Evidence map›Paper›PMID 18815303›Full record

ArticleJournal of virology2008

Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production.

Chung-Pei Lee, Yu-Hao Huang, Su-Fang Lin, Yao Chang, Yu-Hsin Chang, Kenzo Takada, Mei-Ru Chen

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 5% 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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 121 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Chromatin Control of EBV Infection and Latency.Current topics in microbiology and immunology · 2025
    Article
  7. Review
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  14. Article
  15. Article
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  17. Article
  18. Nuclear Cytoskeleton in Virus Infection.International journal of molecular sciences · 2022
    Review
  19. Review
  20. Review

32 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Chung-Pei LeeGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Yu-Hao Huang
Su-Fang Lin
Yao Chang
Yu-Hsin Chang
Kenzo Takada
Mei-Ru Chen
National Taiwan University · TWHokkaido University · JPNational Health Research Institutes · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA viruses adopt various strategies to modulate the cellular environment for efficient genome replication and virion production. Previously, we demonstrated that the BGLF4 kinase of Epstein-Barr virus (EBV) induces premature chromosome condensation through the activation of condensin and topoisomerase IIalpha (C. P. Lee, J. Y. Chen, J. T. Wang, K. Kimura, A. Takemoto, C. C. Lu, and M. R. Chen, J. Virol. 81:5166-5180, 2007). In this study, we show that BGLF4 interacts with lamin A/C and phosphorylates lamin A protein in vitro. Using a green fluorescent protein (GFP)-lamin A system, we found that Ser-22, Ser-390, and Ser-392 of lamin A are important for the BGLF4-induced disassembly of the nuclear lamina and the EBV reactivation-mediated redistribution of nuclear lamin. Virion production and protein levels of two EBV primary envelope proteins, BFRF1 and BFLF2, were reduced significantly by the expression of GFP-lamin A(5A), which has five Ser residues replaced by Ala at amino acids 22, 390, 392, 652, and 657 of lamin A. Our data indicate that BGLF4 kinase phosphorylates lamin A/C to promote the reorganization of the nuclear lamina, which then may facilitate the interaction of BFRF1 and BFLF2s and subsequent virion maturation. UL kinases of alpha- and betaherpesviruses also induce the disassembly of the nuclear lamina through similar sites on lamin A/C, suggesting a conserved mechanism for the nuclear egress of herpesviruses.

Indexed as

Adenosine TriphosphatasesAntigens, NeoplasmDNA-Binding ProteinsDNA Topoisomerases, Type IIHeLa CellsHerpesvirus 4, HumanHumansLamin Type AMembrane ProteinsMultiprotein ComplexesNuclear LaminaPhosphorylationProtein KinasesProtein Serine-Threonine KinasesViral ProteinsVirionAdenosine TriphosphatasesAntigens, NeoplasmBFRF1 protein, Human herpesvirus 4BGLF4 protein, Epstein-Barr viruscondensin complexesDNA-Binding ProteinsDNA Topoisomerases, Type IIlamin CLamin Type AMembrane ProteinsMultiprotein ComplexesProtein KinasesProtein Serine-Threonine KinasesUL13 protein, SimplexvirusViral Proteins

Identifiers

PMID18815303
PMCPMC2583647
OpenAlexW2121353617

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.