Martin Nilsson (a), Joakim Bjerketorp (a), Åsa Wiebensjö (a), Åsa Ljungh (b), Lars Frykberg (a) and Bengt Guss (a)
FEMS Microbiology Letters, 2004, 234:155-161
Abstract
In the present study, a phage display library covering the genome of Staphylococcus lugdunensis, was affinity-selected against von Willebrand factor (vWf). This led to the identification of a gene, vwbl, encoding a putative cell surface protein of 2060 amino acids, denoted vWbl. The deduced protein has an overall organisation typical of staphylococcal cell surface proteins, with an N-terminal signal peptide, and a C-terminal cell wall sorting signal. The vWf-binding part is located in repetitive domains and antibodies against vWbl or vWf can inhibit the binding. Southern blot analysis showed that vwbl was present in the 12 S. lugdunensis strains tested.
Author Keywords: Coagulase-negative staphylococci; Staphylococcus lugdunensis; Phage display; von Willebrand factor; Adhesin; LPXTG motif
Corresponding author. Tel.: +46-0-1867-3205; fax: +46-0-1867-3392
(a) Department of Microbiology, Swedish University of Agricultural Sciences, SE75007, Uppsala, Sweden
(b) Department of Medical Microbiology, Dermatology and Infection, Lund University, Sölvegatan 23, SE223 62, Lund, Sweden | 
