Pathogenic bacteria attach to human fibronectin through a tandem β-zipper

Ulrich Schwarz-Linek, Jörn M. Werner, Andrew R. Pickford, Sivashankarappa Gurusiddappa, Jung Hwa Kim Ewa, S. Pilka, John A.G. Briggs, T. Sebastian Gough, Magnus Höök, Iain D. Campbell, Jennifer R. Potts

Research output: Contribution to journalArticlepeer-review

317 Scopus citations


Staphylococcus aureus and Streptococcus pyogenes, two important human pathogens, target host fibronectin (Fn) in their adhesion to and invasion of host cells. Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats in an unfolded region of the protein. The bacterium-binding site in the amino-terminal domain ( 1-5F1) of Fn contains five sequential Fn type 1 (F1) modules. Here we show the structure of a streptococcal (S. dysgalactiae) FnBP peptide (B3) in complex with the module pair 1F1 2F1. This identifies 1F1- and 2F1-binding motifs in B3 that form additional antiparallel β-strands on sequential F1 modules - the first example of a tandem β-zipper. Sequence analyses of larger regions of FnBPs from S. pyogenes and S. aureus reveal a repeating pattern of F1-binding motifs that match the pattern of F1 modules in 1-5F1 of Fn. In the process of Fn-mediated invasion of host cells, therefore, the bacterial proteins seem to exploit the modular structure of Fn by forming extended tandem β-zippers. This work is a vital step forward in explaining the full mechanism of the integrin-dependent FnBp-mediated invasion of host cells.

Original languageEnglish (US)
Pages (from-to)177-181
Number of pages5
Issue number6936
StatePublished - May 8 2003

ASJC Scopus subject areas

  • General


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