Evidence map›Paper›PMID 39293445›Full record

ArticleCell2024

Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.

Reika Watanabe, Dawid Zyla, Diptiben Parekh, Connor Hong, Ying Jones, Sharon L Schendel, William Wan, Guillaume Castillon, Erica Ollmann Saphire

Abstract read
In one paragraph

Article in Cell, 2024. 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
–field-weighted citation impact
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.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. bioRxiv : the preprint server for biology · 2024
    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

9 authors.

Reika WatanabeCenter for Vaccine Innovation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
Dawid ZylaCenter for Vaccine Innovation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
Diptiben ParekhCenter for Vaccine Innovation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
Connor HongCenter for Vaccine Innovation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
Ying JonesElectron Microscopy Core, University of California, San Diego, La Jolla, CA 92037, USA.
Sharon L SchendelCenter for Vaccine Innovation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
William WanVanderbilt University Center for Structural Biology, Nashville, TN 37235, USA.
Guillaume CastillonElectron Microscopy Core, University of California, San Diego, La Jolla, CA 92037, USA.
Erica Ollmann SaphireCenter for Vaccine Innovation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA; Department of Medicine, University of California, San Diego, La Jolla, CA 92037, USA. Electronic address: erica@lji.org.

Funding

Filovirus nucleocapsid assembly, caught in the act, by in situ structural biologyR21AI180801 · NIAID · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI SAPHIRE, ERICA OLLMANN · 2024 to 2025
$503k
NIAID NIH HHS R21 AI180801
6 · The paper itself

Abstract

Filoviruses, including the Ebola and Marburg viruses, cause hemorrhagic fevers with up to 90% lethality. The viral nucleocapsid is assembled by polymerization of the nucleoprotein (NP) along the viral genome, together with the viral proteins VP24 and VP35. We employed cryo-electron tomography of cells transfected with viral proteins and infected with model Ebola virus to illuminate assembly intermediates, as well as a 9 Å map of the complete intracellular assembly. This structure reveals a previously unresolved third and outer layer of NP complexed with VP35. The intrinsically disordered region, together with the C-terminal domain of this outer layer of NP, provides the constant width between intracellular nucleocapsid bundles and likely functions as a flexible tether to the viral matrix protein in the virion. A comparison of intracellular nucleocapsids with prior in-virion nucleocapsid structures reveals that the nucleocapsid further condenses vertically in the virion. The interfaces responsible for nucleocapsid assembly are highly conserved and offer targets for broadly effective antivirals.

Indexed as

EbolavirusElectron Microscope TomographyNucleocapsidVirus AssemblyAnimalsChlorocebus aethiopsCryoelectron MicroscopyHemorrhagic Fever, EbolaHumansModels, MolecularNucleocapsid ProteinsNucleoproteinsViral ProteinsVirionNucleocapsid ProteinsNucleoproteinsViral ProteinsVP24 protein, Ebola virusantiviralcorrelative light and electron microscopycryo-electron tomographyEbola virusfilovirusfocused-ion beam millingimmune suppressorin situ structural biologyintegrative modelingMononegaviralesnucleocapsidnucleoproteinphosphoproteinsubtomogram averagingvirus assemblyvirus pathogenesisvirus structure

Identifiers

PMID39293445
PMCPMC11455616

What OpenQuestion holds

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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.