Amino acid residue Ala-62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis-associated Escherichia coli to collagens.

@article{Pouttu1999AminoAR,
  title={Amino acid residue Ala-62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis-associated Escherichia coli to collagens.},
  author={Riitta Pouttu and T Puustinen and Ritva Virkola and Joerg M. Hacker and Peter L. Klemm and Timo K. Korhonen},
  journal={Molecular microbiology},
  year={1999},
  volume={31 6},
  pages={
          1747-57
        }
}
Adhesion of meningitis-associated Escherichia coli O18acK1H7 to collagens was characterized. The E. coli strain IHE 3034 adhered to type IV and type I collagens but not to type III collagen immobilized on glass. Collagens lack terminal mannosyl units, yet the bacterial adhesion was completely abolished in the presence of alpha-methyl-D-mannoside. A cat cassette was introduced into the filmA gene of IHE 3034, and the resulting mutant strain IHE 3034-2 failed to adhere to collagens. In contrast… CONTINUE READING
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