Organisation and in vitro expression of esp genes of the LEE (locus of enterocyte effacement) of bovine enteropathogenic and enterohemorrhagic Escherichia coli

Vet Microbiol. 2001 Nov 26;83(3):275-86. doi: 10.1016/s0378-1135(01)00418-7.

Abstract

Enteropathogenic (EPEC) and enterohemorrhagic (EHEC) Escherichia coli infections are characterised by the formation of attaching and effacing (AE) lesions on intestinal epithelial cells. Secretion of extracellular proteins (EspA, EspB, and EspD) via a type III secretion apparatus is necessary for the formation of the AE lesions by human EPEC. In this study, we show that bovine EPEC and EHEC are also able to secrete polypeptides homologous to the already described Esp proteins, most probably via a type III secretion system. Bovine EPEC and EHEC strains present two different secretion profiles of Esp proteins which correlate to the pathotypes of the esp genes as determined by PCR. We also demonstrate that genes encoding secreted proteins, present in the LEE of two bovine strains, are organised in the same way as in the human EPEC strain E2348/69.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism
  • Base Sequence
  • Cattle
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel / veterinary
  • Enterocytes / microbiology
  • Enterocytes / pathology
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Infections / microbiology*
  • Escherichia coli Infections / pathology
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial
  • Immunoblotting / veterinary
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Polymerase Chain Reaction / veterinary

Substances

  • Bacterial Outer Membrane Proteins
  • EaeB protein, E coli
  • Escherichia coli Proteins
  • EspA protein, E coli
  • EspD protein, E coli
  • Membrane Proteins