Abstract

Staphylococcus aureus encodes a secreted von Willebrand factor-binding protein (vWbp) of 482 amino acids. The N-terminal part of this protein is homologous to staphylocoagulase and therefore we investigated whether vWbp has coagulating activity. Recombinant vWbp was shown to coagulate human and porcine plasma efficiently, but was less active against plasma from other species. The coagulation efficiency was concentration dependent, and could be inhibited by specific antibodies against vWbp. Furthermore, the species-specific coagulation by vWbp depended on the interaction with prothrombin. This interaction also resulted in specific cleavage of vWbp, releasing the C-terminal part from the coagulating domain. (C) 2004 Federation of European Micro biological Societies. Published by Elsevier B.V. All rights reserved

Published in

FEMS Microbiology Letters
2004, Volume: 234, number: 2, pages: 309-314
Publisher: ELSEVIER SCIENCE BV

SLU Authors

• Bjerketorp, Joakim

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

• Frykberg, Lars

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

• Jacobsson, Karin

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

Publication identifier

DOI: https://doi.org/10.1016/j.femsle.2004.03.040

Permanent link to this page (URI)

https://res.slu.se/id/publ/2815