Evidence map›Paper›PMID 29348171›Full record

ArticleThe Journal of biological chemistry2018

A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine.

Kathryn Del Vecchio, Cary T Frick, Jeevan B Gc, Shun-Ichiro Oda, Bernard S Gerstman, Erica Ollmann Saphire, Prem P Chapagain, Robert V Stahelin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

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  5. 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
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  7. A novelMicrobiology spectrum · 2023
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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

8 authors at 3 institutions in 3 countries.

Kathryn Del VecchioFrom the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556.
Cary T FrickFrom the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556.
Jeevan B Gcthe Department of Physics and.ORCID 0000-0002-3589-0408
Shun-Ichiro Odathe Department of Immunology and Microbiology and.
Bernard S Gerstmanthe Department of Physics and.ORCID 0000-0003-4258-529X
Erica Ollmann Saphirethe Department of Immunology and Microbiology and.ORCID 0000-0002-1206-7451
Prem P Chapagainthe Department of Physics and.ORCID 0000-0002-0999-4975
Robert V StahelinFrom the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, rstaheli@purdue.edu.ORCID 0000-0001-5443-7863
Florida International University · USUniversity of Notre Dame · USScripps Research Institute · US

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
A New System to Modulate Phosphatidylserine to Investigate Filovirus BuddingR21AI121841 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI SCHWARZ, MARGARET A · 2016 to 2017
$416k
NIAID NIH HHS R01 AI081077NIAID NIH HHS R21 AI121841NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

Ebola virus (EBOV) is a filamentous lipid-enveloped virus that causes hemorrhagic fever with a high fatality rate. Viral protein 40 (VP40) is the major EBOV matrix protein and regulates viral budding from the plasma membrane. VP40 is a transformer/morpheein that can structurally rearrange its native homodimer into either a hexameric filament that facilitates viral budding or an RNA-binding octameric ring that regulates viral transcription. VP40 associates with plasma-membrane lipids such as phosphatidylserine (PS), and this association is critical to budding from the host cell. However, it is poorly understood how different VP40 structures interact with PS, what essential residues are involved in this association, and whether VP40 has true selectivity for PS among different glycerophospholipid headgroups. In this study, we used lipid-binding assays, MD simulations, and cellular imaging to investigate the molecular basis of VP40-PS interactions and to determine whether different VP40 structures (

Indexed as

Cell MembraneEbolavirusHEK293 CellsHumansMolecular Dynamics SimulationMutationPhosphatidylserinesProtein BindingProtein DomainsProtein MultimerizationProtein Structure, QuaternaryProtein TransportSubstrate SpecificityViral Matrix ProteinsPhosphatidylserinesViral Matrix ProteinsVP40 protein, virusEbola virusfiloviruslipid-binding proteinoligomerizationphosphatidylserineplasma membraneviral buddingVP40

Identifiers

PMID29348171
PMCPMC5836117
OpenAlexW2783011783

What Socratic holds

Textmetadata
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.