Evidence map›Paper›PMID 17699575›Full record

ArticleJournal of virology2007

Protein kinase CK2 phosphorylation of EB2 regulates its function in the production of Epstein-Barr virus infectious viral particles.

Cahora Medina-Palazon, Henri Gruffat, Fabrice Mure, Odile Filhol, Valérie Vingtdeux-Didier, Hervé Drobecq, Claude Cochet, Nicolas Sergeant, Alain Sergeant, Evelyne Manet

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Post-Translational Modifications of TOE3 Regulate Antiviral Defense in Tobacco.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  18. Kaposi's sarcoma-associated herpesvirus ORF57 in viral RNA processing.Frontiers in bioscience (Landmark edition) · 2009
    Review
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 6 institutions in 1 country.

Cahora Medina-PalazonINSERM U758, ENS-Lyon, 46 allée d'Italie, 69364 Lyon Cedex 07, France.
Henri Gruffat
Fabrice Mure
Odile Filhol
Valérie Vingtdeux-Didier
Hervé Drobecq
Claude Cochet
Nicolas Sergeant
Alain Sergeant
Evelyne Manet
École Normale Supérieure de Lyon · FRCentre de Recherche Jean Pierre Aubert · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FRInstitut de Recherches en Technologies et Sciences pour le Vivant · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Epstein-Barr Virus (EBV) early protein EB2 (also called BMLF1, Mta, or SM) promotes the nuclear export of a subset of early and late viral mRNAs and is essential for the production of infectious virions. We show here that in vitro, protein kinase CK2alpha and -beta subunits bind both individually and, more efficiently, as a complex to the EB2 N terminus and that the CK2beta regulatory subunit also interacts with the EB2 C terminus. Immunoprecipitated EB2 has CK2 activity that phosphorylates several sites within the 80 N-terminal amino acids of EB2, including Ser-55, -56, and -57, which are localized next to the nuclear export signal. EB2S3E, the phosphorylation-mimicking mutant of EB2 at these three serines, but not the phosphorylation ablation mutant EB2S3A, efficiently rescued the production of infectious EBV particles by HEK293(BMLF1-KO) cells harboring an EB2-defective EBV genome. The defect of EB2S3A in transcomplementing 293(BMLF1-KO) cells was not due to impaired nucleocytoplasmic shuttling of the mutated protein but was associated with a decrease in the cytoplasmic accumulation of several late viral mRNAs. Thus, EB2-mediated production of infectious EBV virions is regulated by CK2 phosphorylation at one or more of the serine residues Ser-55, -56, and -57.

Indexed as

Amino Acid SequenceCasein Kinase IICell LineCytoplasmGlutathione TransferaseHeLa CellsHumansMolecular Sequence DataPhosphoproteinsPhosphorylationPlasmidsProtein Structure, TertiarySequence Homology, Amino AcidSerineTrans-ActivatorsTransfectionCasein Kinase IIGlutathione TransferasePhosphoproteinsSerineSM protein, Human herpesvirus 4Trans-ActivatorsViral Proteins

Identifiers

PMID17699575
PMCPMC2168784
OpenAlexW2140662587

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.