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

Nature

Volumn 423, Issue 6936, 2003, Pages 177-181

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

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b TEXAS A AND M HEALTH SCIENCE CENTER   (United States)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN FIBRONECTIN;

ADHESION; CELLS; PATHOLOGY; PROTEINS;

BACTERIA;

BACTERIAL PROTEIN; FIBRONECTIN; FIBRONECTIN BINDING PROTEIN; UNCLASSIFIED DRUG;

BACTERIUM; PATHOGEN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL VIRULENCE; BINDING SITE; CELL INVASION; CONTROLLED STUDY; HOST CELL; HUMAN; NONHUMAN; PATHOGENICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN MOTIF; STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS PYOGENES;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL ADHESION; BINDING SITES; FIBRONECTINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS PYOGENES;

BACTERIA (MICROORGANISMS); POSIBACTERIA; STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS DYSGALACTIAE; STREPTOCOCCUS PYOGENES;

EID: 0037653702     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01589     Document Type: Article

References (30)

1. Peacock, S. I., Foster, T. J., Cameron, B. I. & Berendt, A. R. Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells. Microbiology 145, 3477-3486 (1999).
2. Ozeri, V., Rosenshine, I., Mosher, D. F., Fässler, R. & Hanski, E. Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1. Mol. Microbial. 30, 625-637 (1998).
3. Patti, J. M., Allen, B. L., McGavin, M. J. & Höök, M. MSCRAMM-mediated adherence of microorganisms to host tissues. Annu. Rev. Microbiol. 48, 585-617 (1994).
4. House-Pompeo, K., Xu, Y., Joh, D., Speziale, P. & Höök, M. Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. J. Biol. Chem. 271, 1379-1384 (1996).
5. Penkett, C. J. et al. Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus. Biochemistry 37, 17054-17067 (1998).
6. McGavin, M. J. et al. Fibronectin receptors from Streptococcus dysgalactiae and Staphylococcus aureus-involvement of conserved residues in ligand binding. J. Biol. Chem. 268, 23946-23953 (1993).
7. Joh, D., Speziale, P., Gurusiddappa, S., Manor, J. & Höök, M. Multiple specificities of the staphylococcal and streptococcal fibronectin-binding microbial surface components recognizing adhesive matrix molecules. Eur. J. Biochem. 258, 897-905 (1998).
8. 1. Cell. Microbiol. 1, 101-117 (1999).
9. Knodler, L. A., Celli, J. & Finlay, B. B. Pathogenic trickery: Deception of host cell processes. Nature Rev. Mol. Cell Biol. 2, 578-588 (2001).
10. Ing, M. B., Baddour, L. M. & Bayers, S. A. in The Staphylococci in Human Disease (eds Crossley, K. B. & Archer, G. L.) 331-354 (Churchill Livingstone, New York, 1997).
11. Greene, C. et al. Adhesion properties of mutants of Staphylococcus aureus defective in fibronectin-binding proteins and studies on the expression of fnb genes. Mol. Microbiol. 17, 1143-1152 (1995).
12. Potts, J. R., Bright, J. R., Bolton, D., Pickford, A. R. & Campbell, I. D. Solution structure of the N-terminal F1 module pair from human fibronectin. Biochemistry 38, 8304-8312 (1999).
13. Jaffe, J., Natanson-Yaron, S., Caparon, M. G. & Hanski, E. Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains. Mol. Microbiol. 21, 373-384 (1996).
14. 5F1 module pair of human fibronectin using heteronuclear NMR spectroscopy. Biochemistry 39, 2887-2893 (2000).
15. Talay, S. R., Valentin-Weigand, P., Jerlstrom, P. G., Timmis, K. N. & Chhatwal, G. S. Fibronectin-binding protein of Streptococcus pyogenes - sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect. Immun. 60, 3837-3844 (1992).
16. Signäs, C. et al. Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus - use of this peptide sequence in the synthesis of biologically-active peptides. Proc. Natl Acad Sci. USA 86, 699-703 (1989).
17. Schwarz-Linek, U. et al. Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N-terminal F1 module pair of human fibronectin involves both modules. FEBS Lett. 497, 137-140 (2001).
18. Huff, S., Matsuka, Y. V., McGavin, M. J. & Ingham, K. C. Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy. J. Biol. Chem. 269, 15563-15570 (1994).
19. Massey, R. C. et al. Fibronectin-binding protein A of Staphylococcus aureus has multiple, substituting, binding regions that mediate adherence to fibronectin and invasion of endothelial cells. Cell. Microbiol. 3, 839-851 (2001).
20. Talay, S. R. et al. Co-operative binding of human fibronectin to SfbI protein triggers streptococcal invasion into respiratory epithelial cells. Cell. Microbial. 2, 521-535 (2000).
21. Derrick, J. P. & Wigley, D. B. Crystal structure of a streptococcal protein-G domain bound to an Fab fragment. Nature 359, 752-754 (1992).
22. 2F2 fragment from human fibronectin enhances gelatin binding. EMBO J. 20, 1519-1529 (2001).
23. Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (1999).
24. Brünger, A. T. X-PLOR (Version 3.1) A System for X-ray Crystallography and NMR (Yale University, New Haven, Connecticut, 1992).
25. Sass, H. J., Musco, G., Stahl, S. J., Wingfield, P. T. & Grzesiek, S. Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes. J. Biomol. NMR 18, 303-309 (2000).
26. Ottiger, M., Delaglio, F. & Bax, A. Measurement of J and dipolar couplings from simplified twodimensional NMR spectra. J. Magn. Reson. 131, 373-378 (1998).
27. 1F2 module pair: A N-15 NMR relaxation study. J. Biomol. NMR 17, 203-214 (2000).
28. Tjandra, N., Garrett, D. S., Gronenborn, A. M., Bax, A. & Clore, G. M. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nature Struct. Biol. 4, 443-449 (1997).
29. Wishart, D. S., Sykes, B. D. & Richards, F. M. The chemical-shift index - a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651 (1992).
30. Talay, S. R., Valentin-Weigand, P., Timmis, K. N. & Chhatwal, G. S. Domain-structure and conserved epitopes of Sfb protein, the fibronectin-binding adhesin of Streptococcus pyogenes. Mol. Microbiol. 13, 531-539 (1994).