Evidence map›Paper›PMID 31283782›Full record

ArticlePLoS pathogens2019

Increased association between Epstein-Barr virus EBNA2 from type 2 strains and the transcriptional repressor BS69 restricts EBNA2 activity.

Rajesh Ponnusamy, Ritika Khatri, Paulo B Correia, C David Wood, Erika J Mancini, Paul J Farrell, Michelle J West

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2019. 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
1.4field-weighted citation impact, top 16% 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, 22 citations in OpenAlex.

  1. Article
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  4. ZMYND11 Restrains KMT2A to Enable a Neuronal Developmental Program.bioRxiv : the preprint server for biology · 2025
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  15. Oncogenic Viruses as Entropic Drivers of Cancer Evolution.Frontiers in virology (Lausanne, Switzerland) · 2021
    Article
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  17. Article
  18. Article
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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 at 2 institutions in 1 country.

Rajesh PonnusamySchool of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Ritika KhatriSchool of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Paulo B CorreiaSection of Virology, Imperial College London, London, United Kingdom.
C David WoodSchool of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Erika J ManciniSchool of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.ORCID 0000-0001-9591-7898
Paul J FarrellSection of Virology, Imperial College London, London, United Kingdom.
Michelle J WestSchool of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.ORCID 0000-0002-9497-9365
University of Sussex · GBImperial College London · GB

Funding

Medical Research Council MR/N010388/1Medical Research Council MR/S009620/1
6 · The paper itself

Abstract

Natural variation separates Epstein-Barr virus (EBV) into type 1 and type 2 strains. Type 2 EBV is less transforming in vitro due to sequence differences in the EBV transcription factor EBNA2. This correlates with reduced activation of the EBV oncogene LMP1 and some cell genes. Transcriptional activation by type 1 EBNA2 can be suppressed through the binding of two PXLXP motifs in its transactivation domain (TAD) to the dimeric coiled-coil MYND domain (CC-MYND) of the BS69 repressor protein (ZMYND11). We identified a third conserved PXLXP motif in type 2 EBNA2. We found that type 2 EBNA2 peptides containing this motif bound BS69CC-MYND efficiently and that the type 2 EBNA2TAD bound an additional BS69CC-MYND molecule. Full-length type 2 EBNA2 also bound BS69 more efficiently in pull-down assays. Molecular weight analysis and low-resolution structures obtained using small-angle X-ray scattering showed that three BS69CC-MYND dimers bound two molecules of type 2 EBNA2TAD, in line with the dimeric state of full-length EBNA2 in vivo. Importantly, mutation of the third BS69 binding motif in type 2 EBNA2 improved B-cell growth maintenance and the transcriptional activation of the LMP1 and CXCR7 genes. Our data indicate that increased association with BS69 restricts the function of type 2 EBNA2 as a transcriptional activator and driver of B cell growth and may contribute to reduced B-cell transformation by type 2 EBV.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBinding SitesB-LymphocytesCarrier ProteinsCell Cycle ProteinsCell LineCell Transformation, ViralCo-Repressor ProteinsDNA-Binding ProteinsEpstein-Barr Virus Nuclear AntigensGenes, ViralHerpesvirus 4, HumanHost Microbial InteractionsHumansModels, MolecularCarrier ProteinsCell Cycle ProteinsCo-Repressor ProteinsDNA-Binding ProteinsEBNA-2 protein, Human herpesvirus 4Epstein-Barr Virus Nuclear AntigensTrans-ActivatorsViral ProteinsZMYND11 protein, human

Identifiers

PMID31283782
PMCPMC6638984
OpenAlexW2958579969

What OpenQuestion holds

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LicenceCC BY
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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.