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

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.

• Authors: S Odenbreit, J Püls, B Sedlmaier, E Gerland, W Fischer, R Haas
• Journal: Science (New York, N.Y.) (Science) Vol. 287 Issue 5457 Pg. 1497-500 (Feb 25 2000) ISSN: 0036-8075 [Print] United States
• PMID: 10688800 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

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

Topics

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