Proteins F1 And F2 of Streptococcus Pyogenes

Properties of Fibronectin Binding
  • Emanuel Hanski
  • Joseph Jaffe
  • Vered Ozeri
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 408)


Microbial adhesion to host tissues is the initial event in the pathogenesis of most infections and, as a such, is an attractive target for the development of new antimicrobial therapeutics. Fibronectin (Fn) is a multifunctional glycoprotein present in soluble form in plasma and other body fluids and in insoluble form in extracellular matrices (ECM) and basement membranes (Mosher, 1989; Hynes, 1990). Since it binds specifically to a variety of receptors and substrates molecules, many bacterial pathogens including staphylococci, Escherichia coli, Treponema pallidum, mycobacteria and streptococci have exploited the binding properties of Fn to acquire a mechanism for adherence, colonization and subsequent invasion of host tissues (Patti et al., 1994). Thus, an understanding of the molecular details of bacteria-Fn interactions will not only provide considerable insight to the pathogenesis of many bacterial diseases, but will also serve as a powerful model system for structural and functional analyses of Fn itself.


Respiratory Epithelial Cell Fibronectin Binding Collagen Binding Domain Cell Wall Binding Domain Streptococcus Dysgalactiae 
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  1. Borsi, L., Castellani, P., Balza, E., Siri, A., Pellecchia, C., De Scalzi, F., and Zardi, L. (1986). Large-scale procedure for the purification of fibronectin domains. Anal. Biochem., 155: 335–345.PubMedCrossRefGoogle Scholar
  2. Hanski, E. Horwitz, P. A., and Caparon M. G. (1992). Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect. Immun. 60: 5119–5125.PubMedGoogle Scholar
  3. Hanski, E., and Caparon, M. G. (1992) Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus— Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA. 89: 6172–6176.PubMedCrossRefGoogle Scholar
  4. Hanski, E., Fogg, G., Tovi, A., Okada, N., Burstein, I., and Caparon M. G. (1995). Molecular analysis of Streptococcus pyogenes adhesion. Methods Enzymol. 253: 269–310.PubMedCrossRefGoogle Scholar
  5. Hasty, D. L., Ofek, I., Courtney, H. S., and Doyle R. J. (1992). Multiple adhesins of streptococci. Infect. Immun. 60: 2147–2152.PubMedGoogle Scholar
  6. Hynes, R. O., (1990). Fibronectins. Springer-Verlag, Berlin.Google Scholar
  7. Jaffe, J., Natanson-Yaron, S., Caparon, M. G., and Hanski, E. (1996) Protein F2, a novel fibronectin binding protein from Streptococcus pyogenes, possesses two binding domains. Mol. Microbiol, (in press).Google Scholar
  8. Lindgren, P.-E., McGavin, M., Signäs, C., Guss, B., Gurusiddappa, S., Höök, M., and Lindberg, M. (1993) Two different genes coding for fibronectin-binding proteins from Streptococcus dysgalactiae: the complete nucleotide sequence and characterization of binding domains. Eur. J. Biochem. 214: 819–827.PubMedCrossRefGoogle Scholar
  9. Lindgren, P.-E., Signäs, C., Rantamäki, L., and Lindberg, M. (1994) A fibronectin-binding protein from Streptococcus equisimilis: characterization of the gene and identification of the binding domain. Vet. Microbiol. 41: 235–247.PubMedCrossRefGoogle Scholar
  10. McGavin, M. J., Gurusiddappa, S., Lindgren, P.-E., Lindberg, M., Raucci, G., and Höök, M. (1993). Fibronectin receptors from Streptococcus dysgalactiae Staphylococcus aureus. J. Biol Chem. 268: 23946–23953.Google Scholar
  11. McGavin, M. J., Raucci, G., Gurusiddappa, S., and Höök, M. (1991). Fibronectin binding determinants of the Staphylococcus aureus fibronectin receptor. J. Biol Chem. 266: 8343–8347.PubMedGoogle Scholar
  12. McKeown-Longo, P. J., and Mosher, D. F. (1985). Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts. J. Cell Biol. 100: 364–374.PubMedCrossRefGoogle Scholar
  13. Mosher, D. F., (1989). Fibronectin. Academic Press. New York.Google Scholar
  14. Natanson, S., Sela, S., Moses, A. E., Musser, J. M., Caparon, M. G., and Hanski, E. (1995) Distribution of fibronectin-binding proteins among Group A streptococci of different M-Types. J. Infect. Dis. : 171: 871–878.PubMedCrossRefGoogle Scholar
  15. Navarre, W. W., and Schneewind, O. (1994) Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in Gram-positive bacteria. Mol. Microbiol. 14: 115–121PubMedCrossRefGoogle Scholar
  16. Norgren, M., Caparon, M. G., Scott, J. R. (1989). A method for allelic replacement that uses the conjugative transposon Tn916: deletion of the emm6.1 allele in Streptococcus pyogenes JRS4. Infect. Immun. 57: 3846–3850.PubMedGoogle Scholar
  17. Ozeri, V., Tovi, A., Burstein, I., Natanson-Yaron, S., Caparon, M. G., Yamada, K. M., Akiyama, S. K., Vlodavsky, I., and Hanski, E. (1996) A Two-domain mechanism for Group A Streptococcal adherence through protein F to extracellular matrix. EMBO J., 15: (in press).Google Scholar
  18. Patti, J. M., Allen, B., L., McGavin, M., J., and Höök, M. (1994) MSCRAMM-mediated adherence of microrganisms to host tissues. Annu. Rev. Microbiol. 48: 586–617.CrossRefGoogle Scholar
  19. Schneewind, O. Model, P., and Fischetti, V. A. (1992) Sorting of protein A to the Staphylococcal cell wall. Cell 70: 267–281.PubMedCrossRefGoogle Scholar
  20. Sela, S., Aviv, A., Tovi, A., Burstein, I., Caparon, M. G., and Hanski, E. (1993). Protein F: an adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains. Mol. Microbiol. 10: 1049–1055.PubMedCrossRefGoogle Scholar
  21. Talay, S. R., Ehrenfeld, E., Chhatwal, G. S., and Timmis K. N. (1991) Expression of the fibronectin-binding components of Streptococcus pyogenes in Escherichia coli demonstrates that they are proteins. Mol. Microbiol. 5: 1727–1734.PubMedCrossRefGoogle Scholar
  22. Talay, S. R., Valentin-Weigand, P., Jerlström, P. G., Timmis, K. N., Chhatwal, G. S. (1992). Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect. Immun. 60: 3837–3844.PubMedGoogle Scholar
  23. Talay, S. R., Valentin-Weigand, P., Timmis, K. N., Chhatwal, G. S. (1994) Domain structure and conserved epitopes of Sfb protein, the fibronectin-binding adhesin of Streptococcus pyogenes. Mol. Microbiol. 13: 531–539.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Emanuel Hanski
    • 1
  • Joseph Jaffe
    • 1
  • Vered Ozeri
    • 1
  1. 1.Department of Clinical MicrobiologyThe Hebrew University-Hadassah Medical SchoolJerusalemIsrael

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