Evidence map›Paper›PMID 26559969›Full record

ArticleThe Journal of biological chemistry2015

The Structure of the Cyprinid herpesvirus 3 ORF112-Zα·Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Response.

Krzysztof Kuś, Krzysztof Rakus, Maxime Boutier, Theokliti Tsigkri, Luisa Gabriel, Alain Vanderplasschen, Alekos Athanasiadis

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Type I Interferon: Monkeypox/Mpox Viruses Achilles Heel?Advances in experimental medicine and biology · 2024
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Z-DNA and Z-RNA: Methods-Past and Future.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Subversion of Programed Cell Death by Poxviruses.Current topics in microbiology and immunology · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Z-DNA and Z-RNA in human disease.Communications biology · 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

7 authors.

Krzysztof KuśFrom the Instituto Gulbenkian de Ciência, 2781-156, Oeiras, Portugal and.
Krzysztof Rakusthe Immunology-Vaccinology Laboratory, Department of Infectious and Parasitic Diseases, Fundamental and Applied Research for Animals & Health, Faculty of Veterinary Medicine, University of Liège, B-4000 Liège, Belgium.
Maxime Boutierthe Immunology-Vaccinology Laboratory, Department of Infectious and Parasitic Diseases, Fundamental and Applied Research for Animals & Health, Faculty of Veterinary Medicine, University of Liège, B-4000 Liège, Belgium.
Theokliti TsigkriFrom the Instituto Gulbenkian de Ciência, 2781-156, Oeiras, Portugal and.
Luisa GabrielFrom the Instituto Gulbenkian de Ciência, 2781-156, Oeiras, Portugal and.
Alain Vanderplasschenthe Immunology-Vaccinology Laboratory, Department of Infectious and Parasitic Diseases, Fundamental and Applied Research for Animals & Health, Faculty of Veterinary Medicine, University of Liège, B-4000 Liège, Belgium.
Alekos AthanasiadisFrom the Instituto Gulbenkian de Ciência, 2781-156, Oeiras, Portugal and alekos@igc.gulbenkian.pt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vertebrate species, the innate immune system down-regulates protein translation in response to viral infection through the action of the double-stranded RNA (dsRNA)-activated protein kinase (PKR). In some teleost species another protein kinase, Z-DNA-dependent protein kinase (PKZ), plays a similar role but instead of dsRNA binding domains, PKZ has Zα domains. These domains recognize the left-handed conformer of dsDNA and dsRNA known as Z-DNA/Z-RNA. Cyprinid herpesvirus 3 infects common and koi carp, which have PKZ, and encodes the ORF112 protein that itself bears a Zα domain, a putative competitive inhibitor of PKZ. Here we present the crystal structure of ORF112-Zα in complex with an 18-bp CpG DNA repeat, at 1.5 Å. We demonstrate that the bound DNA is in the left-handed conformation and identify key interactions for the specificity of ORF112. Localization of ORF112 protein in stress granules induced in Cyprinid herpesvirus 3-infected fish cells suggests a functional behavior similar to that of Zα domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCarpsConserved SequenceDNA-Activated Protein KinaseDNA, Z-FormFish DiseasesInterferonsModels, MolecularNucleic Acid ConformationPoxviridaeProtein BindingProtein Structure, TertiaryRNA, Double-StrandedRNA VirusesDNA-Activated Protein KinaseDNA, Z-FormInterferonsRNA, Double-StrandedViral ProteinsDNA virusesinterferonprotein-nucleic acid interactionstress granuleX-ray crystallographyZalpha domain

Identifiers

PMID26559969
PMCPMC4692202

What OpenQuestion holds

Textmetadata
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.