ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 130 citations in OpenAlex.
- A small molecule inhibits Ebola virus entry through glycoprotein stabilization.Nature communications · 2026Article
- Molecular Insights into High-Pathogenicity RNA Viruses.Viruses · 2026Review
- A highly potent nanobody-based bispecific therapeutic provides broad-spectrum protection against ebolavirus.Nature communications · 2026Article
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- A highly potent and broadly accessible bispecific nanobody for the treatment of ebola virus infections.PLoS pathogens · 2026Article
- Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1.Communications biology · 2025Article
- Exploring the influence of anionic lipids in the host cell membrane on viral fusion.Biochemical Society transactions · 2024Review
- Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection.PLoS pathogens · 2024Article
- Novel proteolytic activation of Ebolavirus glycoprotein GP by TMPRSS2 and cathepsin L at an uncharted position can compensate for furin cleavage.Virus research · 2024Article
- Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.ACS infectious diseases · 2024Article
- A novel MARV glycoprotein-specific antibody with potentials of broad-spectrum neutralization to filovirus.eLife · 2024Article
- A Salt Bridge and Disulfide Bond within the Lassa Virus Fusion Domain Are Required for the Initiation of Membrane Fusion.ACS omega · 2024Article
- A novelMicrobiology spectrum · 2023Article
- Viral Membrane Fusion: A Dance Between Proteins and Lipids.Annual review of virology · 2023Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Structure of the Inmazeb cocktail and resistance to Ebola virus escape.Cell host & microbe · 2023Article
- Pseudotyped Viruses for Marburgvirus and Ebolavirus.Advances in experimental medicine and biology · 2023Article
- Activation of Toll-like receptor 4 by Ebola virus-shed glycoprotein is direct and requires the internal fusion loop but not glycosylation.Cell reports · 2022Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Ebolavirus (Ebov), an enveloped virus of the family Filoviridae, causes hemorrhagic fever in humans and nonhuman primates. The viral glycoprotein (GP) is solely responsible for virus-host membrane fusion, but how it does so remains elusive. Fusion occurs after virions reach an endosomal compartment where GP is proteolytically primed by cathepsins. Fusion by primed GP is governed by an internal fusion loop found in GP2, the fusion subunit. This fusion loop contains a stretch of hydrophobic residues, some of which have been shown to be critical for GP-mediated infection. Here we present liposome fusion data and NMR structures for a complete (54-residue) disulfide-bonded internal fusion loop (Ebov FL) in a membrane mimetic. The Ebov FL induced rapid fusion of liposomes of varying compositions at pH values at or below 5.5. Consistently, circular dichroism experiments indicated that the α-helical content of the Ebov FL in the presence of either lipid-mimetic micelles or small liposomes increases in samples exposed to pH ≤5.5. NMR structures in dodecylphosphocholine micelles at pH 7.0 and 5.5 revealed a conformational change from a relatively flat extended loop structure at pH 7.0 to a structure with an ∼90° bend at pH 5.5. Induction of the bend at low pH reorients and compacts the hydrophobic patch at the tip of the FL. We propose that these changes facilitate disruption of lipids at the site of virus-host cell membrane contact and, hence, initiate Ebov fusion.
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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.