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The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence.
Title | The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence. |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Velayudhan, J, Castor, M, Richardson, A, Main-Hester, KL, Fang, FC |
Journal | Mol Microbiol |
Volume | 63 |
Issue | 5 |
Pagination | 1495-507 |
Date Published | 2007 Mar |
ISSN | 0950-382X |
Keywords | Aconitate Hydratase, Animals, Anti-Bacterial Agents, Bacterial Proteins, Cytoplasm, Female, Ferritins, Gene Deletion, Gene Expression Regulation, Bacterial, Hydrogen Peroxide, Iron, Liver, Mice, Mice, Inbred C3H, Oxidative Stress, Repressor Proteins, RNA, Bacterial, RNA, Messenger, Salmonella Infections, Animal, Salmonella typhimurium, Survival, Virulence |
Abstract | Ferritins are ubiquitous iron (Fe) storage proteins that play a fundamental role in cellular Fe homeostasis. The enteric pathogen Salmonella enterica serovar Typhimurium possesses four ferritins: bacterioferritin, ferritin A, ferritin B and Dps. The haem-containing bacterioferritin (Bfr) accounts for the majority of stored Fe, followed by ferritin A (FtnA). Inactivation of bfr elevates the intracellular free Fe concentration and enhances susceptibility to H2O2 stress. The DNA-binding Dps protein provides protection from oxidative damage without affecting the steady-state intracellular free Fe concentration. FtnB appears to be particularly important for the repair of oxidatively damaged Fe-sulphur clusters of aconitase and, in contrast to Bfr and FtnA, is required for Salmonella virulence in mice. Moreover, ftnB and dps are repressed by the Fe-responsive regulator Fur and induced under conditions of Fe limitation, whereas bfr and ftnA are maximally expressed when Fe is abundant. The absence of a conserved ferroxidase domain and the potentiation of oxidative stress by FtnB in some strains lacking Dps suggest that FtnB serves as a facile cellular reservoir of Fe2+. |
DOI | 10.1111/j.1365-2958.2007.05600.x |
Alternate Journal | Mol. Microbiol. |
PubMed ID | 17302823 |
Grant List | AI39557 / AI / NIAID NIH HHS / United States AI50660 / AI / NIAID NIH HHS / United States P30 ES07033 / ES / NIEHS NIH HHS / United States |