharides (LPS) to the outer membrane, most likely by transporting the lipid A core moiety. Consistent with the homology of MsbA to the multidrug transporter LmrA in the gram-positive Lactococcus lactis, our recent work in E. coli suggested that MsbA might interact with multiple drugs. To enable a more detailed analysis of multidrug transport by MsbA in an environment deficient in LPS, we functionally expressed MsbA in L. lactis. MsbA expression conferred an 86-fold increase in resistance to the macrolide erythromycin. A kinetic characterization of MsbA-mediated ethidium and Hoechst 33342 transport revealed apparent single-site kinetics and competitive inhibition of these transport reactions by vinblastine with Ki values of 16 and 11 μM …
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B Woebking, G Reuter, RA Shilling, S Velamakanni… - Journal of bacteriology, 2005