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.
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Pouttu, R. et al. (2002). Functional Variability of Type 1 Fimbriae of Escherichia coli. In: Emoődy, L., Pál, T., Hacker, J., Blum-Oehler, G. (eds) Genes and Proteins Underlying Microbial Urinary Tract Virulence. Advances in Experimental Medicine and Biology, vol 485. Springer, Boston, MA. https://doi.org/10.1007/0-306-46840-9_8
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