HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Bjerketorp, J. Articles by Frykberg, L. Search for Related Content PubMed PubMed Citation Articles by Bjerketorp, J. Articles by Frykberg, L. Agricola Articles by Bjerketorp, J. Articles by Frykberg, L.

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus^a

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

Author for correspondence: Lars Frykberg. Tel: +46 18673299. Fax: +46 18673392. e-mail: Lars.Frykberg{at}mikrob.slu.se

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.

Keywords: receptin, virulence factor, phage display

Abbreviations: HSA, human serum albumin; HRP, horseradish peroxidase; RT, room temperature; vWf, von Willebrand factor; vWbp, von Willebrand factor binding protein

^a The GenBank accession number for the sequence reported in this paper is AY032850.

This article has been cited by other articles:

				K. L. Frank, J. L. del Pozo, and R. Patel From Clinical Microbiology to Infection Pathogenesis: How Daring To Be Different Works for Staphylococcus lugdunensis Clin. Microbiol. Rev., January 1, 2008; 21(1): 111 - 133. [Abstract] [Full Text] [PDF]

				N. Harraghy, D. Homerova, M. Herrmann, and J. Kormanec Mapping the Transcription Start Points of the Staphylococcus aureus eap, emp, and vwb Promoters Reveals a Conserved Octanucleotide Sequence That Is Essential for Expression of These Genes J. Bacteriol., January 1, 2008; 190(1): 447 - 451. [Abstract] [Full Text] [PDF]

				S. Watanabe, T. Ito, F. Takeuchi, M. Endo, E. Okuno, and K. Hiramatsu Structural Comparison of Ten Serotypes of Staphylocoagulases in Staphylococcus aureus J. Bacteriol., June 1, 2005; 187(11): 3698 - 3707. [Abstract] [Full Text] [PDF]

				N. Harraghy, J. Kormanec, C. Wolz, D. Homerova, C. Goerke, K. Ohlsen, S. Qazi, P. Hill, and M. Herrmann sae is essential for expression of the staphylococcal adhesins Eap and Emp Microbiology, June 1, 2005; 151(6): 1789 - 1800. [Abstract] [Full Text] [PDF]

				J. Bjerketorp, A. Rosander, M. Nilsson, K. Jacobsson, and L. Frykberg Sorting a Staphylococcus aureus phage display library against ex vivo biomaterial J. Med. Microbiol., October 1, 2004; 53(10): 945 - 951. [Abstract] [Full Text] [PDF]

				T. Wall, S. Roos, K. Jacobsson, A. Rosander, and H. Jonsson Phage display reveals 52 novel extracellular and transmembrane proteins from Lactobacillus reuteri DSM 20016T Microbiology, December 1, 2003; 149(12): 3493 - 3505. [Abstract] [Full Text] [PDF]