UafB is a serine-rich repeat adhesin of Staphylococcus saprophyticus that mediates binding to fibronectin, fibrinogen and human uroepithelial cells

King, Nathan P., Beatson, Scott A., Totsika, Makrina, Ulett, Glen C., Alm, Richard A., Manning, Paul A. and Schembri, Mark A. (2011) UafB is a serine-rich repeat adhesin of Staphylococcus saprophyticus that mediates binding to fibronectin, fibrinogen and human uroepithelial cells. Microbiology, 157 4: 1161-1175. doi:10.1099/mic.0.047639-0


Author King, Nathan P.
Beatson, Scott A.
Totsika, Makrina
Ulett, Glen C.
Alm, Richard A.
Manning, Paul A.
Schembri, Mark A.
Title UafB is a serine-rich repeat adhesin of Staphylococcus saprophyticus that mediates binding to fibronectin, fibrinogen and human uroepithelial cells
Formatted title
UafB is a serine-rich repeat adhesin of Staphylococcus saprophyticus that mediates binding to fibronectin, fibrinogen and human uroepithelial cells
Journal name Microbiology   Check publisher's open access policy
ISSN 1350-0872
1465-2080
Publication date 2011-04
Sub-type Article (original research)
DOI 10.1099/mic.0.047639-0
Volume 157
Issue 4
Start page 1161
End page 1175
Total pages 15
Place of publication Reading, Berks., United Kingdom
Publisher Society for General Microbiology
Collection year 2012
Language eng
Formatted abstract
Staphylococcus saprophyticus is an important cause of urinary tract infection (UTI), particularly among young women, and is second only to uropathogenic Escherichia coli as the most frequent cause of UTI. The molecular mechanisms of urinary tract colonization by S. saprophyticus remain poorly understood. We have identified a novel 6.84 kb plasmid-located adhesin-encoding gene in S. saprophyticus strain MS1146 which we have termed uro-adherence factor B (uafB). UafB is a glycosylated serine-rich repeat protein that is expressed on the surface of S. saprophyticus MS1146. UafB also functions as a major cell surface hydrophobicity factor. To characterize the role of UafB we generated an isogenic uafB mutant in S. saprophyticus MS1146 by interruption with a group II intron. The uafB 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 uafB in other staphylococci which, like uafB, appear to be located on transposable elements. Thus, our data indicate that UafB is a novel adhesin of S. saprophyticus that contributes to cell surface hydrophobicity, mediates adhesion to fibronectin and fibrinogen, and exhibits tropism for human uroepithelial cells.
Keyword ECM, extracellular matrix
TEM, transmission electron microscopy
UPEC, uropathogenic E. coli
UTI, urinary tract infection
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
 
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