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Histone modifications are critical in regulating gene expression, cell cycle, cell proliferation, and development. Relatively few studies have investigated whether  Helicobacter pylori , the major cause of human gastric diseases, affects histone modification. We therefore investigated the effects of  H. pylori  infection on histone modifications in a global and promoter-specific manner in gastric epithelial cells. Infection of gastric epithelial cells by wild-type  H. pylori  induced time- and dose-dependent dephosphorylation of histone H3 at serine 10 (H3 Ser10) and decreased acetylation of H3 lysine 23, but had no effects on seven other specific modifications. Different  cag  pathogenicity island (PAI)-containing-clinical isolates showed similar abilities to induce H3 Ser10 dephosphorylation. Mutation of  cagA, vacA , nonphosphorylateable CagA mutant  cagA EPISA  , or disruption of the flagella showed no effects, while deletion of the entire  cag PAI restored the H3 Ser10 phosphorylation to control levels. Analysis of 27  cag PAI mutants indicated that the genes that caused H3 Ser10 dephosphorylation were similar to those that were previously found to induce interleukin-8, irrespective of CagA translocation. This effect was independent of ERK or p38 pathways and type I interferon signaling. Additionally,  c-Jun  and  hsp70  gene expression was associated with this histone modification. These results demonstrate that  H. pylori  alters histone modification and host response via a  cagA -,  vacA -independent, but  cag PAI-dependent mechanisms, which contribute to its persistent infection and pathogenesis.

Helicobacter pylori-Induced Histone Modification, Associated Gene Expression in Gastric Epithelial Cells, and Its Implication in Pathogenesis