Streptococcal M1 protein constructs a pathological host fibrinogen network

Pauline Macheboeuf, Cosmo Buffalo, Chi-yu Fu, Annelies S. Zinkernagel, Jason N. Cole, John E. Johnson, Victor Nizet and Partho Ghosh ()
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Pauline Macheboeuf: University of California
Cosmo Buffalo: University of California
Chi-yu Fu: The Scripps Research Institute
Annelies S. Zinkernagel: University of California
Jason N. Cole: University of California
John E. Johnson: The Scripps Research Institute
Victor Nizet: University of California
Partho Ghosh: University of California

Nature, 2011, vol. 472, issue 7341, 64-68

Abstract: 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.

Date: 2011
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DOI: 10.1038/nature09967

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