Characterization of the adhesin of Escherichia coli F18 fimbriae

Infect Immun. 2001 Dec;69(12):7941-5. doi: 10.1128/IAI.69.12.7941-7945.2001.

Abstract

Previous research has suggested that the adhesin encoded by the F18 fimbrial operon in Escherichia coli is either the FedE or FedF protein. In this work, we show that anti-FedF antibodies, unlike anti-FedE serum, were able to inhibit E. coli adhesion to porcine enterocytes. Moreover, specific adhesion to enterocytes was shown with purified FedF-maltose binding protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial*
  • Animals
  • Antibodies, Bacterial
  • Bacterial Adhesion
  • Cloning, Molecular
  • Enterocytes / microbiology
  • Escherichia coli / genetics
  • Escherichia coli / pathogenicity*
  • Escherichia coli Proteins / immunology
  • Escherichia coli Proteins / physiology*
  • Fimbriae, Bacterial / chemistry*
  • Fimbriae, Bacterial / genetics
  • Fluorescent Antibody Technique, Indirect
  • Ileum / cytology
  • Ileum / microbiology
  • Jejunum / cytology
  • Jejunum / microbiology
  • Molecular Sequence Data
  • Recombinant Fusion Proteins
  • Swine

Substances

  • Adhesins, Bacterial
  • Antibodies, Bacterial
  • Escherichia coli Proteins
  • FedF protein, E coli
  • Recombinant Fusion Proteins

Associated data

  • GENBANK/AF222806