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Blood, 15 September 2000, Vol. 96, No. 6, pp. 2149-2156
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Protein A is the von Willebrand factor binding protein on
Staphylococcus aureus
Jörg Hartleib,
Nicola Köhler,
Richard B. Dickinson,
Gursharan S. Chhatwal,
Jan J. Sixma,
Orla M. Hartford,
Timothy J. Foster,
Georg Peters,
Beate E. Kehrel, and
Mathias Herrmann
From the Departments of Anaesthesiology and Surgical
Intensive Care Medicine, Division of Experimental and Clinical
Hemostasis, Institute of Medical Microbiology, University of
Münster, Münster, Germany; the Department of Microbial
Pathogenesis, Gesellschaft für Biotechnologische Forschung,
Braunschweig, Germany; the Department of Chemical Engineering,
University of Florida, Gainesville, FL; Moyne Institute of Preventive
Medicine, Trinity College, Dublin, Ireland; and the Department of
Hematology, University of Utrecht, Utrecht, The Netherlands.
Endovascular infection is a highly critical complication of
invasive Staphylococcus aureus disease. For colonization,
staphylococci must first adhere to adhesive endovascular foci. Von
Willebrand factor (vWF) is a large, multimeric glycoprotein mediating
platelet adhesion at sites of endothelial damage. Earlier it was
demonstrated that vWF binds to and promotes the surface adhesion of
S. aureus, prompting this effort to identify the vWF
adhesin. In Western ligand assays of S. aureus lysates,
staphylococcal protein A (SPA) was recognized by purified vWF. Surface
plasmon resonance demonstrated the binding of soluble vWF to
immobilized recombinant protein A with a Kd of
1.49 × 10 8 mol/L. Using flow cytometry, the binding of
fluorescein isothiocyanate-labeled vWF to S. aureus was
found to be saturable and inhibitable by unlabeled vWF, antiprotein-A
antibodies, or IgG. Isogenic
 spa::Tcr mutants were constructed
by the insertion of a tetracycline resistance cassette into
spa using allelic replacement, and it exhibited decreased
binding of soluble vWF and decreased adhesion to vWF-adsorbed surfaces.
The interaction was restored on complementation of the mutants with
spa-containing plasmid pSPA7235. In conclusion, protein A
confers interaction of S. aureus with soluble and
immobilized vWF in a newly discovered function characterizing protein A
as a novel member of the staphylococcal surface protein adhesin
superfamily and suggesting its potential role in the pathogenesis of
endovascular staphylococcal disease.
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