Evidence map›Paper›PMID 35767585›Full record

ArticlePLoS pathogens2022

A surface pocket in the cytoplasmic domain of the herpes simplex virus fusogen gB controls membrane fusion.

Zemplen Pataki, Erin K Sanders, Ekaterina E Heldwein

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 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
3.3field-weighted citation impact, top 7% 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, 23 citations in OpenAlex.

  1. Review
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  9. Allosteric mechanism of membrane fusion activation in a herpesvirus.bioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Oncolytic α-herpesvirus and myeloid-tropic cytomegalovirus cooperatively enhance systemic antitumor responses.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
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  15. Review
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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 1 institution in 1 country.

Zemplen PatakiDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts, United States of America.
Erin K SandersGraduate Program in Cellular, Molecular, and Developmental Biology, Graduate School of Biomedical Sciences, Tufts University School of Medicine, Boston, Massachusetts, United States of America.
Ekaterina E HeldweinDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts, United States of America.ORCID 0000-0003-3113-6958
Tufts University · US

Funding

Structure, antigenicity, and function of HCMV fusogen gBR01AI164698 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2021 to 2025
$3.4M
Roles of the cytoplasmic domains of the HSV-1 glycoproteins gH and gB in membrane fusionF30AI161795 · NIAID · TUFTS UNIVERSITY BOSTON · PI PATAKI, ZEMPLEN · 2022 to 2023
$63k
Howard Hughes Medical Institute 55108533NIAID NIH HHS F30 AI161795NIAID NIH HHS R01 AI164698
6 · The paper itself

Abstract

Membrane fusion during the entry of herpesviruses is carried out by the viral fusogen gB that is activated by its partner protein gH in some manner. The fusogenic activity of gB is controlled by its cytoplasmic (or intraviral) domain (gBCTD) and, according to the current model, the gBCTD is a trimeric, inhibitory clamp that restrains gB in the prefusion conformation. But how the gBCTD clamp is released by gH is unclear. Here, we identified two new regulatory elements within gB and gH from the prototypical herpes simplex virus 1: a surface pocket within the gBCTD and residue V831 within the gH cytoplasmic tail. Mutagenesis and structural modeling suggest that gH V831 interacts with the gB pocket. The gB pocket is located above the interface between adjacent protomers, and we hypothesize that insertion of the gH V831 wedge into the pocket serves to push the protomers apart, which releases the inhibitory clamp. In this manner, gH activates the fusogenic activity of gB. Both gB and gH are conserved across all herpesviruses, and this activation mechanism could be used by other gB homologs. Our proposed mechanism emphasizes a central role for the cytoplasmic regions in regulating the activity of a viral fusogen.

Indexed as

Herpes SimplexHerpesvirus 1, HumanHumansMembrane FusionProtein SubunitsViral Envelope ProteinsVirus InternalizationProtein SubunitsViral Envelope Proteins

Identifiers

PMID35767585
PMCPMC9275723
OpenAlexW4283731066

What OpenQuestion holds

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LicenceCC BY
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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.