ArticleViruses2020
Real-Time Analysis of Individual Ebola Virus Glycoproteins Reveals Pre-Fusion, Entry-Relevant Conformational Dynamics.
Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Molecular basis for the increased fusion activity of the Ebola virus glycoprotein epidemic variant A82V: Insights from simulations and experiments.Cell reports · 2025Article
- Identification of Filovirus Entry Inhibitors from Marine Fungus-Derived Indole Alkaloids.Marine drugs · 2025Article
- Single-molecule imaging reveals allosteric stimulation of SARS-CoV-2 spike receptor binding domain by host sialic acid.Science advances · 2024Article
- Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.ACS infectious diseases · 2024Article
- Regulation of Ebola GP conformation and membrane binding by the chemical environment of the late endosome.PLoS pathogens · 2023Article
- A novelMicrobiology spectrum · 2023Article
- Viral Membrane Fusion: A Dance Between Proteins and Lipids.Annual review of virology · 2023Review
- Detergent modulates the conformational equilibrium of SARS-CoV-2 Spike during cryo-EM structural determination.Nature communications · 2023Article
- Article
- Antibody affinity as a driver of signal generation in a paper-based immunoassay for Ebola virus surveillance.Analytical and bioanalytical chemistry · 2021Article
- Identification of filovirus entry inhibitors targeting the endosomal receptor NPC1 binding site.Antiviral research · 2021Article
- Review
- Review
- Comparisons of Antibody Populations in Different Pre-Fusion F VLP-Immunized Cotton Rat Dams and Their Offspring.Vaccines · 2020Article
- Conformational changes in the Ebola virus membrane fusion machine induced by pH, Ca2+, and receptor binding.PLoS biology · 2020Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The Ebola virus (EBOV) envelope glycoprotein (GP) mediates the fusion of the virion membrane with the membrane of susceptible target cells during infection. While proteolytic cleavage of GP by endosomal cathepsins and binding of the cellular receptor Niemann-Pick C1 protein (NPC1) are essential steps for virus entry, the detailed mechanisms by which these events promote membrane fusion remain unknown. Here, we applied single-molecule Förster resonance energy transfer (smFRET) imaging to investigate the structural dynamics of the EBOV GP trimeric ectodomain, and the functional transmembrane protein on the surface of pseudovirions. We show that in both contexts, pre-fusion GP is dynamic and samples multiple conformations. Removal of the glycan cap and NPC1 binding shift the conformational equilibrium, suggesting stabilization of conformations relevant to viral fusion. Furthermore, several neutralizing antibodies enrich alternative conformational states. This suggests that these antibodies neutralize EBOV by restricting access to GP conformations relevant to fusion. This work demonstrates previously unobserved dynamics of pre-fusion EBOV GP and presents a platform with heightened sensitivity to conformational changes for the study of GP function and antibody-mediated neutralization.
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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.