1887

Abstract

is an important cause of urinary tract infection (UTI), particularly among young women, and is second only to uropathogenic as the most frequent cause of UTI. The molecular mechanisms of urinary tract colonization by remain poorly understood. We have identified a novel 6.84 kb plasmid-located adhesin-encoding gene in strain MS1146 which we have termed uro-adherence factor B (). UafB is a glycosylated serine-rich repeat protein that is expressed on the surface of MS1146. UafB also functions as a major cell surface hydrophobicity factor. To characterize the role of UafB we generated an isogenic mutant in MS1146 by interruption with a group II intron. The mutant had a significantly reduced ability to bind to fibronectin and fibrinogen. Furthermore, we show that a recombinant protein containing the putative binding domain of UafB binds specifically to fibronectin and fibrinogen. UafB was not involved in adhesion in a mouse model of UTI; however, we observed a striking UafB-mediated adhesion phenotype to human uroepithelial cells. We have also identified genes homologous to in other staphylococci which, like , appear to be located on transposable elements. Thus, our data indicate that UafB is a novel adhesin of that contributes to cell surface hydrophobicity, mediates adhesion to fibronectin and fibrinogen, and exhibits tropism for human uroepithelial cells.

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2011-04-01
2024-04-19
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