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大肠杆菌IrgA同源黏附素的表达受铁摄取调节蛋白调控。

Expression of the Escherichia coli IrgA homolog adhesin is regulated by the ferric uptake regulation protein.

作者信息

Rashid Rebecca A, Tarr Phillip I, Moseley Steve L

机构信息

Department of Microbiology, University of Washington, 1959 NE Pacific St. Mailstop 357242, Seattle, WA 98195, USA.

出版信息

Microb Pathog. 2006 Dec;41(6):207-17. doi: 10.1016/j.micpath.2006.07.006. Epub 2006 Sep 6.

Abstract

The IrgA homolog adhesin (Iha) is an adherence-conferring outer membrane protein of Escherichia coli associated with enterohemorrhagic and uropathogenic strains. Here, we used primer extension analysis to identify iha promoters in O157:H7 and uropathogenic E. coli strains. Transcriptional fusions demonstrated that iha transcription is repressed by iron. Gel shifts using purified ferric uptake regulator protein (Fur) demonstrated that repression involves a direct interaction between Fur and the iha promoter. We identified strain-dependent differences in iha expression and determined that single nucleotide polymorphisms upstream of the iha promoter, in particular position -85, contribute to differences in expression levels.

摘要

IrgA同源粘附素(Iha)是一种赋予大肠杆菌粘附能力的外膜蛋白,与肠出血性和尿路致病性菌株有关。在此,我们使用引物延伸分析来鉴定O157:H7和尿路致病性大肠杆菌菌株中的iha启动子。转录融合实验表明,iha转录受到铁的抑制。使用纯化的铁摄取调节蛋白(Fur)进行的凝胶迁移实验表明,这种抑制涉及Fur与iha启动子之间的直接相互作用。我们确定了iha表达的菌株依赖性差异,并确定iha启动子上游的单核苷酸多态性,特别是-85位,导致了表达水平的差异。

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