Evidence map›Paper›PMID 37082863›Full record

ArticleThe EMBO journal2023

The Ebola virus VP40 matrix layer undergoes endosomal disassembly essential for membrane fusion.

Sophie L Winter, Gonen Golani, Fabio Lolicato, Melina Vallbracht, Keerthihan Thiyagarajah, Samy Sid Ahmed, Christian Lüchtenborg, Oliver T Fackler, Britta Brügger, Thomas Hoenen and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.1field-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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. How endosomal PIKfyve inhibition prevents viral membrane fusion and entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  11. A novelMicrobiology spectrum · 2023
    Article
  12. Article
  13. Review
  14. Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023
    Review
  15. Article
  16. Article
  17. Article
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

13 authors at 3 institutions in 3 countries.

Sophie L WinterSchaller Research Groups, Department of Infectious Diseases, Virology, University Hospital Heidelberg, Heidelberg, Germany.ORCID 0000-0001-6099-7314
Gonen GolaniBioQuant-Center for Quantitative Biology, Heidelberg University, Heidelberg, Germany.ORCID 0000-0003-4792-6807
Fabio LolicatoHeidelberg University Biochemistry Center, Heidelberg, Germany.ORCID 0000-0001-7537-0549
Melina VallbrachtSchaller Research Groups, Department of Infectious Diseases, Virology, University Hospital Heidelberg, Heidelberg, Germany.
Keerthihan ThiyagarajahSchaller Research Groups, Department of Infectious Diseases, Virology, University Hospital Heidelberg, Heidelberg, Germany.ORCID 0000-0002-1381-8093
Samy Sid AhmedDepartment of Infectious Diseases, Integrative Virology, University Hospital Heidelberg, Heidelberg, Germany.
Christian LüchtenborgHeidelberg University Biochemistry Center, Heidelberg, Germany.
Oliver T FacklerDepartment of Infectious Diseases, Integrative Virology, University Hospital Heidelberg, Heidelberg, Germany.ORCID 0000-0003-2982-4209
Britta BrüggerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Thomas HoenenInstitute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Insitut, Greifswald-Insel Riems, Greifswald, Germany.ORCID 0000-0002-5829-6305
Walter NickelHeidelberg University Biochemistry Center, Heidelberg, Germany.ORCID 0000-0002-6496-8286
Ulrich S SchwarzBioQuant-Center for Quantitative Biology, Heidelberg University, Heidelberg, Germany.ORCID 0000-0003-1483-640X
Petr ChlandaSchaller Research Groups, Department of Infectious Diseases, Virology, University Hospital Heidelberg, Heidelberg, Germany.ORCID 0000-0002-7782-2139
Heidelberg University · DEFriedrich-Loeffler-Institut · DEUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ebola viruses (EBOVs) assemble into filamentous virions, whose shape and stability are determined by the matrix viral protein 40 (VP40). Virus entry into host cells occurs via membrane fusion in late endosomes; however, the mechanism of how the remarkably long virions undergo uncoating, including virion disassembly and nucleocapsid release into the cytosol, remains unknown. Here, we investigate the structural architecture of EBOVs entering host cells and discover that the VP40 matrix disassembles prior to membrane fusion. We reveal that VP40 disassembly is caused by the weakening of VP40-lipid interactions driven by low endosomal pH that equilibrates passively across the viral envelope without a dedicated ion channel. We further show that viral membrane fusion depends on VP40 matrix integrity, and its disassembly reduces the energy barrier for fusion stalk formation. Thus, pH-driven structural remodeling of the VP40 matrix acts as a molecular switch coupling viral matrix uncoating to membrane fusion during EBOV entry.

Indexed as

EbolavirusHemorrhagic Fever, EbolaEndosomesHumansMembrane FusionNucleoproteinsViral Core ProteinsViral Matrix ProteinsNucleoproteinsnucleoprotein VP40, Ebola virusViral Core ProteinsViral Matrix ProteinsEbola virusin situ cryo-ETmembrane fusionmembrane modeling and molecular dynamics simulationsvirus entry and uncoating

Identifiers

PMID37082863
PMCPMC10233383
OpenAlexW4366603629

What Socratic 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 Socratic graph.