Evidence map›Paper›PMID 31941785›Full record

ArticleJournal of virology2020

Phase Separation of Epstein-Barr Virus EBNA2 and Its Coactivator EBNALP Controls Gene Expression.

Qiu Peng, Lujuan Wang, Zailong Qin, Jia Wang, Xiang Zheng, Lingyu Wei, Xiaoyue Zhang, Xuemei Zhang, Can Liu, Zhengshuo Li and 4 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025
    Review
  9. Review
  10. 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
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  14. Review
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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

14 authors at 3 institutions in 1 country.

Qiu Peng *Department of Clinical Laboratory, Xiangya Hospital, Central South University, Changsha, China.
Lujuan Wang *Department of Clinical Laboratory, Xiangya Hospital, Central South University, Changsha, China.
Zailong QinGenetic and Metabolic Central Laboratory, Maternal and Child Health Hospital of Guangxi Zhuang Autonomous Region, Nanning, Guangxi, China.
Jia WangCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Xiang ZhengCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Lingyu WeiCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Xiaoyue ZhangCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Xuemei ZhangAffiliated Hospital of Guilin Medical University, Guilin, Guangxi, China.
Can LiuCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Zhengshuo LiCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Yangge WuCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Guiyuan LiCancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
Qun YanDepartment of Clinical Laboratory, Xiangya Hospital, Central South University, Changsha, China yanqun@csu.edu.cn majian@csu.edu.cn.
Jian MaDepartment of Clinical Laboratory, Xiangya Hospital, Central South University, Changsha, China yanqun@csu.edu.cn majian@csu.edu.cn.ORCID 0000-0001-9395-0416
Central South University · CNMinistry of Education of the People's Republic of China · CNGuangxi Maternal and Child Health Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological macromolecule condensates formed by liquid-liquid phase separation (LLPS) have been discovered in recent years to be prevalent in biology. These condensates are involved in diverse processes, including the regulation of gene expression. LLPS of proteins have been found in animal, plant, and bacterial species but have scarcely been identified in viral proteins. Here, we discovered that Epstein-Barr virus (EBV) EBNA2 and EBNALP form nuclear puncta that exhibit properties of liquid-like condensates (or droplets), which are enriched in superenhancers of MYC and Runx3. EBNA2 and EBNALP are transcription factors, and the expression of their target genes is suppressed by chemicals that perturb LLPS. Intrinsically disordered regions (IDRs) of EBNA2 and EBNALP can form phase-separated droplets, and specific proline residues of EBNA2 and EBNALP contribute to droplet formation. These findings offer a foundation for understanding the mechanism by which LLPS, previously determined to be related to the organization of P bodies, membraneless organelles, nucleolus homeostasis, and cell signaling, plays a key role in EBV-host interactions and is involved in regulating host gene expression. This work suggests a novel anti-EBV strategy where developing appropriate drugs of interfering LLPS can be used to destroy the function of the EBV's transcription factors.

Indexed as

Gene Expression RegulationCell Line, TumorCell NucleolusCell NucleusCore Binding Factor Alpha 3 SubunitEpstein-Barr Virus Nuclear AntigensGenes, mycHEK293 CellsHerpesvirus 4, HumanHumansIntrinsically Disordered ProteinsLeukocytes, MononuclearMicroscopy, FluorescenceProlinePromoter Regions, GeneticProtein DomainsCore Binding Factor Alpha 3 SubunitEBNA-2 protein, Human herpesvirus 4EBNA-LP protein, Human herpesvirus 4Epstein-Barr Virus Nuclear AntigensIntrinsically Disordered ProteinsProlineRunx3 protein, humanViral ProteinsEBNA2EBNALPEpstein-Barr virusphase separationsuperenhancer

Identifiers

PMID31941785
PMCPMC7081900
OpenAlexW3000522892

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.