Evidence map›Paper›PMID 19158247›Full record

ArticleJournal of virology2009

Self-assembly of Epstein-Barr virus capsids.

Brandon W Henson, Edward M Perkins, Jonathan E Cothran, Prashant Desai

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 15% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

  1. Pooled it
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  8. Review
  9. The autophagy machinery interacts with EBV capsids during viral envelope release.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Regulation of Epstein-Barr Virus Minor Capsid Protein BORF1 by TRIM5α.International journal of molecular sciences · 2022
    Article
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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

4 authors at 2 institutions in 1 country.

Brandon W HensonViral Oncology Program, The Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University, 353 CRB1 Viral Oncology, 1650 New Orleans St., Baltimore, MD 21117, USA.
Edward M Perkins
Jonathan E Cothran
Prashant Desai
Sidney Kimmel Comprehensive Cancer Center · USImaging Center · US

Funding

MOLECULAR GENETICS OF HSV-1 CAPSIDSR01AI033077 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DESAI, PRASHANT · 1994 to 2007
$2.5M
Maturation functions of the HSV-1 tegumentR01AI061382 · NIAID · JOHNS HOPKINS UNIVERSITY · PI DESAI, PRASHANT J · 2006 to 2010
$1.8M
NIAID NIH HHS AI0333077NIAID NIH HHS AI061382NIAID NIH HHS R01 AI033077NIAID NIH HHS R01 AI061382
6 · The paper itself

Abstract

Epstein-Barr virus (EBV), a member of the Gammaherpesvirus family, primarily infects B lymphocytes and is responsible for a number of lymphoproliferative diseases. The molecular genetics of the assembly pathway and high-resolution structural analysis of the capsid have not been determined for this lymphocryptovirus. As a first step in studying EBV capsid assembly, the baculovirus expression vector (BEV) system was used to express the capsid shell proteins BcLF1 (major capsid protein), BORF1 (triplex protein), BDLF1 (triplex protein), and BFRF3 (small capsid protein); the internal scaffold protein, BdRF1; and the maturational protease (BVRF2). Coinfection of insect cells with the six viruses expressing these proteins resulted in the production of closed capsid structures as judged by electron microscopy and sedimentation methods. Therefore, as shown for other herpesviruses, only six proteins are required for EBV capsid assembly. Furthermore, the small capsid protein of EBV (BFRF3), like that of Kaposi's sarcoma-associated herpesvirus, was found to be required for assembly of a stable structure. Localization of the small capsid protein to nuclear assembly sites required both the major capsid (BcLF1) and scaffold proteins (BdRF1) but not the triplex proteins. Mutational analysis of BFRF3 showed that the N-terminal half (amino acids 1 to 88) of this polypeptide is required and sufficient for capsid assembly. A region spanning amino acids 65 to 88 is required for the concentration of BFRF3 at a subnuclear site and the N-terminal 65 amino acids contain the sequences required for interaction with major capsid protein. These studies have identified the multifunctional role of the gammaherpesvirus small capsid proteins.

Indexed as

Virus AssemblyAnimalsBaculoviridaeCapsidCapsid ProteinsCell LineCentrifugation, Density GradientDNA Mutational AnalysisHerpesvirus 4, HumanMicroscopy, Electron, TransmissionProtein BindingProtein Interaction MappingSpodopteraCapsid Proteins

Identifiers

PMID19158247
PMCPMC2663254
OpenAlexW2154010136

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.