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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Antigens, Bacterial*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Biological Transport
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Enzyme Inhibitors / pharmacology
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Epithelial Cells / metabolism
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Epithelial Cells / microbiology
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Fluorescent Antibody Technique
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Gastric Mucosa / metabolism*
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Gastric Mucosa / microbiology*
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Genes, Bacterial
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Genetic Complementation Test
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Genistein / pharmacology
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Helicobacter pylori / genetics
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Helicobacter pylori / metabolism*
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Helicobacter pylori / pathogenicity
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Humans
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Mutation
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Phosphorylation
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Phosphotyrosine / metabolism
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Protein-Tyrosine Kinases / antagonists & inhibitors
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Protein-Tyrosine Kinases / metabolism
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Staurosporine / pharmacology
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Tumor Cells, Cultured
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Virulence
Substances
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Antigens, Bacterial
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Bacterial Proteins
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Enzyme Inhibitors
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cagA protein, Helicobacter pylori
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Phosphotyrosine
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Genistein
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Protein-Tyrosine Kinases
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Staurosporine