The von Willebrand factor-binding protein (vWbp) of Staphylococcus aureus is a coagulase.
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.
Bjerketorp
Joakim
J
Department of Microbiology, Swedish University of Agricultural Sciences, SLU, Box 7025, SE-75007 Uppsala, Sweden.
Jacobsson
Karin
K
Frykberg
Lars
L
D000818:Animals; D001483:Base Sequence; D001777:Blood Coagulation; D003030:Coagulase / Q000235:genetics / Q000378:metabolism*; D017931:DNA Primers; D006801:Humans; D010980:Platelet Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D011817:Rabbits; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000235:genetics
D003030:Coagulase; D017931:DNA Primers; D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; C028254:von Willebrand factor receptor