Staphylococcal superantigen-like 5 activates platelets and supports platelet adhesion under flow conditions, which involves glycoprotein Ibα and αIIbβ3

C. J.C. De Haas, C. Weeterings, M. M. Vughs, P. G. De Groot, J. A. Van Strijp, T. Lisman*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

42 Citations (Scopus)

Abstract

Objectives: Staphylococcal superantigen-like 5 (SSL5) is an exoprotein secreted by Staphylococcus aureus that has been shown to inhibit neutrophil rolling over activated endothelial cells via a direct interaction with P-selectin glycoprotein ligand 1 (PSGL-1). Methods and Results: When purified recombinant SSL5 was added to washed platelets in an aggregometry set-up, complete and irreversible aggregation was observed. Proteolysis of the extracellular part of GPIbα or the addition of dRGDW abrogated platelet aggregation. When a mixture of isolated platelets and red cells was perfused over immobilized SSL5 at a shear rate of 300 s-1, stable platelet aggregates were observed, and platelet deposition was substantially reduced after proteolysis of GPIb or after addition of dRGDW. SSL5 was shown to interact with glycocalicin, a soluble GPIbα fragment, and binding of SSL5 to platelets resulted in GPIb-mediated signal transduction as evidenced by translocation of 14-3-3ζ. In addition, SSL5 was shown to interact with endothelial cell matrix (ECM) and this interaction enhanced aggregation of platelets from whole blood to this ECM. Conclusions: SSL5 activates and aggregates platelets in a GPIbα-dependent manner, which could be important in colonization of the vascular bed and evasion of the immune system by S. aureus.

Original languageEnglish
Pages (from-to)1867-1874
Number of pages8
JournalJournal of Thrombosis and Haemostasis
Volume7
Issue number11
DOIs
Publication statusPublished - 1 Nov 2009

Keywords

  • Flow conditions
  • GPIbα
  • Platelets
  • S. aureus
  • SSL5

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