White Rose University Consortium logo
University of Leeds logo University of Sheffield logo York University logo

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

Schwarz-Linek, U., Werner, J.M., Pickford, A.R., Gurusiddappa, S., Kim, J.H., Pilka, E.S., Briggs, J.A.G., Gough, T.S., Hook, M., Campbell, I.D. and Potts, J.R. (2003) Pathogenic bacteria attach to human fibronectin through a tandem ß-zipper. Nature, 423 (6936). pp. 177-181. ISSN 0028-0836

Full text not available from this repository.

Abstract

Staphylococcus aureus and Streptococcus pyogenes, two important human pathogens, target host fibronectin (Fn) in their adhesion to and invasion of host cells1, 2. Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats3 in an unfolded4, 5 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)6, 7 in complex with the module pair 1F12F1. This identifies 1F1- and 2F1-binding motifs in B3 that form additional antiparallel beta-strands on sequential F1 modules—the first example of a tandem beta-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 beta-zippers. This work is a vital step forward in explaining the full mechanism of the integrin-dependent2, 8 FnBP-mediated invasion of host cells.

Item Type: Article
Academic Units: The University of York > Biology (York)
Depositing User: York RAE Import
Date Deposited: 09 Feb 2009 10:06
Last Modified: 09 Feb 2009 10:19
Published Version: http://dx.doi.org/10.1038/nature01589
Status: Published
Publisher: Nature Publishing Group
Identification Number: 10.1038/nature01589
URI: http://eprints.whiterose.ac.uk/id/eprint/7645

Actions (login required)

View Item View Item