Evidence map›Paper›PMID 28278207›Full record

ArticlePloS one2017

PA28 modulates antigen processing and viral replication during coxsackievirus B3 infection.

Dorota Respondek, Martin Voss, Ina Kühlewindt, Karin Klingel, Elke Krüger, Antje Beling

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The Significant Role of PA28αβ in CD8International journal of molecular sciences · 2024
    Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. 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

6 authors at 3 institutions in 1 country.

Dorota RespondekInstitut für Biochemie, Charité Universitätsmedizin Berlin, Berlin, Germany.
Martin VossInstitut für Biochemie, Charité Universitätsmedizin Berlin, Berlin, Germany.
Ina KühlewindtInstitut für Biochemie, Charité Universitätsmedizin Berlin, Berlin, Germany.
Karin KlingelInstitut für Molekulare Pathologie, Universitätsklinikum Tübingen, Tübingen, Germany.
Elke KrügerInstitut für Biochemie, Charité Universitätsmedizin Berlin, Berlin, Germany.
Antje BelingInstitut für Biochemie, Charité Universitätsmedizin Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0002-1826-5248
German Centre for Cardiovascular Research · DECharité - Universitätsmedizin Berlin · DEUniversitätsklinikum Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The function of the proteasome is modulated at the level of subunit expression and by association with its regulatory complexes. During coxsackievirus B3 (CVB3) myocarditis, IFN-induced formation of immunoproteasomes (ip) is known to be critical for regulating immune modulating molecules. The function of the IFN-γ-inducible proteasome regulator subunits PA28 α and β, however, in this context was unknown. During viral myocarditis, we found an increased abundance of PA28β subunits in heart tissue. PA28α/β exists in PA28-20S-PA28 and PA700-20S-PA28 hybrid proteasome complexes in cells both with either predominant ip and standard proteasome (sp) expression. Being in line with reduced proteasome activity in PA28α/β-deficient cells, we observed increased levels of oxidized and poly-ubiquitinated proteins upon TLR3-activation in these cells. Moreover, PA28α/β is capable to interfere directly with viral replication of CVB3 and facilitates the generation of CVB3-derived MHC class I epitopes by the proteasome. In contrast to a distinct function of PA28α/β in vitro, gene ablation of PA28α/β in mice being on a genetic background with resistance towards the development of severe infection had no significant impact on disease progression. Other than reported for the ip, in this host PA28α/β is dispensable to meet the demand of increased peptide hydrolysis capacity by the proteasome during viral myocarditis.

Indexed as

Virus ReplicationAnimalsAntigen PresentationAutoantigensCoxsackievirus InfectionsEnterovirus B, HumanEpitopesFemaleMiceMice, Inbred C57BLMice, KnockoutMyocarditisProteasome Endopeptidase ComplexAutoantigensEpitopesPA700 proteasome activatorProteasome Endopeptidase ComplexPsme1 protein, mousePSME2 protein, human

Identifiers

PMID28278207
PMCPMC5344377
OpenAlexW2593556121

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.