ArticleBiophysical journal2012
Investigation of Ebola VP40 assembly and oligomerization in live cells using number and brightness analysis.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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.
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.
Who cites it
49 citing papers in PubMed.
- Self-adjuvanting Ebola virus-like particles that incorporate a cellular interferon-inducing domain.Research square · 2026Article
- Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 2025Article
- Investigating the effects of temporal correlation on accurate molecular brightness determination.Biophysical journal · 2025Article
- Marburg virus exploits the Rab11-mediated endocytic pathway in viral-particle production.Microbiology spectrum · 2024Article
- Impact of Ebola virus nucleoprotein on VP40 virus-like particle production: a computational approach.Communications biology · 2024Article
- Evaluation of fendiline treatment in VP40 system with nucleation-elongation process: a computational model of Ebola virus matrix protein assembly.Microbiology spectrum · 2024Article
- Minor changes in electrostatics robustly increase VP40 membrane binding, assembly, and budding of Ebola virus matrix protein derived virus-like particles.bioRxiv : the preprint server for biology · 2024Article
- Elucidating Residue-Level Determinants Affecting Dimerization of Ebola Virus Matrix Protein Using High-Throughput Site Saturation Mutagenesis and Biophysical Approaches.The journal of physical chemistry. B · 2023Article
- Cheminformatics-Based Study Identifies Potential Ebola VP40 Inhibitors.International journal of molecular sciences · 2023Article
- Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.EMBO reports · 2022Article
- Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.Science advances · 2022Article
- Mechanisms of phosphatidylserine influence on viral production: A computational model of Ebola virus matrix protein assembly.The Journal of biological chemistry · 2022Article
- Development of an imaging system for visualization of Ebola virus glycoprotein throughout the viral lifecycle.Frontiers in microbiology · 2022Article
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
- Negative-sense RNA viruses: An underexplored platform for examining virus-host lipid interactions.Molecular biology of the cell · 2021Review
- Article
- Oligomerization and Cell Egress Controlled by Two Microdomains of Canine Distemper Virus Matrix Protein.mSphere · 2021Article
- Article
- A Conserved Tryptophan in the Ebola Virus Matrix Protein C-Terminal Domain Is Required for Efficient Virus-Like Particle Formation.Pathogens (Basel, Switzerland) · 2020Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Ebola virus assembles and buds from the inner leaflet of the plasma membrane of mammalian cells, which is primarily attributed to its major matrix protein VP40. Oligomerization of VP40 has been shown to be essential to the life cycle of the virus including formation of virions from infected cells. To date, VP40 oligomerization has mainly been assessed by chemical cross-linking following cell fractionation studies with VP40 transfected cells. This has made it difficult to discern the spatial and temporal dynamics of VP40 oligomerization. To gain a better understanding of the VP40 assembly and oligomerization process in live cells, we have employed real-time imaging of enhanced green fluorescent protein tagged VP40. Here, we use both confocal and total internal reflection microscopy coupled with number and brightness analysis to show that VP40 oligomers are localized on the plasma membrane and are highly enriched at sites of membrane protrusion, consistent with sites of viral budding. These filamentous plasma membrane protrusion sites harbor VP40 hexamers, octamers, and higher order oligomers. Consistent with previous reports, abrogation of VP40 oligomerization through mutagenesis greatly diminished VP40 egress and also abolished membrane protrusion sites enriched with VP40. In sum, real-time single-molecule imaging of fluorescently labeled Ebola VP40 is able to resolve the spatial and temporal dynamics of VP40 oligomerization.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.