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We produced defined isogenicHelicobacter pylori ureI mutants to investigate the function of UreI, the product of one of the genes of the urease cluster. The insertion of acat cassette had a strong polar effect on the expression of the downstream urease genes, resulting in very weak urease activity. Urease activity, measured in vitro, was normal in a strain in whichureI was almost completely deleted and replaced with a nonpolar cassette. In contrast to previous reports, we thus found that the product ofureI was not necessary for the synthesis of active urease. Experiments with the mouse-adaptedH. pylori SS1 strain carrying the nonpolarureI deletion showed that UreI is essential forH. pylori survival in vivo and/or colonization of the mouse stomach. The replacement ofureI with the nonpolar cassette strongly reducedH. pylori survival in acidic conditions (1-h incubation in phosphate-buffered saline solution at pH 2.2) in the presence of 10 mM urea. UreI is predicted to be an integral membrane protein and may therefore be involved in a transport process essential forH. pylori survival in vivo.

The Helicobacter pylori UreI Protein Is Not Involved in Urease Activity but Is Essential for Bacterial Survival In Vivo