Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion

Science. 2000 Feb 25;287(5457):1497-500. doi: 10.1126/science.287.5457.1497.

Abstract

The Gram-negative bacterium Helicobacter pylori is a causative agent of gastritis and peptic ulcer disease in humans. Strains producing the CagA antigen (cagA(+)) induce strong gastric inflammation and are strongly associated with gastric adenocarcinoma and MALT lymphoma. We show here that such strains translocate the bacterial protein CagA into gastric epithelial cells by a type IV secretion system, encoded by the cag pathogenicity island. CagA is tyrosine-phosphorylated and induces changes in the tyrosine phosphorylation state of distinct cellular proteins. Modulation of host cells by bacterial protein translocation adds a new dimension to the chronic Helicobacter infection with yet unknown consequences.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Antigens, Bacterial*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Biological Transport
  • Enzyme Inhibitors / pharmacology
  • Epithelial Cells / metabolism
  • Epithelial Cells / microbiology
  • Fluorescent Antibody Technique
  • Gastric Mucosa / metabolism*
  • Gastric Mucosa / microbiology*
  • Genes, Bacterial
  • Genetic Complementation Test
  • Genistein / pharmacology
  • Helicobacter pylori / genetics
  • Helicobacter pylori / metabolism*
  • Helicobacter pylori / pathogenicity
  • Humans
  • Mutation
  • Phosphorylation
  • Phosphotyrosine / metabolism
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / metabolism
  • Staurosporine / pharmacology
  • Tumor Cells, Cultured
  • Virulence

Substances

  • Antigens, Bacterial
  • Bacterial Proteins
  • Enzyme Inhibitors
  • cagA protein, Helicobacter pylori
  • Phosphotyrosine
  • Genistein
  • Protein-Tyrosine Kinases
  • Staurosporine