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Background   Helicobacter pylori  ( H. pylori ) infection affects cell survival signaling pathways including cell apoptosis and proliferation, which are considered risk factors for the development of gastric cancer when unregulated. In the present study, we investigated the effect of  H. pylori  infection on the phosphorylation state of 3-phosphoinositide-dependent kinase-1 (PDK-1), a master kinase that regulates phosphorylation of Akt (also known as protein kinase B, PKB) and cell survival.Methods  The activity of PDK-1 was examined in human gastric epithelial cells incubated in the presence or absence of different  H. pylori  strains. In addition, the role of  H. pylori  type IV secretion system and the mechanism of  H. pylori  effect on PDK-1 activity was examined.    Results  In the presence of  H. pylori , phosphorylation of the activation loop (serine 241) PDK-1 was rapidly lost suggesting that dephosphorylation of PDK-1 is a target for  H. pylori  to modulate cell survival. The extent of dephosphorylation was strain dependent with  H. pylori  60190 being the most effective.  H. pylori  infection of gastric epithelial cells resulted in altered phosphorylation and degradation of Akt, suggesting that PDK-1 dephosphorylation affects cell survival pathways and thereby may contribute to disease pathogenesis.    Conclusion  We propose that dephosphorylation of PDK-1 and the resulting changes to Akt phosphorylation is one of the mechanisms by which infection with  H. pylori  alter the balance between apoptosis and cell proliferation and identify a host molecular mechanism regulated by  H. pylori  that ultimately contributes to carcinogenesis. Our studies therefore provide insights into one of the mechanisms by which  H. pylori  infection contributes to gastric cancer by regulating the activity of a cell survival signaling pathway.

Helicobacter pylori modulates host cell survival regulation through the serine-threonine kinase, 3-phosphoinositide dependent kinase 1 (PDK-1)