Evidence map›Paper›PMID 28528442›Full record

ReviewAdvances in anatomy, embryology, and cell biology2017

Herpesvirus Capsid Assembly and DNA Packaging.

Jason D Heming, James F Conway, Fred L Homa

Open access · greenAbstract readReview
In one paragraph

Review in Advances in anatomy, embryology, and cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
51.8field-weighted citation impact, top 1% 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

118 citing papers in PubMed, 164 citations in OpenAlex.

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58 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

3 authors at 2 institutions in 1 country.

Jason D HemingDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA, 15282, USA.
James F ConwayDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15261, USA.
Fred L HomaDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA, 15282, USA. flhoma@pitt.edu.
Duquesne University · USUniversity of Pittsburgh · US

Funding

Structure and Function of the Herpesvirus Capsid and its DNA-Packaging MachineryR01AI089803 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CONWAY, JAMES F., HOMA, FREDERICK L · 2011 to 2019
$4.0M
Herpes Simplex Virus Capsid Assembly and DNA PackagingR01AI060836 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HOMA, FREDERICK L · 2006 to 2010
$1.6M
Direct electron detecting (DED) cameraS10OD019995 · OD · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CONWAY, JAMES F. · 2015 to 2015
$548k
Uncoating of the Herpes Simplex Virus GenomeR21AI132967 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CONWAY, JAMES F., HOMA, FREDERICK L · 2017 to 2018
$429k
Herpes Simples Virus Capsid Assembly and DNA PackagingR56AI060836 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HOMA, FREDERICK L · 2011 to 2011
$379k
NIAID NIH HHS R01 AI060836NIAID NIH HHS R01 AI089803NIAID NIH HHS R21 AI132967NIAID NIH HHS R56 AI060836NIH HHS S10 OD019995
6 · The paper itself

Abstract

Herpes simplex virus type I (HSV-1) is the causative agent of several pathologies ranging in severity from the common cold sore to life-threatening encephalitic infection. During productive lytic infection, over 80 viral proteins are expressed in a highly regulated manner, resulting in the replication of viral genomes and assembly of progeny virions. The virion of all herpesviruses consists of an external membrane envelope, a proteinaceous layer called the tegument, and an icosahedral capsid containing the double-stranded linear DNA genome. The capsid shell of HSV-1 is built from four structural proteins: a major capsid protein, VP5, which forms the capsomers (hexons and pentons), the triplex consisting of VP19C and VP23 found between the capsomers, and VP26 which binds to VP5 on hexons but not pentons. In addition, the dodecameric pUL6 portal complex occupies 1 of the 12 capsid vertices, and the capsid vertex specific component (CVSC), a heterotrimer complex of pUL17, pUL25, and pUL36, binds specifically to the triplexes adjacent to each penton. The capsid is assembled in the nucleus where the viral genome is packaged into newly assembled closed capsid shells. Cleavage and packaging of replicated, concatemeric viral DNA requires the seven viral proteins encoded by the UL6, UL15, UL17, UL25, UL28, UL32, and UL33 genes. Considerable advances have been made in understanding the structure of the herpesvirus capsid and the function of several of the DNA packaging proteins by applying biochemical, genetic, and structural techniques. This review is a summary of recent advances with respect to the structure of the HSV-1 virion capsid and what is known about the function of the seven packaging proteins and their interactions with each other and with the capsid shell.

Indexed as

DNA PackagingAnimalsCapsidHerpesviridaeHumansViral ProteinsVirionVirus AssemblyViral ProteinsCapsidCryo-Electron MicroscopyCVSCDNA PackagingHerpesvirusHSV-1PRVStructureTriplex

Identifiers

PMID28528442
PMCPMC5548147
OpenAlexW2615860428

What OpenQuestion holds

Textmetadata
LicenceTDM
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.