Evidence map›Paper›PMID 20106921›Full record

ArticleJournal of virology2010

Comparison of the biological and biochemical activities of several members of the alphaherpesvirus ICP0 family of proteins.

Roger D Everett, Chris Boutell, Carol McNair, Louise Grant, Anne Orr

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Sp140L functions as a herpesvirus restriction factor suppressing viral transcription and activating interferon-stimulated genes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. The Fate of Speckled Protein 100 (Sp100) During Herpesviruses Infection.Frontiers in cellular and infection microbiology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Viral Interplay with the Host Sumoylation System.Advances in experimental medicine and biology · 2017
    Review
  18. Article
  19. Article
  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

5 authors.

Roger D EverettMRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, Scotland, United Kingdom. r.everett@mrcvu.gla.ac.uk
Chris Boutell
Carol McNair
Louise Grant
Anne Orr

Funding

Medical Research Council MC_U130169966Medical Research Council MC_UP_A550_1030Medical Research Council MC_UU_12014/5
6 · The paper itself

Abstract

Immediate-early protein ICP0 of herpes simplex virus type 1 (HSV-1) is an E3 ubiquitin ligase of the RING finger class that is required for efficient lytic infection and reactivation from latency. Other alphaherpesviruses also express ICP0-related RING finger proteins, but these have limited homology outside the core RING domain. Existing evidence indicates that ICP0 family members have similar properties, but there has been no systematic comparison of the biochemical activities and biological functions of these proteins. Here, we describe an inducible cell line system that allows expression of the ICP0-related proteins of bovine herpes virus type 1 (BHV-1), equine herpesvirus type 1 (EHV-1), pseudorabies virus (PRV), and varicella-zoster virus (VZV) and their subsequent functional analysis. We report that the RING domains of all the proteins have E3 ubiquitin ligase activity in vitro. The BHV-1, EHV-1, and PRV proteins complement ICP0-null mutant HSV-1 plaque formation and induce derepression of quiescent HSV-1 genomes to levels similar to those achieved by ICP0 itself. VICP0, the ICP0 expressed by VZV, was found to be extremely unstable, which limited its analysis in this system. We compared the abilities of the ICP0-related proteins to disrupt ND10, to induce degradation of PML and Sp100, to affect key components of the interferon signaling pathway, and to interfere with induction of interferon-stimulated genes. We found that the property that correlated most closely with their biological activities was the ability to preclude the recruitment of cellular ND10 proteins to sites closely associated with incoming HSV-1 genomes and early replication compartments.

Indexed as

AnimalsAntigens, NuclearAutoantigensCell LineGenome, ViralHerpesvirus 1, BovineHerpesvirus 1, HumanHerpesvirus 1, SuidHerpesvirus 3, HumanHumansImmediate-Early ProteinsNuclear ProteinsPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexResponse ElementsTranscription FactorsAntigens, NuclearAutoantigensCALCOCO2 protein, humangene 63 protein, Equine herpesvirus 1Immediate-Early ProteinsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexSP100 protein, humanTranscription FactorsTumor Suppressor ProteinsUbiquitin-Protein LigasesViral ProteinsVmw110 protein, Human herpesvirus 1

Identifiers

PMID20106921
PMCPMC2838103
OpenAlexW2100773500

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.