Evidence map›Paper›PMID 28611252›Full record

ArticlemBio2017

The Primary Enveloped Virion of Herpes Simplex Virus 1: Its Role in Nuclear Egress.

William W Newcomb, Juan Fontana, Dennis C Winkler, Naiqian Cheng, J Bernard Heymann, Alasdair C Steven

Open access · goldAbstract read
In one paragraph

Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

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  14. High resolution electron tomography and segmentation-by-modeling interpretation in Bsoft.Protein science : a publication of the Protein Society · 2021
    Article
  15. Nuclear Egress.Current issues in molecular biology · 2021
    Review
  16. Article
  17. Article
  18. 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

6 authors at 2 institutions in 2 countries.

William W NewcombLaboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Juan FontanaAstbury Centre for Structural Molecular Biology and Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-9084-2927
Dennis C WinklerLaboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Naiqian ChengLaboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.
J Bernard HeymannLaboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Alasdair C StevenLaboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA stevena@mail.nih.gov.
National Institutes of Health · USUniversity of Leeds · GB

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
STRUCTURAL BIOLOGY OF VIRUS ASSEMBLYZ01AR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 1987 to 2008
$3.0M
Intramural NIH HHS Z01 AR027002NIAMS NIH HHS Z01 AR027002
6 · The paper itself

Abstract

Many viruses migrate between different cellular compartments for successive stages of assembly. The HSV-1 capsid assembles in the nucleus and then transfers into the cytoplasm. First, the capsid buds through the inner nuclear membrane, becoming coated with nuclear egress complex (NEC) protein. This yields a primary enveloped virion (PEV) whose envelope fuses with the outer nuclear membrane, releasing the capsid into the cytoplasm. We investigated the associated molecular mechanisms by isolating PEVs from US3-null-infected cells and imaging them by cryo-electron microscopy and tomography. (pUS3 is a viral protein kinase in whose absence PEVs accumulate in the perinuclear space.) Unlike mature extracellular virions, PEVs have very few glycoprotein spikes. PEVs are ~20% smaller than mature virions, and the little space available between the capsid and the NEC layer suggests that most tegument proteins are acquired later in the egress pathway. Previous studies have proposed that NEC is organized as hexamers in honeycomb arrays in PEVs, but we find arrays of heptameric rings in extracts from US3-null-infected cells. In a PEV, NEC contacts the capsid predominantly via the pUL17/pUL25 complexes which are located close to the capsid vertices. Finally, the NEC layer dissociates from the capsid as it leaves the nucleus, possibly in response to pUS3-mediated phosphorylation. Overall, nuclear egress emerges as a process driven by a program of multiple weak interactions.

Indexed as

Virus ReleaseAnimalsCapsidCapsid ProteinsCell NucleusChlorocebus aethiopsCryoelectron MicroscopyHerpesvirus 1, HumanNuclear EnvelopePhosphorylationVero CellsViral ProteinsVirionVirus AssemblyCapsid ProteinsViral Proteinscryo-electron microscopycryo-electron tomographyHSV capsidnuclear egressnuclear egress complexnuclear envelopenuclear export

Identifiers

PMID28611252
PMCPMC5472190
OpenAlexW2624757630

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.