铜绿假单胞菌外膜蛋白OprH的膜拓扑结构：PCR介导的定点插入和缺失诱变
Membrane topology of the outer membrane protein OprH from Pseudomonas aeruginosa: PCR-mediated site-directed insertion and deletion mutagenesis.
作者信息
Rehm B H, Hancock R E
机构信息
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
出版信息
J Bacteriol. 1996 Jun;178(11):3346-9. doi: 10.1128/jb.178.11.3346-3349.1996.
Abstract
The 21-kDa outer membrane protein OprH from Pseudomonas aeruginosa is overexpressed under Mg2+ starvation conditions and when overproduced causes resistance to polymyxin B, gentamicin, and EDTA. By circular dichroism analysis, OprH revealed a calculated beta-sheet structure content of 47.3%. PCR-based site-directed deletion and epitope insertion mutagenesis was used to test a topological model of OprH as an eight-stranded beta-barrel. Three permissive and seven nonpermissive malarial epitope insertion mutants and four permissive and four nonpermissive deletion mutants confirmed the general accuracy of this model. Thus, OprH is the smallest outer membrane protein to date to be confirmed as a beta-stranded protein.
摘要
铜绿假单胞菌的21-kDa外膜蛋白OprH在Mg2+饥饿条件下过表达，过量产生时会导致对多粘菌素B、庆大霉素和EDTA产生抗性。通过圆二色性分析，OprH显示计算出的β-折叠结构含量为47.3%。基于PCR的定点缺失和表位插入诱变用于测试OprH作为八链β-桶的拓扑模型。三个允许和七个不允许的疟疾表位插入突变体以及四个允许和四个不允许的缺失突变体证实了该模型的总体准确性。因此，OprH是迄今为止被确认为β-链蛋白的最小外膜蛋白。
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