H. pylori-induced metabolic changes in gastric epithelial cells

In order to survive and cope with the acidic conditions of the stomach, H. pylori possesses a number of metabolic enzymes, which were shown to also effect host cells. For instance, H. pylori gamma-glutamyltranspeptidase (gGT) breaks down glutathione and glutamine to generate glutamate, which alters host cell glutamine metabolism and redox status. H. pylori arginase inhibits nitric oxide production by eukaryotic cells by consuming l-arginine, which prevents macrophage induced killing of H. pylori. H. pylori urease is a very potent enzyme consuming local urea and producing ammonia, which is used for H. pylori diagnosis. Finally, H. pylori also induces arginase II, generating ornithine, and ornithine decarboxylase (ODC), generating polyamines, especially spermine. Although it is clear that products of bacterial metabolism affect host cells, the global metabolomic changes induced by H. pylori have not yet been completely elucidated. In this project, we aim to systematically analyze metabolome alterations induced by H. pylori in murine models of infection as well as in human gastric biopsies.