Fibrinogen is a ligand for the Staphylococcus aureus Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM) Bone sialoprotein-binding protein (Bbp)

Vanessa Vazquez, Xiaowen Liang, Jenny K. Horndahl, Vannakambadi K. Ganesh, Emanuel Smeds, Timothy J. Foster, Magnus Hook

    Research output: Contribution to journalArticlepeer-review

    85 Scopus citations

    Abstract

    Microbial surface components recognizing adhesive matrix molecules (MSCRAMMs) are bacterial surface proteins mediating adherence of the microbes to components of the extracellular matrix of the host. On Staphylococci, the MSCRAMMs often have multiple ligands. Consequently, we hypothesized that the Staphylococcus aureus MSCRAMM bone sialoprotein-binding protein (Bbp) might recognize host molecules other than the identified bone protein. A ligand screen revealed that Bbp binds human fibrinogen (Fg) but not Fg from other mammals. We have characterized the interaction between Bbp and Fg. The binding site for Bbp was mapped to residues 561-575 in the Fg Aα chain using recombinant Fg chains and truncation mutants in Far Western blots and solid-phase binding assays. Surface plasmon resonance was used to determine the affinity of Bbp for Fg. The interaction of Bbp with Fg peptides corresponding to the mapped residues was further characterized using isothermal titration calorimetry. In addition, Bbp expressed on the surface of bacteria mediated adherence to immobilized Fg Aα. Also, Bbp interferes with thrombin-induced Fg coagulation. Together these data demonstrate that human Fg is a ligand for Bbp and that Bbp can manipulate the biology of the Fg ligand in the host.

    Original languageEnglish (US)
    Pages (from-to)29797-29805
    Number of pages9
    JournalJournal of Biological Chemistry
    Volume286
    Issue number34
    DOIs
    StatePublished - Aug 26 2011

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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