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Microbiology. 2002 Jul;148(Pt 7):2037-2044. doi: 10.1099/00221287-148-7-2037.

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus.

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Department of Microbiology, Swedish University of Agricultural Sciences, Box 7025, SE-75007 Uppsala, Sweden1.
Department of Infectious Diseases and Medical Microbiology, Lund University, Sölvegatan 23, SE-22362 Lund, Sweden2.
Department of Microbiology, Pathology and Immunology, Huddinge University Hospital, Karolinska Institutet, SE-14186 Huddinge, Sweden3.


When a shotgun phage-display library of Staphylococcus aureus Newman was affinity selected (panned) against recombinant von Willebrand factor (vWf), a novel von Willebrand factor binding protein (vWbp) was found. Experimental data indicate that the interaction between vWbp and vWf is very specific and mediated by a region of 26 aa residues in the C-terminal part of vWbp. vWbp has an N-terminal secretory signal sequence but no cell wall anchoring motif, suggesting a soluble extracellular location. Mature vWbp could be purified from the culture supernatant and the identity of the protein was confirmed by N-terminal sequencing. vWbp migrates with an apparent molecular mass of 66 kDa and the deduced protein consists of 482 aa. The gene encoding vWbp, named vwb, was present in all S. aureus strains investigated.

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