{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T20:20:29Z","timestamp":1793132429108,"version":"4.5.0"},"reference-count":44,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2002,12,11]],"date-time":"2002-12-11T00:00:00Z","timestamp":1039564800000},"content-version":"vor","delay-in-days":893,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2000,7]]},"abstract":"<jats:p>The genome sequence of <jats:italic>Helicobacter pylori<\/jats:italic> suggests that this bacterium possesses several Fe acquisition systems, including both Fe<jats:sup>2+<\/jats:sup>\u2010 and Fe<jats:sup>3+<\/jats:sup>\u2010citrate transporters. The role of these transporters was investigated by generating insertion mutants in <jats:italic>feoB<\/jats:italic>, <jats:italic>tonB<\/jats:italic>, <jats:italic>fecA1<\/jats:italic> and <jats:italic>fecDE<\/jats:italic>. Fe transport in the <jats:italic>feoB<\/jats:italic> mutant was \u2248\u200a10\u2010fold lower than in the wild type (with 0.5\u2003\u03bcM Fe), irrespective of whether Fe was supplied in the Fe<jats:sup>2+<\/jats:sup> or Fe<jats:sup>3+<\/jats:sup> form. In contrast, transport rates were unaffected by the other mutations. Complementation of the <jats:italic>feoB<\/jats:italic> mutation fully restored both Fe<jats:sup>2+<\/jats:sup> and Fe<jats:sup>3+<\/jats:sup> transport. The growth inhibition exhibited by the <jats:italic>feoB<\/jats:italic> mutant in Fe\u2010deficient media was relieved by human holo\u2010transferrin, holo\u2010lactoferrin and Fe<jats:sup>3+<\/jats:sup>\u2010dicitrate, but not by FeSO<jats:sub>4<\/jats:sub>. The <jats:italic>feoB<\/jats:italic> mutant had less cellular Fe and was more sensitive to growth inhibition by transition metals in comparison with the wild type. Biphasic kinetics of Fe<jats:sup>2+<\/jats:sup> transport in the wild type suggested the presence of high\u2010 and low\u2010affinity uptake systems. The high\u2010affinity system (apparent <jats:bold>K<\/jats:bold><jats:sub>s<\/jats:sub>\u2003=\u20030.54\u2003\u03bcM) is absent in the <jats:italic>feoB<\/jats:italic> mutant. Transport via FeoB is highly specific for Fe<jats:sup>2+<\/jats:sup> and was inhibited by FCCP, DCCD and vanadate, indicating an active process energized by ATP. Ferrozine inhibition of Fe<jats:sup>2+<\/jats:sup> and Fe<jats:sup>3+<\/jats:sup> uptake implied the concerted involvement of both an Fe<jats:sup>3+<\/jats:sup> reductase and FeoB in the uptake of Fe supplied as Fe<jats:sup>3+<\/jats:sup>. Taken together, the results are consistent with FeoB\u2010mediated Fe<jats:sup>2+<\/jats:sup> uptake being a major pathway for <jats:bold><jats:italic>H. pylori<\/jats:italic><\/jats:bold> Fe acquisition. <jats:bold><jats:italic>feoB<\/jats:italic><\/jats:bold> mutants were unable to colonize the gastric mucosa of mice, indicating that FeoB makes an important contribution to Fe acquisition by <jats:bold><jats:italic>H. pylori<\/jats:italic><\/jats:bold> in the low\u2010pH, low\u2010O<jats:sub>2<\/jats:sub> environment of the stomach.<\/jats:p>","DOI":"10.1046\/j.1365-2958.2000.01987.x","type":"journal-article","created":{"date-parts":[[2003,3,12]],"date-time":"2003-03-12T11:32:12Z","timestamp":1047468732000},"page":"274-286","source":"Crossref","is-referenced-by-count":244,"title":["Iron acquisition and virulence in <i>Helicobacter pylori<\/i>: a major role for FeoB, a high\u2010affinity ferrous iron 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