Evidence map›Paper›PMID 18541662›Full record

ArticleInfection and immunity2008

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

Open access · greenAbstract readComparative Study
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.5field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Dpr-mediated HJournal of bacteriology · 2024
    Article
  3. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Pathogens (Basel, Switzerland) · 2021
    Review
  9. Review
  10. Article
  11. Frontiers in microbiology · 2020
    Article
  12. In vivo 3'-to-5' exoribonuclease targetomes ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. The XRE Family Transcriptional Regulator SrtR inFrontiers in cellular and infection microbiology · 2018
    Article
  17. The PerR-Regulated PInfection and immunity · 2017
    Article
  18. Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 4 countries.

Chih-Cheng TsouInstitute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Chuan Chiang-Ni
Yee-Shin Lin
Woei-Jer Chuang
Ming-T Lin
Ching-Chuan Liu
Jiunn-Jong Wu
Institute of Physiology and Basic Medicine · RUPediatrics and Genetics · USInstitute of Basic Medical Sciences of the Chinese Academy of Medical SciencesLaboratoire de Biochimie · FRNational Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 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 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.

Indexed as

Adaptation, PhysiologicalAcidsBacterial ProteinsColony Count, MicrobialCulture MediaDNA-Binding ProteinsGene DeletionGenetic Complementation TestHydrogen PeroxideIron-Binding ProteinsMetalsMicrobial ViabilityMutagenesis, InsertionalOxidative StressStreptococcus pyogenesAcidsBacterial ProteinsCulture MediaDNA-Binding ProteinsDpr protein, StreptococcusHydrogen PeroxideIron-Binding ProteinsMetals

Identifiers

PMID18541662
PMCPMC2519395
OpenAlexW2165218607

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.