Evidence map›Paper›PMID 35215889›Full record

ReviewViruses2022

Well Put Together-A Guide to Accessorizing with the Herpesvirus gH/gL Complexes.

Gonzalo L Gonzalez-Del Pino, Ekaterina E Heldwein

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2022. 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
4.2field-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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Allosteric mechanism of membrane fusion activation in a herpesvirus.bioRxiv : the preprint server for biology · 2024
    Article
  13. Article
  14. Article
  15. Article
  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

2 authors at 1 institution in 1 country.

Gonzalo L Gonzalez-Del PinoDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.ORCID 0000-0002-0365-8583
Ekaterina E HeldweinDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.ORCID 0000-0003-3113-6958
Tufts University · 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
In-vitro analysis of HSV-1 membrane fusion mechanismR21AI160821 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2021 to 2022
$455k
Dissection of HSV-1 entry mechanisms using VSV pseudotype platformR21AI140711 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2018 to 2019
$454k
Single-particle analysis of HSV-1 membrane fusion mechanismR21AI145272 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2020 to 2021
$453k
NIAID NIH HHS K12 GM133314NIAID NIH HHS R01 AI164698NIAID NIH HHS R21 AI140711NIAID NIH HHS R21 AI145272NIAID NIH HHS R21 AI160821NIGMS NIH HHS K12 GM133314
6 · The paper itself

Abstract

Herpesviruses are enveloped, double-stranded DNA viruses that infect a variety of hosts across the animal kingdom. Nine of these establish lifelong infections in humans, for which there are no cures and few vaccine or treatment options. Like all enveloped viruses, herpesviruses enter cells by fusing their lipid envelopes with a host cell membrane. Uniquely, herpesviruses distribute the functions of receptor engagement and membrane fusion across a diverse cast of glycoproteins. Two glycoprotein complexes are conserved throughout the three herpesvirus subfamilies: the trimeric gB that functions as a membrane fusogen and the heterodimeric gH/gL, the role of which is less clearly defined. Here, we highlight the conserved and divergent functions of gH/gL across the three subfamilies of human herpesviruses by comparing its interactions with a broad range of accessory viral proteins, host cell receptors, and neutralizing or inhibitory antibodies. We propose that the intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a "trigger" signal that activates the fusogenic ability of gB.

Indexed as

Antibodies, NeutralizingGlycoproteinsHerpesviridaeHumansProtein BindingProtein ConformationReceptors, VirusViral Envelope ProteinsViral Regulatory and Accessory ProteinsVirus InternalizationAntibodies, NeutralizingGlycoproteinsReceptors, VirusViral Envelope ProteinsViral Regulatory and Accessory ProteinsgH/gLglycoproteinsherpesvirusesmembrane fusionviral entry

Identifiers

PMID35215889
PMCPMC8874593
OpenAlexW4210336291

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.