Evidence map›Paper›PMID 30068640›Full record

ArticleJournal of virology2018

Epstein-Barr Virus-Induced Nodules on Viral Replication Compartments Contain RNA Processing Proteins and a Viral Long Noncoding RNA.

Richard Park, George Miller

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Richard ParkDepartment of Molecular Biophysics, Yale University School of Medicine, New Haven, Connecticut, USA.
George MillerDepartment of Molecular Biophysics, Yale University School of Medicine, New Haven, Connecticut, USA george.miller@yale.edu.
Yale University · US

Funding

VIRAL SMALL RNPS--ROLES IN CELL TRANSFORMATIONP01CA016038 · NCI · YALE UNIVERSITY · PI DIMAIO, DANIEL C. · 1985 to 2020
$25.6M
STUDIES OF EPSTEIN-BARR VIRUSR37CA012055 · NCI · YALE UNIVERSITY · PI MILLER, I. GEORGE · 1989 to 2012
$4.4M
STUDIES OF EPSTEIN-BARR VIRUSR01CA012055 · NCI · YALE UNIVERSITY · PI MILLER, I. GEORGE · 1985 to 2002
$737k
A super-resolution microscope for research and educationS10OD020142 · OD · YALE UNIVERSITY · PI NATHANSON, MICHAEL H · 2015 to 2015
$600k
NCI NIH HHS P01 CA016038NCI NIH HHS R01 CA012055NCI NIH HHS R37 CA012055NIH HHS S10 OD020142
6 · The paper itself

Abstract

Profound alterations in host cell nuclear architecture accompany the lytic phase of Epstein-Barr virus (EBV) infection. Viral replication compartments assemble, host chromatin marginalizes to the nuclear periphery, cytoplasmic poly(A)-binding protein translocates to the nucleus, and polyadenylated mRNAs are sequestered within the nucleus. Virus-induced changes to nuclear architecture that contribute to viral host shutoff (VHS) must accommodate selective processing and export of viral mRNAs. Here we describe additional previously unrecognized nuclear alterations during EBV lytic infection in which viral and cellular factors that function in pre-mRNA processing and mRNA export are redistributed. Early during lytic infection, before formation of viral replication compartments, two cellular pre-mRNA splicing factors, SC35 and SON, were dispersed from interchromatin granule clusters, and three mRNA export factors, Y14, ALY, and NXF1, were depleted from the nucleus. During late lytic infection, virus-induced nodular structures (VINORCs) formed at the periphery of viral replication compartments. VINORCs were composed of viral (BMLF1 and BGLF5) and cellular (SC35, SON, SRp20, and NXF1) proteins that mediate pre-mRNA processing and mRNA export. BHLF1 long noncoding RNA was invariably found in VINORCs. VINORCs did not contain other nodular nuclear cellular proteins (PML or coilin), nor did they contain viral proteins (BRLF1 or BMRF1) found exclusively within replication compartments. VINORCs are novel EBV-induced nuclear structures. We propose that EBV-induced dispersal and depletion of pre-mRNA processing and mRNA export factors during early lytic infection contribute to VHS; subsequent relocalization of these pre-mRNA processing and mRNA export proteins to VINORCs and viral replication compartments facilitates selective processing and export of viral mRNAs.

Indexed as

Virus ReplicationCell NucleusHEK293 CellsHerpesvirus 4, HumanHumansMicroscopy, FluorescenceRNA, Long NoncodingRNA, ViralViral ProteinsRNA, Long NoncodingRNA, ViralViral ProteinsBMLF1Epstein-Barr virusnuclear organizationNXF1RNA exportRNA processingSC35SONSRp20viral host shutoff

Identifiers

PMID30068640
PMCPMC6158406
OpenAlexW2883250072

What OpenQuestion holds

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Registered trials

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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.