Evidence map›Paper›PMID 22291899›Full record

ArticlePloS one2012

Group B streptococcus GAPDH is released upon cell lysis, associates with bacterial surface, and induces apoptosis in murine macrophages.

Liliana Oliveira, Pedro Madureira, Elva Bonifácio Andrade, Abdelouhab Bouaboud, Eric Morello, Paula Ferreira, Claire Poyart, Patrick Trieu-Cuot, Shaynoor Dramsi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

48 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface ofInternational journal of molecular sciences · 2024
    Article
  6. SubcutaneousJournal of veterinary science · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. "Applied and environmental microbiology · 2021
    Article
  12. Article
  13. International journal of molecular sciences · 2020
    Article
  14. Article
  15. Biology open · 2020
    Article
  16. Review
  17. Article
  18. Review
  19. Why Do Intravascular Schistosomes Coat Themselves in Glycolytic Enzymes?BioEssays : news and reviews in molecular, cellular and developmental biology · 2019
    Article
  20. Genetics of Lactococci.Microbiology spectrum · 2019
    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

9 authors at 6 institutions in 2 countries.

Liliana OliveiraUniversidade do Porto, ICBAS-Instituto de Ciências Biomédicas de Abel Salazar, Porto, Portugal.
Pedro Madureira
Elva Bonifácio Andrade
Abdelouhab Bouaboud
Eric Morello
Paula Ferreira
Claire Poyart
Patrick Trieu-Cuot
Shaynoor Dramsi
Instituto de Biologia Molecular e CelularInstitut Pasteur · FRSorbonne Paris Cité · FRCentre National de la Recherche Scientifique · FRInserm · FRUniversidade do Porto · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyceraldehyde 3-phosphate dehydrogenases (GAPDH) are cytoplasmic glycolytic enzymes that, despite lacking identifiable secretion signals, have been detected at the surface of several prokaryotic and eukaryotic organisms where they exhibit non-glycolytic functions including adhesion to host components. Group B Streptococcus (GBS) is a human commensal bacterium that has the capacity to cause life-threatening meningitis and septicemia in newborns. Electron microscopy and fluorescence-activated cell sorter (FACS) analysis demonstrated the surface localization of GAPDH in GBS. By addressing the question of GAPDH export to the cell surface of GBS strain NEM316 and isogenic mutant derivatives of our collection, we found that impaired GAPDH presence in the surface and supernatant of GBS was associated with a lower level of bacterial lysis. We also found that following GBS lysis, GAPDH can associate to the surface of many living bacteria. Finally, we provide evidence for a novel function of the secreted GAPDH as an inducer of apoptosis of murine macrophages.

Indexed as

AnimalsAntigens, SurfaceApoptosisBacterial AdhesionBacterial LysatesBacterial ProteinsCell ExtractsCells, CulturedFemaleFimbriae, BacterialGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)MacrophagesMiceMice, Inbred C57BLOrganisms, Genetically ModifiedProtein BindingAntigens, SurfaceBacterial LysatesBacterial ProteinsBroncho-VaxomCell ExtractsGAPDH protein, Streptococcus agalactiaeGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)

Identifiers

PMID22291899
PMCPMC3264557
OpenAlexW2024634380

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.