A novel proline-rich protein, EspF, is secreted from enteropathogenic Escherichia coli via the type III export pathway

FEMS Microbiol Lett. 1998 Sep 1;166(1):71-8. doi: 10.1111/j.1574-6968.1998.tb13185.x.

Abstract

Enteropathogenic Escherichia coli (EPEC) cause a characteristic attaching and effacing (A/E) lesion in intestinal epithelial cells that is associated with the expression and export of specific bacterial proteins via a type III secretion pathway. These effector proteins and components of the type III export apparatus are encoded on a pathogenicity island known as the locus of enterocyte effacement (LEE). In this study, we describe a proline-rich protein, EspF, encoded by the LEE that is secreted by the EPEC type III secretion apparatus. Whereas an espF deletion mutant does not synthesize or secrete EspF, surprisingly it retains the ability to induce host signaling events, perform A/E activities, and invade host epithelial cells. Although these results do not indicate on obvious role for EspF in the formation of A/E lesions nor in the invasion of epithelial cells, they do not preclude a role played by EspF in other aspects of EPEC pathogenesis.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Cell Line
  • DNA Primers / genetics
  • Escherichia coli / genetics
  • Escherichia coli / pathogenicity*
  • Escherichia coli / physiology*
  • Genes, Bacterial
  • Humans
  • Intestines / microbiology
  • Open Reading Frames
  • Polymerase Chain Reaction
  • Proline / chemistry
  • Virulence / genetics
  • Virulence / physiology

Substances

  • Bacterial Proteins
  • DNA Primers
  • Proline