The outer membrane protein of enteropathogenic Escherichia coli, described as the 'localised adherence factor', is OmpF and probably not involved in adhesion to HEp-2 cells

FEMS Microbiol Lett. 1989 Oct 15;52(3):291-5. doi: 10.1016/0378-1097(89)90213-9.

Abstract

Strains of enteropathogenic Escherichia coli (EPEC) were examined for a factor, described as an outer membrane protein (OMP) of 32 kilodaltons (kDa) and reported to be involved in the adhesion of EPEC to HeLa cells. A comparable OMP of 35 kDa was detected in strains of EPEC, although expression of this protein was not related to the ability of strains to adhere to HEp-2 cells. The 35 kDa OMP was found to be heat-modifiable and peptidoglycan associated, and considered to be the porin protein OmpF.

MeSH terms

  • Bacterial Adhesion / physiology*
  • Bacterial Outer Membrane Proteins / isolation & purification
  • Bacterial Outer Membrane Proteins / metabolism*
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / pathogenicity
  • Escherichia coli / physiology*
  • Humans
  • Immunoblotting
  • Molecular Weight
  • Porins

Substances

  • Bacterial Outer Membrane Proteins
  • Porins