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Bacterial Gastroenteritis01:18

Bacterial Gastroenteritis

Bacterial gastroenteritis, characterized by diarrhea, abdominal cramps, and vomiting, is often caused by ingestion of contaminated food or water and is frequently associated with pathogenic Escherichia coli strains. These microbes exploit two principal mechanisms to inflict disease.Shiga toxin–producing E. coli, also referred to as STEC—notably O157:H7—release Shiga toxins that target ribosomes, blocking protein synthesis. The B subunit of the toxin binds the host glycolipid receptor...
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Assessment of Intestinal Transcytosis of Neonatal Escherichia coli Bacteremia Isolates
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Assessment of Intestinal Transcytosis of Neonatal Escherichia coli Bacteremia Isolates

Published on: February 17, 2023

Tight junctions and enteropathogenic E. coli.

Andrew W Weflen1, Neal M Alto, Gail A Hecht

  • 1Department of Medicine, Section of Digestive Diseases and Nutrition, University of Illinois at Chicago, Chicago, Illinois 60612, USA.

Annals of the New York Academy of Sciences
|June 23, 2009
PubMed
Summary
This summary is machine-generated.

Enteropathogenic E. coli (EPEC) disrupts intestinal cells using the EspF protein. EspF hijacks host cell endocytosis by interacting with SNX9 and N-WASP, contributing to infant diarrhea.

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Area of Science:

  • Microbiology
  • Cell Biology
  • Pathogenesis

Background:

  • Enteropathogenic E. coli (EPEC) causes severe infantile diarrhea, a major global health issue.
  • EPEC utilizes type three secretion systems to deliver virulence effectors into host intestinal cells, disrupting cellular functions and causing disease.

Purpose of the Study:

  • To investigate the mechanism by which the EPEC effector protein EspF disrupts host intestinal epithelial cells.
  • To identify protein-protein interactions of EspF involved in its pathogenic activity.

Main Methods:

  • In vitro protein interaction assays to study EspF binding to host factors.
  • Biochemical assays to assess the impact of EspF-protein interactions on actin polymerization and endocytosis.

Main Results:

  • EspF interacts with endocytic regulators sorting nexin 9 (SNX9) and N-WASP through distinct binding sites.
  • EspF interaction with SNX9 alters SNX9's endocytic activity, inducing tubular vesicle formation.
  • EspF interactions promote actin polymerization in vitro.

Conclusions:

  • EspF utilizes SNX9 and potentially N-WASP to hijack host cell endocytic pathways.
  • This hijacking of endocytosis by EspF is a key mechanism in EPEC pathogenesis, leading to disease phenotypes.