Phosphorylation-Independent Effects of CagA during Interaction between Helicobacter pylori and T84 Polarized Monolayers

To extend our knowledge of host-cell targets of Helicobacter pylori, we characterized the interaction between H. pylori and human T84 epithelial cell polarized monolayers. Transcriptional analysis by use of human microarrays and a panel of isogenic H. pylori mutants revealed distinct responses to in...

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Bibliographic Details
Published in:The Journal of infectious diseases 2004-10, Vol.190 (8), p.1516-1523
Main Authors: El-Etr, Sahar H., Mueller, Anne, Tompkins, Lucy S., Falkow, Stanley, Merrell, D. Scott
Format: Article
Language:English
Subjects:
Antigens, Bacterial - genetics
Antigens, Bacterial - metabolism
Apoptosis
Bacteria
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Cadherins
Cell Line, Tumor - microbiology
Cell Line, Tumor - physiology
Cell lines
Cell Polarity
Cell Shape
Epithelial cells
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
Genes
Helicobacter pylori
Helicobacter pylori - genetics
Helicobacter pylori - metabolism
Helicobacter pylori - pathogenicity
Humans
Infections
Infectious diseases
Intercellular junctions
Medical sciences
Microbiology
Microscopy, Confocal
Miscellaneous
Mutation
Oligonucleotide Array Sequence Analysis
Phosphorylation
Signal Transduction
Virulence Factors - genetics
Virulence Factors - metabolism
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Summary:To extend our knowledge of host-cell targets of Helicobacter pylori, we characterized the interaction between H. pylori and human T84 epithelial cell polarized monolayers. Transcriptional analysis by use of human microarrays and a panel of isogenic H. pylori mutants revealed distinct responses to infection. Of the 670 genes whose expression changed, most (92%) required the cag pathogenicity island (PAI). Although altered expression of many genes was dependent on CagA (80% of the PAI-dependent genes), expression of >30% of these host genes occurred independent of the phosphorylation state of the CagA protein. Similarly, we found that injected CagA localized to the apical surface of cells and showed preferential accumulation at the apical junctions in a phosphorylation-independent manner. These data suggest the presence of distinct functional domains within the CagA protein that play essential roles in protein targeting and alteration of host-cell signaling pathways.
ISSN:0022-1899
1537-6613
DOI:10.1086/424526