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Staphylococcus aureus Keratinocyte Invasion Is Dependent upon Multiple High-Affinity Fibronectin- Binding Repeats within FnBPA

by Andrew M. Edwards, Ursula Potter, Nicola A. G. Meenan, Jennifer R. Potts, Ruth C. Massey
"... Staphylococcus aureus is a commensal organism and a frequent cause of skin and soft tissue infections, which can progress to serious invasive disease. This bacterium uses its fibronectin binding proteins (FnBPs) to invade host cells and it has been hypothesised that this provides a protected niche f ..."
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invasion but not to the same levels as S. aureus expressing an FnBPA variant containing three high-affinity repeats. In summary, invasion of keratinocytes by S. aureus requires multiple high-affinity

Staphylococcus aureus Host Cell Invasion and Virulence in Sepsis is Facilitated by the Multiple Repeats within FnBPA. PLoS Pathog. 6(6): e1000964

by Andrew M. Edwards, Jennifer R. Potts, Elisabet Josefsson, Ruth C. Massey , 2010
"... Entry of Staphylococcus aureus into the bloodstream can lead to metastatic abscess formation and infective endocarditis. Crucial to the development of both these conditions is the interaction of S. aureus with endothelial cells. In vivo and in vitro studies have shown that the staphylococcal invasin ..."
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be facilitated by a single high-affinity, but not low-affinity FnBR. Studies using a nisin-inducible system that controlled surface expression of FnBPA revealed that variants encoding fewer FnBRs required higher levels of surface expression to mediate invasion. High expression levels of FnBPA bearing a single

Research article Fibronectin-binding protein B variation in Staphylococcus aureus Open Access

by Fiona M Burke, Niamh Mccormack, Simonetta Rindi, Pietro Speziale, Timothy J Foster
"... Background: Fibronectin binding proteins A and B (FnBPA and FnBPB) mediate adhesion of S. aureus to fibrinogen, elastin and fibronectin. We previously identified seven different isotypes of FnBPA based on divergence in the fibrinogen- and elastin-binding A domains. The variation created differences ..."
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in antigenicity while ligand binding functions were retained. Here, FnBPB variation was examined in both human and bovine isolates and compared to that of FnBPA. Results: Seven different fnbB allelic variants were identified. Some strains that cluster by phylogenetic analysis contain different fnbB variants

Correspondence

by Rebecca M. Corrigan, David Rigby, Pauline H, Timothy J. Foster, Timothy J. Foster , 2007
"... Staphylococcus aureus colonizes the moist squamous epithelium of the anterior nares. One of the adhesins likely to be responsible is the S. aureus surface protein G (SasG), which has sequence similarity with the proteins Pls (plasmin sensitive) of S. aureus and Aap (accumulation associated protein) ..."
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. Expression of SasG masked the ability of exponentially grown S. aureus cells expressing protein A (Spa), clumping factor B (ClfB) and the fibronectin binding proteins A and B (FnBPA and FnBPB) to bind to IgG, cytokeratin 10 and fibronectin, respectively. SasG also masked binding to fibrinogen mediated
Results 1 - 4 of 4