Tamilselvam Batcha - Activation of the abundant nuclear factor poly(ADP-ribose) polymerase-1 by Helicobacter pylori

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      Publication Details (including relevant citation   information):

        Proc Natl Acad Sci U S A. 2009 Nov 24;106(47):19998-20003.   Epub 2009 Nov 6.


      Modification of eukaryotic proteins is a powerful strategy used   by pathogenic bacteria to modulate host cells during infection.   Previously, we demonstrated that Helicobacter pylori modify an   unidentified protein within mammalian cell lysates in a manner   consistent with the action of a bacterial ADP-ribosylating toxin.   Here, we identified the modified eukaryotic factor as the   abundant nuclear factor poly(ADP-ribose) polymerase-1 (PARP-1),   which is important in the pathologies of several disease states   typically associated with chronic H. pylori infection. However,   rather than being ADP-ribosylated by an H. pylori toxin, the   intrinsic poly(ADP-ribosyl) polymerase activity of PARP-1 is   activated by a heat- and protease-sensitive H. pylori factor,   resulting in automodification of PARP-1 with polymers of   poly(ADP-ribose) (PAR). Moreover, during infection of gastric   epithelial cells, H. pylori induce intracellular PAR-production   by a PARP-1-dependent mechanism. Activation of PARP-1 by a   pathogenic bacterium represents a previously unrecognized   strategy for modulating host cell signaling during infection.

      Address (URL): http://www.ncbi.nlm.nih.gov/pubmed/19897724