Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3417111 | Microbial Pathogenesis | 2006 | 11 Pages |
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.
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Authors
Rebecca A. Rashid, Phillip I. Tarr, Steve L. Moseley,