ArticleJournal of virology2014
Ebolavirus entry requires a compact hydrophobic fist at the tip of the fusion loop.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Molecular basis for the increased fusion activity of the Ebola virus glycoprotein epidemic variant A82V: Insights from simulations and experiments.Cell reports · 2025Article
- Exploring the influence of anionic lipids in the host cell membrane on viral fusion.Biochemical Society transactions · 2024Review
- Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.ACS infectious diseases · 2024Article
- A Salt Bridge and Disulfide Bond within the Lassa Virus Fusion Domain Are Required for the Initiation of Membrane Fusion.ACS omega · 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
- Structure of the Inmazeb cocktail and resistance to Ebola virus escape.Cell host & microbe · 2023Article
- TIM-1 Augments Cellular Entry of Ebola Virus Species and Mutants, Which Is Blocked by Recombinant TIM-1 Protein.Microbiology spectrum · 2022Article
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Filovirus Neutralising Antibodies: Mechanisms of Action and Therapeutic Application.Pathogens (Basel, Switzerland) · 2021Review
- Lysosomal ion channels involved in cellular entry and uncoating of enveloped viruses: Implications for therapeutic strategies against SARS-CoV-2.Cell calcium · 2021Review
- Article
- Ebola virus glycoprotein interacts with cholesterol to enhance membrane fusion and cell entry.Nature structural & molecular biology · 2021Article
- Article
- An exploration of conditions proposed to trigger the Ebola virus glycoprotein for fusion.PloS one · 2019Article
- Growth-Adaptive Mutations in the Ebola Virus Makona Glycoprotein Alter Different Steps in the Virus Entry Pathway.Journal of virology · 2018Article
- Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop.Nature communications · 2018Article
- All-atom virus simulations.Current opinion in virology · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
unlabelledEbolavirus is an enveloped virus causing severe hemorrhagic fever. Its surface glycoproteins undergo proteolytic cleavage and rearrangements to permit membrane fusion and cell entry. Here we focus on the glycoprotein's internal fusion loop (FL), critical for low-pH-triggered fusion in the endosome. Alanine mutations at L529 and I544 and particularly the L529 I544 double mutation compromised viral entry and fusion. The nuclear magnetic resonance (NMR) structures of the I544A and L529A I544A mutants in lipid environments showed significant disruption of a three-residue scaffold that is required for the formation of a consolidated fusogenic hydrophobic surface at the tip of the FL. Biophysical experiments and molecular simulation revealed the position of the wild-type (WT) FL in membranes and showed the inability of the inactive double mutant to reach this position. Consolidation of hydrophobic residues at the tip of FLs may be a common requirement for internal FLs of class I, II, and III fusion proteins. IMPORTANCE: Many class I, II, and III viral fusion proteins bear fusion loops for target membrane insertion and fusion. We determined structures of the Ebolavirus fusion loop and found residues critical for forming a consolidated hydrophobic surface, membrane insertion, and viral entry.
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