ReviewFrontiers in microbiology2014
Membrane binding and bending in Ebola VP40 assembly and egress.
Review in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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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.
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Who cites it
47 citing papers in PubMed, 84 citations in OpenAlex.
- Review
- Nanoscale Mechanical and Morphological Characterization of Ebolavirus-like Particles: Implications for Therapeutic Development.International journal of molecular sciences · 2025Article
- Biomechanics Model to Characterize Atomic Force Microscopy-Based Virus-Host Cell Adhesion Measurements.The journal of physical chemistry. B · 2024Article
- Ebola Virus Matrix Protein VP40 Single Mutations G198R and G201R Significantly Enhance Plasma Membrane Localization.The journal of physical chemistry. B · 2024Article
- Article
- Identification of Prospective Ebola Virus VP35 and VP40 Protein Inhibitors from Myxobacterial Natural Products.Biomolecules · 2024Article
- Evaluation of fendiline treatment in VP40 system with nucleation-elongation process: a computational model of Ebola virus matrix protein assembly.Microbiology spectrum · 2024Article
- 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 · 2024Article
- Efficient Estimates of Surface Diffusion Parameters for Spatio-Temporally Resolved Virus Replication Dynamics.International journal of molecular sciences · 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
- The Ebola virus VP40 matrix layer undergoes endosomal disassembly essential for membrane fusion.The EMBO journal · 2023Article
- Cheminformatics-Based Study Identifies Potential Ebola VP40 Inhibitors.International journal of molecular sciences · 2023Article
- Extracellular vesicle storm during the course of Ebola virus infection in primates.Frontiers in cellular and infection microbiology · 2023Article
- Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.EMBO reports · 2022Article
- Structure of the Ebola virus polymerase complex.Nature · 2022Article
- Mechanisms of phosphatidylserine influence on viral production: A computational model of Ebola virus matrix protein assembly.The Journal of biological chemistry · 2022Article
- Algal and Cyanobacterial Lectins and Their Antimicrobial Properties.Marine drugs · 2021Review
- Article
- Negative-sense RNA viruses: An underexplored platform for examining virus-host lipid interactions.Molecular biology of the cell · 2021Review
- Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Lipid-enveloped viruses contain a lipid bilayer coat that protects their genome and helps to facilitate entry into the host cell. Filoviruses are lipid-enveloped viruses that have up to 90% clinical fatality and include Marbug (MARV) and Ebola (EBOV). These pleomorphic filamentous viruses enter the host cell through their membrane-embedded glycoprotein and then replicate using just seven genes encoded in their negative-sense RNA genome. EBOV budding occurs from the inner leaflet of the plasma membrane (PM) and is driven by the matrix protein VP40, which is the most abundantly expressed protein of the virus. VP40 expressed in mammalian cells alone can trigger budding of filamentous virus-like particles (VLPs) that are nearly indistinguishable from authentic EBOV. VP40, such as matrix proteins from other viruses, has been shown to bind anionic lipid membranes. However, how VP40 selectively interacts with the inner leaflet of the PM and assembles into a filamentous lipid enveloped particle is mostly unknown. This article describes what is known regarding VP40 membrane interactions and what answers will fill the gaps.
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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.