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Streptococcal M1 protein constructs a pathological host fibrinogen network

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  • Pauline Macheboeuf

    (University of California
    Present addresses: Unit of Virus Host Cell Interactions, UMI 3265, Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz 38042 Grenoble, France (P.M.); University Hospital Zurich, University Zurich, Rämistrstr. 100, 8091 Zurich, Switzerland (A.S.Z.).)

  • Cosmo Buffalo

    (University of California)

  • Chi-yu Fu

    (The Scripps Research Institute)

  • Annelies S. Zinkernagel

    (University of California
    Present addresses: Unit of Virus Host Cell Interactions, UMI 3265, Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz 38042 Grenoble, France (P.M.); University Hospital Zurich, University Zurich, Rämistrstr. 100, 8091 Zurich, Switzerland (A.S.Z.).)

  • Jason N. Cole

    (University of California
    School of Chemistry and Molecular Biosciences, The University of Queensland)

  • John E. Johnson

    (The Scripps Research Institute)

  • Victor Nizet

    (University of California
    School of Pharmacy and Pharmaceutical Sciences, University of California)

  • Partho Ghosh

    (University of California)

Abstract

M1 protein, a major virulence factor of the leading invasive strain of group A Streptococcus, is sufficient to induce toxic-shock-like vascular leakage and tissue injury. These events are triggered by the formation of a complex between M1 and fibrinogen that, unlike M1 or fibrinogen alone, leads to neutrophil activation. Here we provide a structural explanation for the pathological properties of the complex formed between streptococcal M1 and human fibrinogen. A conformationally dynamic coiled-coil dimer of M1 was found to organize four fibrinogen molecules into a specific cross-like pattern. This pattern supported the construction of a supramolecular network that was required for neutrophil activation but was distinct from a fibrin clot. Disruption of this network into other supramolecular assemblies was not tolerated. These results have bearing on the pathophysiology of streptococcal toxic shock.

Suggested Citation

  • Pauline Macheboeuf & Cosmo Buffalo & Chi-yu Fu & Annelies S. Zinkernagel & Jason N. Cole & John E. Johnson & Victor Nizet & Partho Ghosh, 2011. "Streptococcal M1 protein constructs a pathological host fibrinogen network," Nature, Nature, vol. 472(7341), pages 64-68, April.
    • Handle: RePEc:nat:nature:v:472:y:2011:i:7341:d:10.1038_nature09967
    DOI: 10.1038/nature09967
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    Cited by:

    1. Qianqiao Liu & Beth M. Stadtmueller, 2023. "SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights into host-pathogen interactions," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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