Evidence map›Paper›PMID 31694953›Full record

ArticleJournal of virology2020

The Novel Nuclear Targeting and BFRF1-Interacting Domains of BFLF2 Are Essential for Efficient Epstein-Barr Virus Virion Release.

Yu-Ching Dai, Yen-Tzu Liao, Yi-Ting Juan, Yi-Ying Cheng, Mei-Tzu Su, Yu-Zhen Su, Hung-Chun Liu, Ching-Hwa Tsai, Chung-Pei Lee, Mei-Ru Chen

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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

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  11. Nanotechnology Frontiers in γ-Herpesviruses Treatments.International journal of molecular sciences · 2021
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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

10 authors at 2 institutions in 1 country.

Yu-Ching Dai *Graduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Yen-Tzu Liao *Graduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Yi-Ting Juan *Graduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Yi-Ying ChengGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Mei-Tzu SuGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Yu-Zhen SuGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Hung-Chun LiuGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Ching-Hwa TsaiGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Chung-Pei LeeSchool of Nursing, National Taipei University of Nursing and Health Sciences, Taipei, Taiwan.
Mei-Ru ChenGraduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan mrc@ntu.edu.tw.
National Taiwan University · TWNational Taipei University of Nursing and Health Science · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) genomic DNA is replicated and packaged into procapsids in the nucleus to form nucleocapsids, which are then transported into the cytoplasm for tegumentation and final maturation. The process is facilitated by the coordination of the viral nuclear egress complex (NEC), which consists of BFLF2 and BFRF1. By expression alone, BFLF2 is distributed mainly in the nucleus. However, it colocalizes with BFRF1 at the nuclear rim and in cytoplasmic nuclear envelope-derived vesicles in coexpressing cells, suggesting temporal control of the interaction between BFLF2 and BFRF1 is critical for their proper function. The N-terminal sequence of BFLF2 is less conserved than that of alpha- and betaherpesvirus homologs. Here, we found that BFLF2 amino acids (aa) 2 to 102 are required for both nuclear targeting and its interaction with BFRF1. Coimmunoprecipitation and confocal analysis indicated that aa 82 to 106 of BFLF2 are important for its interaction with BFRF1. Three crucial amino acids (R47, K50, and R52) and several noncontinuous arginine and histidine residues within aa 59 to 80 function together as a noncanonical nuclear localization signal (NLS), which can be transferred onto yellow fluorescent protein (YFP)-LacZ for nuclear targeting in an importin β-dependent manner. Virion secretion is defective in 293 cells harboring a BFLF2 knockout EBV bacmid upon lytic induction and is restored by

Indexed as

Amino Acid Sequencebeta KaryopherinsCell LineCell NucleusCytoplasmGlutathione TransferaseHEK293 CellsHeLa CellsHerpesvirus 4, HumanHumansMembrane ProteinsModels, MolecularNuclear EnvelopeNuclear Localization SignalsProtein ConformationSequence Analysis, Proteinbeta KaryopherinsBFRF1 protein, Human herpesvirus 4Glutathione TransferaseMembrane ProteinsNuclear Localization SignalsViral ProteinsBFLF2BFRF1EBVEpstein-Barr virusherpesvirusesimportin betaNLSnuclear egressnuclear egress complexnuclear localization signal

Identifiers

PMID31694953
PMCPMC7000978
OpenAlexW2986573162

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.