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Volume 272, Number 43, Issue of October 24, 1997 pp. 26978-26984
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

A Matrix Form of Fibronectin Mediates Enhanced Binding of Streptococcus pyogenes to Host Tissue

(Received for publication, November 4, 1996, and in revised form, June 17, 1997)

Nobuhiko Okada , Masahisa Watarai , Vered Ozeri ^¶ , Emanuel Hanski ^¶ , Michael Caparon and Chihiro Sasakawa

From the  Department of Bacteriology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan, the ^¶ Department of Clinical Microbiology, The Hebrew University Hadassah Medical School, Jerusalem 91010, Israel, and the  Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110

The pathogenic Gram-positive bacterium Streptococcus pyogenes (group A streptococcus) binds to fibronectin via protein F. In this study, we have investigated the binding properties of protein F to various multimeric tissue forms of fibronectin that appear on cell surfaces and in the extracellular matrix. We show that binding of S. pyogenes through protein F is more efficient to an in vitro-derived polymerized form of fibronectin (superfibronectin) than to soluble fibronectin immobilized in a solid phase. In addition, Chinese hamster ovary cells overexpressing the ₅₁ integrin produced an increased amount of a fibronectin matrix and consequently bound a higher number of S. pyogenes cells. Inhibition and direct binding assays using purified proteins demonstrated that binding to a fibronectin matrix involved both domains of protein F (UR and RD2) that have previously been implicated in interactions with fibronectin. Using intact S. pyogenes bacteria in which various domains of protein F were expressed as hybrids with the surface-exposed region of an unrelated protein, we revealed that, in contrast to the predominantly UR-mediated binding to soluble fibronectin, the maximal binding to the fibronectin matrix required RD2 in addition to UR. Since in some infections S. pyogenes may initially encounter a matrix form of fibronectin, these results suggest that UR and RD2 may be important for the initiation of streptococcal infectious processes.

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