Mar 10, 2001

Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function

The Journal of Clinical Investigation
B P McNamaraGail A Hecht

Abstract

The mechanisms by which enteropathogenic Escherichia coli (EPEC), an important cause of diarrhea among infants in developing countries, induce symptoms are not defined. EPEC have a type III secretion system required for characteristic attaching and effacing changes that modify the cytoskeleton and apical surface of host cells. Infection of polarized intestinal epithelial cell monolayers by EPEC leads to a loss of transepithelial electrical resistance, which also requires the type III secretion system. We demonstrate here that EspF, a protein that is secreted by EPEC via the type III secretion system, is not required for quantitatively and qualitatively typical attaching and effacing lesion formation in intestinal epithelial cells. However, EspF is required in a dose-dependent fashion for the loss of transepithelial electrical resistance, for increased monolayer permeability, and for redistribution of the tight junction-associated protein occludin. Furthermore, the analysis of EPEC strains expressing EspF-adenylate cyclase fusion proteins indicates that EspF is translocated via the type III secretion system to the cytoplasm of host cells, a result confirmed by immunofluorescence microscopy. These studies suggest a novel role for...Continue Reading

Mentioned in this Paper

Ohmic Resistance
Bacterial Proteins
Occludin
(L)-Mannitol
Alkalescens-Dispar Group
Squamous Transitional Epithelial Cell Count
Tight Junction Assembly Pathway
Immunofluorescence Microscopy
Structure of Intestinal Gland
Staphylococcal Protein A

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