Function and Molecular Architecture of E.Coli Adhesins

  • Heinz Hoschützky
  • Thomas Bühler
  • Ralph Ahrens
  • Klaus Jann
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 58)


The pathogenicity of E.coli has been ascribed to different virulence factors such as toxins, cytolysins, serum resistance, O- and K-antigens or adhesive properties. The adherence of the bacteria to epithelial surfaces — e.g. cell membranes and/or mucosal surfaces — is an important early event in host parasite interactions leading to bacterial colonization and infection (1). The term adhesion as used in this context describes a specific interaction of recognition proteins attached to the bacterial surface with complex carbohydrate moieties of glycoproteins and/or glycolipids on mammalian cells. These recognition proteins (also termed adhesins, hemagglutinins or lectins) may have different appearances in the electron microscope. Structures that can be demonstrated directly by negative staining procedures have been termed fimbriae or pili (rigid, 5–7 nm diameter) and fibrillae (flexible, 2–3 nm diameter). Nonfimbrial adhesive structures can only be visualized after stabilization with specific antibodies and then have a capsule like appearance (2).


Adhesive Property Molecular Architecture Receptor Binding Site Minor Protein Host Parasite Interaction 
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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Heinz Hoschützky
    • 1
  • Thomas Bühler
    • 1
  • Ralph Ahrens
    • 1
  • Klaus Jann
    • 1
  1. 1.Max-Planck-Institute for ImmunobiologyFreiburgGermany

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