Iron Incorporation in Streptococcus suis Dps-like Peroxide Resistance Protein Dpr Requires Mobility in the Ferroxidase Center and Leads to the Formation of a Ferrihydrite-like Core

Kauko, Anni; Pulliainen, Arto T.; Haataja, Sauli; Meyer‐Klaucke, Wolfram; Finne, Jukka; Papageorgiou, Anastassios C.

doi:10.1016/j.jmb.2006.08.061

Cited by 34 publications

(36 citation statements)

References 59 publications

(101 reference statements)

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“…Dps-like proteins in intracellular bacteria, such as ferritinlike Dps in S. enterica serovar Typhimurium and Fri in L. monocytogenes, are important virulence factors (14,26). The iron-binding activities of Dps-like proteins are found in most bacteria (17,21,30,35,46), but the DNA-binding activities are present in only some bacteria, like H. pylori, Mycobacterium smegmatis, and Porphyromonas gingivalis (10,13,35,41). Most of the dpr homologues are required for resistance to hydrogen peroxide (35).…”

Section: Discussionmentioning

confidence: 99%

An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus pyogenes against Multiple Stresses

Tsou

Chiang-Ni

Lin³

et al. 2008

Infect Immun

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Streptococcus pyogenes does not produce catalase, but it can grow in aerobic environments and survive in the presence of peroxide. One of the stress proteins of this organism, peroxide resistance protein (Dpr), has been studied to examine its role in resistance to hydrogen peroxide, but the protective mechanism of Dpr is not clear. The aim of this study was to characterize the dpr gene and its role in dealing with different stresses. A dpr deletion mutant was constructed by double-crossover mutagenesis. The dpr mutant was more sensitive to H 2 O 2 , and complementation could partially restore the defect in the mutant. Pretreatment with the iron chelator deferoxamine mesylate rescued the survival activity of the mutant under oxidative stress conditions. The dpr mutant also showed a low survival rate in the long-term stationary phase, when it was treated with extreme acids, and under alkaline pH conditions compared to the wild-type strain. The growth of the dpr mutant was slower than that of the wild-type strain in iron-limiting conditions. The dpr mutant showed high sensitivity to iron and zinc but not to manganese, copper, nickel, and calcium. Recombinant Dpr protein was purified and showed iron-binding activity, whereas no DNA-binding activity was found. These data indicate that an ironbinding protein, Dpr, provides protection from hydrogen peroxide stress by preventing the Fenton reaction, and Dpr was identified as a novel stress protein that protects against several stresses in group A streptococci.

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Section: Discussionmentioning

confidence: 99%

An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus pyogenes against Multiple Stresses

Tsou

Chiang-Ni

Lin³

et al. 2008

Infect Immun

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“…The native iron core of Dps-like proteins contains only tens of iron atoms, with different ratios of phosphate [11,53]. The core can also contain other metals, such as Zn, Cu, Cr, Mn, Co, Ni and Mo [11].…”

Section: Iron Core Formationmentioning

confidence: 99%

“…The in vitro loaded iron core of Dps-like proteins is widely characterized [53][54][55]. Typically, the in vitro loaded core contains up to 500 iron atoms.…”

Section: Iron Core Formationmentioning

confidence: 99%

Dps-like proteins: structural and functional insights into a versatile protein family

Haikarainen

Papageorgiou

2009

Cell. Mol. Life Sci.

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130

136

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Dps-like proteins are key factors involved in the protection of prokaryotic cells from oxidative damage. They act by either oxidizing iron to prevent the formation of oxidative radicals or by forming Dps-DNA complexes to physically protect DNA. All Dps-like proteins are characterized by a common three-dimensional architecture and are found as spherical dodecamers with a hollow central cavity. Despite their structural similarities, recent biochemical and structural data have suggested different functions among members of the family that range from protection inside the cells in response to various stress signals to adhesion and virulence during bacterial infections. Moreover, the Dps-like proteins have lately attracted considerable interest in the field of nanotechnology owing to their ability to act as protein cages for iron and various other metals. A better understanding of their function and mechanism could therefore lead to novel applications in biotechnology and nanotechnology.

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“…Oxygen and hydrogen peroxide are the major cellular oxidants consumed during this reaction (7,9,60). Ferritins can concentrate and store iron as a mineral (hydrated ferric oxide) in their central cavity (10,25,32). This sequestered iron is nonreactive and can serve as a reserve when the exogenous availability of this metal becomes limited.…”

mentioning

confidence: 99%

Differential Role of Ferritins in Iron Metabolism and Virulence of the Plant-Pathogenic BacteriumErwinia chrysanthemi3937

et al. 2008

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During infection, the phytopathogenic enterobacterium Erwinia chrysanthemi has to cope with iron-limiting conditions and the production of reactive oxygen species by plant cells. Previous studies have shown that a tight control of the bacterial intracellular iron content is necessary for full virulence. The E. chrysanthemi genome possesses two loci that could be devoted to iron storage: the bfr gene, encoding a heme-containing bacterioferritin, and the ftnA gene, coding for a paradigmatic ferritin. To assess the role of these proteins in the physiology of this pathogen, we constructed ferritin-deficient mutants by reverse genetics. Unlike the bfr mutant, the ftnA mutant had increased sensitivity to iron deficiency and to redox stress conditions. Interestingly, the bfr ftnA mutant displayed an intermediate phenotype for sensitivity to these stresses. Whole-cell analysis by Mössbauer spectroscopy showed that the main iron storage protein is FtnA and that there is an increase in the ferrous iron/ferric iron ratio in the ftnA and bfr ftnA mutants. We found that ftnA gene expression is positively controlled by iron and the transcriptional repressor Fur via the small antisense RNA RyhB. bfr gene expression is induced at the stationary phase of growth. The S transcriptional factor is necessary for this control. Pathogenicity tests showed that FtnA and the Bfr contribute differentially to the virulence of E. chrysanthemi depending on the host, indicating the importance of a perfect control of iron homeostasis in this bacterial species during infection.

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Iron Incorporation in Streptococcus suis Dps-like Peroxide Resistance Protein Dpr Requires Mobility in the Ferroxidase Center and Leads to the Formation of a Ferrihydrite-like Core

Cited by 34 publications

References 59 publications

An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus pyogenes against Multiple Stresses

An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus pyogenes against Multiple Stresses

Dps-like proteins: structural and functional insights into a versatile protein family

Differential Role of Ferritins in Iron Metabolism and Virulence of the Plant-Pathogenic BacteriumErwinia chrysanthemi3937

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