Evidence map›Paper›PMID 32978151›Full record

ArticleScience advances2020

The prefusion structure of herpes simplex virus glycoprotein B.

B Vollmer, V Pražák, D Vasishtan, E E Jefferys, A Hernandez-Duran, M Vallbracht, B G Klupp, T C Mettenleiter, M Backovic, F A Rey and 2 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 91 citations in OpenAlex.

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  13. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
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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

12 authors at 5 institutions in 3 countries.

B VollmerOxford Particle Imaging Centre, Department of Structural Biology, Wellcome Centre Human Genetics, University of Oxford, Oxford, UK.ORCID 0000-0002-7526-0582
V PražákOxford Particle Imaging Centre, Department of Structural Biology, Wellcome Centre Human Genetics, University of Oxford, Oxford, UK.ORCID 0000-0001-8149-218X
D VasishtanOxford Particle Imaging Centre, Department of Structural Biology, Wellcome Centre Human Genetics, University of Oxford, Oxford, UK.
E E JefferysDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0002-0097-0520
A Hernandez-DuranInstitute of Structural and Molecular Biology, Birkbeck, London, UK.
M VallbrachtFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Insel Riems, Germany.ORCID 0000-0002-3619-3663
B G KluppFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Insel Riems, Germany.
T C MettenleiterFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Insel Riems, Germany.
M BackovicInstitut Pasteur, Structural Virology Unit, Department of Virology, Paris, France.ORCID 0000-0001-8814-4428
F A ReyInstitut Pasteur, Structural Virology Unit, Department of Virology, Paris, France.ORCID 0000-0002-9953-7988
M TopfInstitute of Structural and Molecular Biology, Birkbeck, London, UK.ORCID 0000-0002-8185-1215
K GrünewaldOxford Particle Imaging Centre, Department of Structural Biology, Wellcome Centre Human Genetics, University of Oxford, Oxford, UK. kay.gruenewald@cssb-hamburg.de.ORCID 0000-0002-4788-2691
Centre for Human Genetics · GBFriedrich-Loeffler-Institut · DEInstitute of Structural and Molecular Biology · GBInstitut Pasteur · FRUniversity of Oxford · GB

Funding

Medical Research Council MR/M019292/1Medical Research Council MR/R017875/1
6 · The paper itself

Abstract

Cell entry of enveloped viruses requires specialized viral proteins that mediate fusion with the host membrane by substantial structural rearrangements from a metastable pre- to a stable postfusion conformation. This metastability renders the herpes simplex virus 1 (HSV-1) fusion glycoprotein B (gB) highly unstable such that it readily converts into the postfusion form, thereby precluding structural elucidation of the pharmacologically relevant prefusion conformation. By identification of conserved sequence signatures and molecular dynamics simulations, we devised a mutation that stabilized this form. Functionally locking gB allowed the structural determination of its membrane-embedded prefusion conformation at sub-nanometer resolution and enabled the unambiguous fit of all ectodomains. The resulting pseudo-atomic model reveals a notable conservation of conformational domain rearrangements during fusion between HSV-1 gB and the vesicular stomatitis virus glycoprotein G, despite their very distant phylogeny. In combination with our comparative sequence-structure analysis, these findings suggest common fusogenic domain rearrangements in all class III viral fusion proteins.

Indexed as

Herpes SimplexHerpesvirus 1, HumanHumansModels, MolecularProtein ConformationVirus Internalization

Identifiers

PMID32978151
PMCPMC7518877
OpenAlexW3087974086

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.