High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules

Ulrich Schwarz-Linek, Ewa S. Pilka, Andrew R. Pickford, Jung Hwa Kim, Magnus Höök, Iain D. Campbell, Jennifer R. Potts

    Research output: Contribution to journalArticlepeer-review

    61 Scopus citations

    Abstract

    Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrin-dependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

    Original languageEnglish (US)
    Pages (from-to)39017-39025
    Number of pages9
    JournalJournal of Biological Chemistry
    Volume279
    Issue number37
    DOIs
    StatePublished - Sep 10 2004

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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