Evidence map›Paper›PMID 26753796›Full record

ArticleScientific reports2016

The Ebola Virus matrix protein, VP40, requires phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) for extensive oligomerization at the plasma membrane and viral egress.

Kristen A Johnson, Geoffrey J F Taghon, Jordan L Scott, Robert V Stahelin

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Review
  2. Secreted Nonstructural Protein 3 is a Pathogenic Determinant of Orbivirus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. PIPScience advances · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Role of phosphatidic acid lipids on plasma membrane association of the Ebola virus matrix protein VP40.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Article
  9. Review
  10. The "basics" of HIV-1 assembly.PLoS pathogens · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

4 authors.

Kristen A JohnsonDepartment of Chemistry and Biochemistry, the Eck Institute for Global Health, and the Boler-Parseghian Center for Rare and Neglected Diseases, University of Notre Dame, Notre Dame, Indiana, 46556.
Geoffrey J F TaghonDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, South Bend, Indiana 46617.
Jordan L ScottDepartment of Chemistry and Biochemistry, the Eck Institute for Global Health, and the Boler-Parseghian Center for Rare and Neglected Diseases, University of Notre Dame, Notre Dame, Indiana, 46556.
Robert V StahelinDepartment of Chemistry and Biochemistry, the Eck Institute for Global Health, and the Boler-Parseghian Center for Rare and Neglected Diseases, University of Notre Dame, Notre Dame, Indiana, 46556.

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
LIPID-PROTEIN INTERACTIONS IN VIRAL ASSEMBLY AND VIRUS LIKE PARTICLE FORMATIONR01AI081077 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL · 2009 to 2019
$3.5M
NIAID NIH HHS AI081077NIAID NIH HHS R01 AI081077NIGMS NIH HHS T32 GM075762NIGMS NIH HHS T32GM075762
6 · The paper itself

Abstract

VP40 is one of eight proteins encoded by the Ebola Virus (EBOV) and serves as the primary matrix protein, forming virus like particles (VLPs) from mammalian cells without the need for other EBOV proteins. While VP40 is required for viral assembly and budding from host cells during infection, the mechanisms that target VP40 to the plasma membrane are not well understood. Phosphatidylserine is required for VP40 plasma membrane binding, VP40 hexamer formation, and VLP egress, However, PS also becomes exposed on the outer membrane leaflet at sites of VP40 budding, raising the question of how VP40 maintains an interaction with the plasma membrane inner leaflet when PS is flipped to the opposite side. To address this question, cellular and in vitro assays were employed to determine if phosphoinositides are important for efficient VP40 localization to the plasma membrane. Cellular studies demonstrated that PI(4,5)P2 was an important component of VP40 assembly at the plasma membrane and subsequent virus like particle formation. Additionally, PI(4,5)P2 was required for formation of extensive oligomers of VP40, suggesting PS and PI(4,5)P2 have different roles in VP40 assembly where PS regulates formation of hexamers from VP40 dimers and PI(4,5)P2 stabilizes and/or induces extensive VP40 oligomerization at the plasma membrane.

Indexed as

Protein MultimerizationVirus ReleaseAnimalsCell MembraneChlorocebus aethiopsCOS CellsEbolavirusLipidsNucleoproteinsPhosphatidylinositol 4,5-DiphosphateProtein BindingStatic ElectricityViral Core ProteinsLipidsNucleoproteinsnucleoprotein VP40, Ebola virusPhosphatidylinositol 4,5-DiphosphateViral Core Proteins

Identifiers

PMID26753796
PMCPMC4709572

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Registered trials

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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.