{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,10]],"date-time":"2025-11-10T07:48:02Z","timestamp":1762760882112},"reference-count":49,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2006,12,1]],"date-time":"2006-12-01T00:00:00Z","timestamp":1164931200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2006,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Helicobacter pylori<\/jats:italic>\n            is dependent upon the production of the highly abundant and active metalloenzyme urease for colonization of the human stomach. Thus,\n            <jats:italic>H. pylori<\/jats:italic>\n            has an absolute requirement for the transition metal nickel, a required cofactor for urease. To investigate the contribution of genes that are factors in this process, microarray analysis comparing the transcriptome of wild-type\n            <jats:italic>H. pylori<\/jats:italic>\n            26695 cultured in brucella broth containing fetal calf serum (BBF) alone or supplemented with 100 \u03bcM NiCl\n            <jats:sub>2<\/jats:sub>\n            suggested that HP1512 is repressed in the presence of 100 \u03bcM supplemental nickel. When measured by comparative real-time quantitative PCR (qPCR), HP1512 transcription was reduced 43-fold relative to the value for the wild type when cultured in BBF supplemented with 10 \u03bcM NiCl\n            <jats:sub>2<\/jats:sub>\n            . When grown in unsupplemented BBF, urease activity of an HP1512::\n            <jats:italic>cat<\/jats:italic>\n            mutant was significantly reduced compared to the wild type, 4.9 \u00b1 0.5 \u03bcmol\/min\/mg of protein (\n            <jats:italic>n<\/jats:italic>\n            = 7) and 17.1 \u00b1 4.9 \u03bcmol\/min\/mg of protein (\n            <jats:italic>n<\/jats:italic>\n            = 13), respectively (\n            <jats:italic>P<\/jats:italic>\n            &lt; 0.0001). In silico analysis of the HP1511-HP1512 (HP1511-1512) intergenic region identified a putative NikR operator upstream of HP1512. Gel shift analysis with purified recombinant NikR verified nickel-dependent binding of\n            <jats:italic>H. pylori<\/jats:italic>\n            NikR to the HP1511-1512 intergenic region. Furthermore, comparative real-time qPCR of four nickel-related genes suggests that mutation of HP1512 results in reduced intracellular nickel concentration relative to wild-type\n            <jats:italic>H. pylori<\/jats:italic>\n            26695. Taken together, these data suggest that HP1512 encodes a NikR-nickel-regulated outer membrane protein.\n          <\/jats:p>","DOI":"10.1128\/iai.01188-06","type":"journal-article","created":{"date-parts":[[2006,11,21]],"date-time":"2006-11-21T01:05:37Z","timestamp":1164071137000},"page":"6811-6820","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":46,"title":["<i>Helicobacter pylori<\/i>\n            HP1512 Is a Nickel-Responsive NikR-Regulated Outer Membrane Protein"],"prefix":"10.1128","volume":"74","author":[{"given":"Gregg S.","family":"Davis","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erika L.","family":"Flannery","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harry L. 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