Evidence map›Paper›PMID 30644558›Full record

ArticleAnnals of the New York Academy of Sciences2019

Species-specific inhibition of antiviral protein kinase R by capripoxviruses and vaccinia virus.

Chorong Park, Chen Peng, Greg Brennan, Stefan Rothenburg

Open access · greenAbstract read
In one paragraph

Article in Annals of the New York Academy of Sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Human Riboviruses: A Comprehensive Study.Journal of molecular evolution · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Antagonism of Protein Kinase R by Large DNA Viruses.Pathogens (Basel, Switzerland) · 2022
    Review
  20. Article
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

4 authors at 2 institutions in 1 country.

Chorong ParkSchool of Medicine, Department of Medial Microbiology and Immunology, University of California Davis, Davis, California.ORCID 0000-0001-5751-5767
Chen PengDivision of Biology, Kansas State University, Manhattan, Kansas.ORCID 0000-0001-6141-8775
Greg BrennanSchool of Medicine, Department of Medial Microbiology and Immunology, University of California Davis, Davis, California.ORCID 0000-0002-4339-9045
Stefan RothenburgSchool of Medicine, Department of Medial Microbiology and Immunology, University of California Davis, Davis, California.ORCID 0000-0002-2525-8230
University of California, Davis · USKansas State University · US

Funding

Importance of Species-Specific Interactions of PKR with Poxvirus Inhibitors for Virus Replication and Host RangeR01AI114851 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ROTHENBURG, STEFAN · 2015 to 2019
$1.8M
National Institute of Allergy and Infectious Diseases AI114851NIAID NIH HHS R01 AI114851
6 · The paper itself

Abstract

Double-stranded RNA-activated protein kinase R (PKR) is an important and rapidly evolving antiviral kinase. Most poxviruses contain two distinct PKR inhibitors, called E3 and K3 in vaccinia virus (VACV), the prototypic orthopoxvirus. E3 prevents PKR homodimerization by binding double-stranded RNA, while K3 acts as a pseudosubstrate inhibitor by binding directly to activated PKR and thereby inhibiting interaction with its substrate eIF2α. In our study here, we analyzed E3 and K3 orthologs from the phylogenetically distinct capripoxviruses (CaPVs), which include lumpy skin disease virus, sheeppox virus, and goatpox virus. Whereas the sheeppox virus E3 ortholog did not substantially inhibit PKR, all three CaPV K3 orthologs showed species-specific inhibition of PKR, with strong inhibition of sheep, goat, and human PKR but only weak inhibition of cow and mouse PKR. In contrast, VACV K3 strongly inhibited cow and mouse PKR but not sheep, goat, or human PKR. Infection of cell lines from the respective species with engineered VACV strains that contained different K3 orthologs showed a good correlation of PKR inhibition with virus replication and eIF2α phosphorylation. Our results show that K3 orthologs can have dramatically different effects on PKR of different species and indicate that effective PKR inhibition by K3 orthologs is crucial for virus replication.

Indexed as

AnimalsCapripoxvirusCattleCell LineeIF-2 KinaseGoatsHeLa CellsHumansMicePoxviridae InfectionsRNA, Double-StrandedSheepSpecies SpecificityVaccinia virusViral ProteinsVirus ReplicationEIF2AK2 protein, humaneIF-2 KinaseRNA, Double-StrandedViral Proteinscapripoxviruseshost-pathogen interactionsPKRpoxvirustranslational regulationvaccinia virus

Identifiers

PMID30644558
PMCPMC7989821
OpenAlexW2910865545

What OpenQuestion holds

Textmetadata
LicenceTDM
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.