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One of the host defense mechanisms that\n                    <jats:italic>Salmonella<\/jats:italic>\n                    encounters during infection is the production of reactive oxygen species by the phagocyte NADPH oxidase. Among them, hydrogen peroxide (H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    ) can diffuse across bacterial membranes and damage biomolecules. Genome analysis allowed us to identify five genes encoding H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    degrading enzymes: three catalases (KatE, KatG, and KatN) and two alkyl hydroperoxide reductases (AhpC and TsaA). Inactivation of the five cognate structural genes yielded the HpxF\n                    <jats:sup>\u2212<\/jats:sup>\n                    mutant, which exhibited a high sensitivity to exogenous H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    and a severe survival defect within macrophages. When the phagocyte NADPH oxidase was inhibited, its proliferation index increased 3.7-fold. Moreover, the overexpression of\n                    <jats:italic>katG<\/jats:italic>\n                    or\n                    <jats:italic>tsaA<\/jats:italic>\n                    in the HpxF\n                    <jats:sup>\u2212<\/jats:sup>\n                    background was sufficient to confer a proliferation index similar to that of the wild type in macrophages and a resistance to millimolar H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    in rich medium. The HpxF\n                    <jats:sup>\u2212<\/jats:sup>\n                    mutant also showed an attenuated virulence in a mouse model. These data indicate that\n                    <jats:italic>Salmonella<\/jats:italic>\n                    catalases and alkyl hydroperoxide reductases are required to degrade H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    and contribute to the virulence. This enzymatic redundancy highlights the evolutionary strategies developed by bacterial pathogens to survive within hostile environments.\n                  <\/jats:p>","DOI":"10.1128\/jb.00144-09","type":"journal-article","created":{"date-parts":[[2009,5,15]],"date-time":"2009-05-15T21:09:37Z","timestamp":1242421777000},"page":"4605-4614","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":185,"title":["Redundant Hydrogen Peroxide Scavengers Contribute to\n                    <i>Salmonella<\/i>\n                    Virulence and Oxidative Stress Resistance"],"prefix":"10.1128","volume":"191","author":[{"given":"Magali","family":"He\u0301brard","sequence":"first","affiliation":[{"name":"CNRS, Laboratoire de Chimie Bacte\u0301rienne (UPR 9043), Institut de Microbiologie de la Me\u0301diterrane\u0301e, IFR 88, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France"},{"name":"Aix-Marseille University, Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie P. M.","family":"Viala","sequence":"additional","affiliation":[{"name":"CNRS, Laboratoire de Chimie Bacte\u0301rienne (UPR 9043), Institut de Microbiologie de la Me\u0301diterrane\u0301e, IFR 88, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France"},{"name":"Aix-Marseille University, Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ste\u0301phane","family":"Me\u0301resse","sequence":"additional","affiliation":[{"name":"Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Univ. Me\u0301diterrane\u0301e, Parc Scientifique de Luminy, Case 906, 13288 Marseille Cedex 9, France"},{"name":"Aix-Marseille University, Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fre\u0301de\u0301ric","family":"Barras","sequence":"additional","affiliation":[{"name":"CNRS, Laboratoire de Chimie Bacte\u0301rienne (UPR 9043), Institut de Microbiologie de la Me\u0301diterrane\u0301e, IFR 88, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France"},{"name":"Aix-Marseille University, Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Aussel","sequence":"additional","affiliation":[{"name":"CNRS, Laboratoire de Chimie Bacte\u0301rienne (UPR 9043), Institut de Microbiologie de la Me\u0301diterrane\u0301e, IFR 88, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France"},{"name":"Aix-Marseille University, Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1182\/blood.V93.5.1464","volume":"93","year":"1999","unstructured":"Babior, B. 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