Evidence map›Paper›PMID 25978044›Full record

ArticlePloS one2015

Subunits of the Pyruvate Dehydrogenase Cluster of Mycoplasma pneumoniae Are Surface-Displayed Proteins that Bind and Activate Human Plasminogen.

Anne Gründel, Kathleen Friedrich, Melanie Pfeiffer, Enno Jacobs, Roger Dumke

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  10. Fibrinolysis: A Primordial System Linked to the Immune Response.International journal of molecular sciences · 2021
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  13. Genome-Wide Analysis ofG3 (Bethesda, Md.) · 2019
    Article
  14. Review
  15. Review
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  17. Genome-Wide Analysis ofG3 (Bethesda, Md.) · 2018
    Article
  18. Article
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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

5 authors at 2 institutions in 1 country.

Anne GründelTU Dresden, Institute of Medical Microbiology and Hygiene, Dresden, Germany.
Kathleen FriedrichTU Dresden, Institute of Medical Microbiology and Hygiene, Dresden, Germany.
Melanie PfeifferTU Dresden, Institute of Medical Microbiology and Hygiene, Dresden, Germany.
Enno JacobsTU Dresden, Institute of Medical Microbiology and Hygiene, Dresden, Germany.
Roger DumkeTU Dresden, Institute of Medical Microbiology and Hygiene, Dresden, Germany.
Institute of Medical Microbiology and Hygiene · DETU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dual role of glycolytic enzymes in cytosol-located metabolic processes and in cell surface-mediated functions with an influence on virulence is described for various micro-organisms. Cell wall-less bacteria of the class Mollicutes including the common human pathogen Mycoplasma pneumoniae possess a reduced genome limiting the repertoire of virulence factors and metabolic pathways. After the initial contact of bacteria with cells of the respiratory epithelium via a specialized complex of adhesins and release of cell-damaging factors, surface-displayed glycolytic enzymes may facilitate the further interaction between host and microbe. In this study, we described detection of the four subunits of pyruvate dehydrogenase complex (PDHA-D) among the cytosolic and membrane-associated proteins of M. pneumoniae. Subunits of PDH were cloned, expressed and purified to produce specific polyclonal guinea pig antisera. Using colony blotting, fractionation of total proteins and immunofluorescence experiments, the surface localization of PDHA-C was demonstrated. All recombinant PDH subunits are able to bind to HeLa cells and human plasminogen. These interactions can be specifically blocked by the corresponding polyclonal antisera. In addition, an influence of ionic interactions on PDHC-binding to plasminogen as well as of lysine residues on the association of PDHA-D with plasminogen was confirmed. The PDHB subunit was shown to activate plasminogen and the PDHB-plasminogen complex induces degradation of human fibrinogen. Hence, our data indicate that the surface-associated PDH subunits might play a role in the pathogenesis of M. pneumoniae infections by interaction with human plasminogen.

Indexed as

Adhesins, BacterialAnimalsBacterial ProteinsCell Line, TumorCell MembraneEscherichia coliGuinea PigsHeLa CellsHumansMembrane ProteinsMycoplasma pneumoniaePlasminogenProtein BindingProtein SubunitsPyruvate Dehydrogenase ComplexVirulenceAdhesins, BacterialBacterial ProteinsMembrane ProteinsPlasminogenProtein SubunitsPyruvate Dehydrogenase ComplexVirulence Factors

Identifiers

PMID25978044
PMCPMC4433191
OpenAlexW1529655496

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.