Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-31199
El-Etr, A H; Mueller, A; Tompkins, L S; Falkow, S; Merrell, D S (2004). Phosphorylation-independent effects of CagA during interaction between Helicobacter pylori and T84 polarized monolayers. Journal of Infectious Diseases, 190(8):1516-23.
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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.
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|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
|Dewey Decimal Classification:||570 Life sciences; biology|
|Deposited On:||09 Jul 2010 07:36|
|Last Modified:||27 Nov 2013 22:54|
|Publisher:||University of Chicago Press|
|Additional Information:||© 2004 by the Infectious Diseases Society of America|
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