An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses

Chih Cheng Tsou, Chuan Chiang-Ni, Yee Shin Lin, Woei Jer Chuang, Ming T. Lin, Ching Chuan Liu, Jiunn Jong Wu

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

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 H2O2, 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 iron-binding 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.

Original languageEnglish
Pages (from-to)4038-4045
Number of pages8
JournalInfection and Immunity
Volume76
Issue number9
DOIs
Publication statusPublished - 2008 Sep 1

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Iron-Binding Proteins
Streptococcus pyogenes
Hydrogen Peroxide
Iron
Peroxides
Heat-Shock Proteins
Deferoxamine
Chelating Agents
Manganese
Streptococcus
Nickel
Recombinant Proteins
Mutagenesis
Catalase
Zinc
Copper
Oxidative Stress
Calcium
Acids
DNA

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

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title = "An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses",
abstract = "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 H2O2, 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 iron-binding 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.",
author = "Tsou, {Chih Cheng} and Chuan Chiang-Ni and Lin, {Yee Shin} and Chuang, {Woei Jer} and Lin, {Ming T.} and Liu, {Ching Chuan} and Wu, {Jiunn Jong}",
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An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses. / Tsou, Chih Cheng; Chiang-Ni, Chuan; Lin, Yee Shin; Chuang, Woei Jer; Lin, Ming T.; Liu, Ching Chuan; Wu, Jiunn Jong.

In: Infection and Immunity, Vol. 76, No. 9, 01.09.2008, p. 4038-4045.

Research output: Contribution to journalArticle

TY - JOUR

T1 - An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses

AU - Tsou, Chih Cheng

AU - Chiang-Ni, Chuan

AU - Lin, Yee Shin

AU - Chuang, Woei Jer

AU - Lin, Ming T.

AU - Liu, Ching Chuan

AU - Wu, Jiunn Jong

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