Evidence map›Paper›PMID 24136784›Full record

ArticleEMBO molecular medicine2013

Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence.

Malek Saleh, Sergio G Bartual, Mohammed R Abdullah, Inga Jensch, Tauseef M Asmat, Lothar Petruschka, Thomas Pribyl, Manuela Gellert, Christopher H Lillig, Haike Antelmann and 2 more

Open access · goldAbstract read
In one paragraph

Article in EMBO molecular medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Factor XII-driven coagulation traps bacterial infections.The Journal of experimental medicine · 2025
    Article
  5. Article
  6. EmergentInfection and immunity · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. The oxidative stress response ofFrontiers in microbiology · 2023
    Review
  16. Article
  17. Article
  18. The Peptide Methionine Sulfoxide Reductase (MsrAB) ofAntioxidants (Basel, Switzerland) · 2022
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 2 countries.

Malek SalehDepartment Genetics of Microorganisms, Interfaculty Institute for Genetics and Functional Genomics, Ernst Moritz Arndt University of Greifswald, Greifswald, Germany.
Sergio G Bartual
Mohammed R Abdullah
Inga Jensch
Tauseef M Asmat
Lothar Petruschka
Thomas Pribyl
Manuela Gellert
Christopher H Lillig
Haike Antelmann
Juan A Hermoso
Sven Hammerschmidt
Universität Greifswald · DEInstituto de Química Física Blas Cabrera · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The respiratory pathogen Streptococcus pneumoniae has evolved efficient mechanisms to resist oxidative stress conditions and to displace other bacteria in the nasopharynx. Here we characterize at physiological, functional and structural levels two novel surface-exposed thioredoxin-family lipoproteins, Etrx1 and Etrx2. The impact of both Etrx proteins and their redox partner methionine sulfoxide reductase SpMsrAB2 on pneumococcal pathogenesis was assessed in mouse virulence studies and phagocytosis assays. The results demonstrate that loss of function of either both Etrx proteins or SpMsrAB2 dramatically attenuated pneumococcal virulence in the acute mouse pneumonia model and that Etrx proteins compensate each other. The deficiency of Etrx proteins or SpMsrAB2 further enhanced bacterial uptake by macrophages, and accelerated pneumococcal killing by H2 O2 or free methionine sulfoxides (MetSO). Moreover, the absence of both Etrx redox pathways provokes an accumulation of oxidized SpMsrAB2 in vivo. Taken together our results reveal insights into the role of two extracellular electron pathways required for reduction of SpMsrAB2 and surface-exposed MetSO. Identification of this system and its target proteins paves the way for the design of novel antimicrobials.

Indexed as

AnimalsBacterial ProteinsCatalytic DomainCrystallography, X-RayDisease Models, AnimalFemaleHydrogen PeroxideMacrophagesMethionineMiceMolecular Sequence DataOxidative StressPhagocytosisPneumoniaProtein Structure, TertiaryRecombinant ProteinsBacterial ProteinsHydrogen PeroxideMethioninemethionine sulfoxideRecombinant Proteinslipoproteinsmeningitisoxidative stresspneumococcipneumonia

Identifiers

PMID24136784
PMCPMC3914529
OpenAlexW2139951580

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.