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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)

Abstract

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.

Keywords

Respiratory Epithelial Cell Fibronectin Binding Collagen Binding Domain Cell Wall Binding Domain Streptococcus Dysgalactiae 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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