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Sci Rep. 2021 Nov 23;11(1):22799. doi: 10.1038/s41598-021-02065-w.

Staphylococcus aureus iron-regulated surface determinant B (IsdB) protein interacts with von Willebrand factor and promotes adherence to endothelial cells.

Scientific reports

Mariangela J Alfeo, Anna Pagotto, Giulia Barbieri, Timothy J Foster, Karen Vanhoorelbeke, Vincenzo De Filippis, Pietro Speziale, Giampiero Pietrocola

Affiliations

  1. Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Viale Taramelli 3/b, 27100, Pavia, Italy.
  2. Department of Pharmaceutical and Pharmacological Sciences, University of Padua, Via Marzolo 5, 35131, Padua, Italy.
  3. Department of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, Via Ferrata 9, 27100, Pavia, Italy.
  4. Microbiology Department, Trinity College Dublin, Dublin, Ireland.
  5. Laboratory for Thrombosis Research, KU Leuven Campus Kulak Kortrijk, Kortrijk, Belgium.
  6. Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Viale Taramelli 3/b, 27100, Pavia, Italy. [email protected].

PMID: 34815454 PMCID: PMC8611056 DOI: 10.1038/s41598-021-02065-w

Abstract

Staphylococcus aureus is the cause of a spectrum of diseases in humans and animals. The molecular basis of this pathogenicity lies in the expression of a variety of virulence factors, including proteins that mediate adherence to the host plasma and extracellular matrix proteins. In this study, we discovered that the iron-regulated surface determinant B (IsdB) protein, besides being involved in iron transport and vitronectin binding, interacts with von Willebrand Factor (vWF). IsdB-expressing bacteria bound to both soluble and immobilized vWF. The binding of recombinant IsdB to vWF was blocked by heparin and reduced at high ionic strength. Furthermore, treatment with ristocetin, an allosteric agent that promotes the exposure of the A1 domain of vWF, potentiates the binding of IsdB to vWF. Both near-iron transporter motifs NEAT1 and NEAT2 of IsdB individually bound recombinant A1 domain with K

© 2021. The Author(s).

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