Evidence map›Paper›PMID 34696343›Full record

ReviewViruses2021

The Ins and Outs of Herpesviral Capsids: Divergent Structures and Assembly Mechanisms across the Three Subfamilies.

Elizabeth B Draganova, Jonathan Valentin, Ekaterina E Heldwein

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
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  6. Article
  7. Oncolytic human herpesvirus for cancer therapy.Molecular biology reports · 2026
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. 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

3 authors at 2 institutions in 1 country.

Elizabeth B DraganovaDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.ORCID 0000-0003-3697-4774
Jonathan ValentinDepartment of Chemical Engineering, University of Florida, Gainesville, FL 32603, USA.
Ekaterina E HeldweinDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.ORCID 0000-0003-3113-6958
Tufts University · USUniversity of Florida · US

Funding

Tufts IRACDAK12GM133314 · NIGMS · TUFTS UNIVERSITY BOSTON · PI CLAIRE L MOORE, Jamie Lynn Maguire · 2019 to 2026
$8.4M
Structure, antigenicity, and function of HCMV fusogen gBR01AI164698 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2021 to 2025
$3.4M
Biophysical and structural analysis of the herpesviral nuclear budding machineryR01AI147625 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2019 to 2023
$3.0M
In-vitro analysis of HSV-1 membrane fusion mechanismR21AI160821 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2021 to 2022
$455k
Single-particle analysis of HSV-1 membrane fusion mechanismR21AI145272 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2020 to 2021
$453k
Mechanisms of Conformational Dynamics and Inhibition of the HSV-1 Nuclear Egress ComplexK99AI151891 · NIAID · TUFTS UNIVERSITY BOSTON · PI DRAGANOVA, ELIZABETH BENNETT · 2021 to 2022
$174k
Structural Dynamics and Regulation of the HSV-1 Nuclear Egress ComplexF32GM126760 · NIGMS · TUFTS UNIVERSITY BOSTON · PI DRAGANOVA, ELIZABETH BENNETT · 2017 to 2018
$116k
NIAID NIH HHS K99 AI151891NIAID NIH HHS R01 AI147625NIAID NIH HHS R01 AI164698NIAID NIH HHS R21 AI145272NIAID NIH HHS R21 AI160821NIGMS NIH HHS K12 GM133314NIH HHS F32GM126760NIH HHS K12GM133314NIH HHS K99AI151891NIH HHS R01AI147625NIH HHS R01AI164698NIH HHS R21AI145272NIH HHS R21AI160821
6 · The paper itself

Abstract

Human herpesviruses, classified into three subfamilies, are double-stranded DNA viruses that establish lifelong latent infections within most of the world's population and can cause severe disease, especially in immunocompromised people. There is no cure, and current preventative and therapeutic options are limited. Therefore, understanding the biology of these viruses is essential for finding new ways to stop them. Capsids play a central role in herpesvirus biology. They are sophisticated vehicles that shelter the pressurized double-stranded-DNA genomes while ensuring their delivery to defined cellular destinations on the way in and out of the host cell. Moreover, the importance of capsids for multiple key steps in the replication cycle makes their assembly an attractive therapeutic target. Recent cryo-electron microscopy reconstructions of capsids from all three subfamilies of human herpesviruses revealed not only conserved features but also remarkable structural differences. Furthermore, capsid assembly studies have suggested subfamily-specific roles of viral capsid protein homologs. In this review, we compare capsid structures, assembly mechanisms, and capsid protein functions across human herpesvirus subfamilies, highlighting the differences.

Indexed as

CapsidCapsid ProteinsCryoelectron MicroscopyHerpesviridaeHumansViral ProteinsVirionVirus AssemblyVirus ReplicationCapsid ProteinsViral Proteinsassemblycapsidcapsid associated-tegument complex (CATC)herpesvirus

Identifiers

PMID34696343
PMCPMC8539031
OpenAlexW3199720552

What OpenQuestion holds

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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.