Evidence map›Paper›PMID 32665273›Full record

ArticlemBio2020

eIF2B as a Target for Viral Evasion of PKR-Mediated Translation Inhibition.

Jennifer Deborah Wuerth, Matthias Habjan, Markus Kainulainen, Besim Berisha, Damien Bertheloot, Giulio Superti-Furga, Andreas Pichlmair, Friedemann Weber

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Current issues in molecular biology · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Frontiers in immunology · 2023
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Inhibition of PKR by Viruses.Frontiers in microbiology · 2021
    Review
  19. 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

8 authors at 6 institutions in 2 countries.

Jennifer Deborah WuerthInstitute for Virology, FB10-Veterinary Medicine, Justus-Liebig University, Giessen, Germany.ORCID 0000-0002-3391-9633
Matthias HabjanInnate Immunity Laboratory, Max-Planck Institute of Biochemistry, Munich, Germany.
Markus KainulainenInstitute for Virology, Philipps-University Marburg, Marburg, Germany.
Besim BerishaInstitute for Virology, FB10-Veterinary Medicine, Justus-Liebig University, Giessen, Germany.
Damien BerthelootInstitute of Innate Immunity, University of Bonn, Bonn, Germany.
Giulio Superti-FurgaCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.
Andreas PichlmairInnate Immunity Laboratory, Max-Planck Institute of Biochemistry, Munich, Germany.
Friedemann WeberInstitute for Virology, FB10-Veterinary Medicine, Justus-Liebig University, Giessen, Germany friedemann.weber@vetmed.uni-giessen.de.ORCID 0000-0001-9737-337X
Philipps University of Marburg · DEUniversity of Bonn · DEAustrian Academy of Sciences · ATGerman Center for Infection Research · DEJustus-Liebig-Universität Gießen · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA-activated protein kinase (PKR) is a major innate immune factor that senses viral double-stranded RNA (dsRNA) and phosphorylates eukaryotic initiation factor (eIF) 2α. Phosphorylation of the α subunit converts the eIF2αβγ complex into a stoichiometric inhibitor of eukaryotic initiation factor eIF2B, thus halting mRNA translation. To escape this protein synthesis shutoff, viruses have evolved countermechanisms such as dsRNA sequestration, eIF-independent translation by an internal ribosome binding site, degradation of PKR, or dephosphorylation of PKR or of phospho-eIF2α. Here, we report that sandfly fever Sicilian phlebovirus (SFSV) confers such a resistance without interfering with PKR activation or eIF2α phosphorylation. Rather, SFSV expresses a nonstructural protein termed NSs that strongly binds to eIF2B. Although NSs still allows phospho-eIF2α binding to eIF2B, protein synthesis and virus replication are unhindered. Hence, SFSV encodes a unique PKR antagonist that acts by rendering eIF2B resistant to the inhibitory action of bound phospho-eIF2α.

Indexed as

Host-Pathogen InteractionsPeptide Chain Initiation, TranslationalA549 CellsAnimalsCell LineChlorocebus aethiopseIF-2 KinaseEukaryotic Initiation Factor-2BHEK293 CellsHumansPhlebovirusPhosphorylationVero CellsViral Nonstructural ProteinsVirus ReplicationeIF-2 KinaseEukaryotic Initiation Factor-2BViral Nonstructural ProteinseIF2Bintegrated stress responseNSs proteinphospho-eIF2αPKRsandfly fever Sicilian phlebovirustranslation inhibitionviral PKR antagonist

Identifiers

PMID32665273
PMCPMC7360930
OpenAlexW3042273469

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.