Evidence map›Paper›PMID 23027531›Full record

ArticleInfection and immunity2012

Thiol peroxidase is an important component of Streptococcus pneumoniae in oxygenated environments.

Barak Hajaj, Hasan Yesilkaya, Rachel Benisty, Maayan David, Peter W Andrew, Nurith Porat

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 53 citations in OpenAlex.

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  7. Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021
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  13. Structure-function analyses of alkylhydroperoxidase D fromThe Journal of biological chemistry · 2020
    Article
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  19. Neutrophils and Bacterial Immune Evasion.Journal of innate immunity · 2018
    Review
  20. Article
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

6 authors at 2 institutions in 2 countries.

Barak HajajPediatric Infectious Disease Unit, Soroka University Medical Center, Faculty of Health Sciences, Department of Microbiology and Immunology, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Hasan Yesilkaya
Rachel Benisty
Maayan David
Peter W Andrew
Nurith Porat
Ben-Gurion University of the Negev · ILUniversity of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pneumoniae is an aerotolerant gram-positive bacterium that causes an array of diseases, including pneumonia, otitis media, and meningitis. During aerobic growth, S. pneumoniae produces high levels of H(2)O(2). Since S. pneumoniae lacks catalase, the question of how it controls H(2)O(2) levels is of critical importance. The psa locus encodes an ABC Mn(2+)-permease complex (psaBCA) and a putative thiol peroxidase, tpxD. This study shows that tpxD encodes a functional thiol peroxidase involved in the adjustment of H(2)O(2) homeostasis in the cell. Kinetic experiments showed that recombinant TpxD removed H(2)O(2) efficiently. However, in vivo experiments revealed that TpxD detoxifies only a fraction of the H(2)O(2) generated by the pneumococcus. Mass spectrometry analysis demonstrated that TpxD Cys(58) undergoes selective oxidation in vivo, under conditions where H(2)O(2) is formed, confirming the thiol peroxidase activity. Levels of TpxD expression and synthesis in vitro were significantly increased in cells grown under aerobic versus anaerobic conditions. The challenge with D39 and TIGR4 with H(2)O(2) resulted in tpxD upregulation, while psaBCA expression was oppositely affected. However, the challenge of ΔtpxD mutants with H(2)O(2) did not affect psaBCA, implying that TpxD is involved in the regulation of the psa operon, in addition to its scavenging activity. Virulence studies demonstrated a notable difference in the survival time of mice infected intranasally with D39 compared to that of mice infected intranasally with D39ΔtpxD. However, when bacteria were administered directly into the blood, this difference disappeared. The findings of this study suggest that TpxD constitutes a component of the organism's fundamental strategy to fine-tune cellular processes in response to H(2)O(2).

Indexed as

AerobiosisAnaerobiosisAnimalsAnimals, Outbred StrainsBacterial ProteinsFemaleGene Expression Regulation, BacterialHydrogen PeroxideMiceOxidative StressOxygenPeroxidaseStreptococcus pneumoniaeSulfhydryl CompoundsVirulenceBacterial ProteinsHydrogen PeroxideOxygenPeroxidasepsaD protein, StreptococcusSulfhydryl Compounds

Identifiers

PMID23027531
PMCPMC3497430
OpenAlexW2102320362

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.