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Functional Variability of Type 1 Fimbriae of Escherichia coli

  • Riitta Pouttu
  • Terhi Puustinen
  • Maini Kukkonen
  • Ritva Virkola
  • Minni Laurila
  • Jörg Hacker
  • Per Klemm
  • Timo K. Korhonen
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 485)

Conclusions

Type 1 fimbriae and the FimH-adhesins of E. coli differ in adhesive functions: those of a meningitis isolate IHE3034 mediate adhesion to collagens whereas those of an avirulent K-12 strain PC31 do not. Amino acid residue Alanine-62 in the FimH is critical for the collagen binding ability: substitution of Ala62 of IHE3034 FimH into serine abolishes collagen adhrence whereas substitution of Ser62 of PC31 FimH into alanine restores the binding.

Fimbriae also are targets for binding of functionally important host proteins. Type 1 fimbriae of E. coli differ in plasminogen receptor function: those of the strain IHE3034 mediate plasminogen receptor function while those of the strain PC31 do not. The Fim-protein(s)and the critical amino acids involved in plasminogen receptor function remain to be identified.

Keywords

Plasminogen Activation Yersinia Enterocolitica Critical Amino Acid Functional Variability Amino Acid Sequence Difference 
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

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Riitta Pouttu
    • 1
  • Terhi Puustinen
    • 1
  • Maini Kukkonen
    • 1
  • Ritva Virkola
    • 1
  • Minni Laurila
    • 1
  • Jörg Hacker
    • 2
  • Per Klemm
    • 3
  • Timo K. Korhonen
    • 1
  1. 1.Division of General Microbiology, Department of BiosciencesUniversity of HelsinkiFinland
  2. 2.Institut für Molekulare Infektions biologieWürzburgGermany
  3. 3.Department of MicrobiologyTechnical University of DenmarkLyngbyDenmark

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