ArticleJournal of virology2012
Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed, 160 citations in OpenAlex.
- Pan-Ebolavirus nanoparticle vaccine provides protection in rodents from lethal infection by Zaire and Sudan viruses.Nature communications · 2026Article
- A broadly-neutralizing antibody against Orthoebolavirus glycoprotein that potentiates the breadth and neutralization of other antibodies.Npj viruses · 2026Article
- A highly potent nanobody-based bispecific therapeutic provides broad-spectrum protection against ebolavirus.Nature communications · 2026Article
- Article
- Identification of Filovirus Entry Inhibitors from Marine Fungus-Derived Indole Alkaloids.Marine drugs · 2025Article
- Endosomal fusion of pH-dependent enveloped viruses requires ion channel TRPM7.Nature communications · 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
- Genome-wide CRISPR/Cas9 screen identifies SLC39A9 and PIK3C3 as crucial entry factors for Ebola virus infection.PLoS pathogens · 2024Article
- SLC38A9 regulates SARS-CoV-2 viral entry.iScience · 2024Article
- A novel MARV glycoprotein-specific antibody with potentials of broad-spectrum neutralization to filovirus.eLife · 2024Article
- Design of universal Ebola virus vaccine candidates via immunofocusing.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Regulation of Ebola GP conformation and membrane binding by the chemical environment of the late endosome.PLoS pathogens · 2023Article
- Identification of CCZ1 as an essential lysosomal trafficking regulator in Marburg and Ebola virus infections.Nature communications · 2023Article
- Design of universal Ebola virus vaccine candidatesbioRxiv : the preprint server for biology · 2023Article
- A novelMicrobiology spectrum · 2023Article
- The Ebola virus VP40 matrix layer undergoes endosomal disassembly essential for membrane fusion.The EMBO journal · 2023Article
- Single-Virus Fusion Measurements Reveal Multiple Mechanistically Equivalent Pathways for SARS-CoV-2 Entry.Journal of virology · 2023Article
- Sphingosine Kinases Promote Ebola Virus Infection and Can Be Targeted to Inhibit Filoviruses, Coronaviruses, and Arenaviruses Using Late Endocytic Trafficking to Enter Cells.ACS infectious diseases · 2023Article
- Structure of the Inmazeb cocktail and resistance to Ebola virus escape.Cell host & microbe · 2023Article
- Ligand-based design of peptide entry inhibitors targeting the endosomal receptor binding site of filoviruses.Antiviral research · 2022Article
46 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cellular entry of Ebola virus (EBOV), a deadly hemorrhagic fever virus, is mediated by the viral glycoprotein (GP). The receptor-binding subunit of GP must be cleaved (by endosomal cathepsins) in order for entry and infection to proceed. Cleavage appears to proceed through 50-kDa and 20-kDa intermediates, ultimately generating a key 19-kDa core. How 19-kDa GP is subsequently triggered to bind membranes and induce fusion remains a mystery. Here we show that 50-kDa GP cannot be triggered to bind to liposomes in response to elevated temperature but that 20-kDa and 19-kDa GP can. Importantly, 19-kDa GP can be triggered at temperatures ∼10°C lower than 20-kDa GP, suggesting that it is the most fusion ready form. Triggering by heat (or urea) occurs only at pH 5, not pH 7.5, and involves the fusion loop, as a fusion loop mutant is defective in liposome binding. We further show that mild reduction (preferentially at low pH) triggers 19-kDa GP to bind to liposomes, with the wild-type protein being triggered to a greater extent than the fusion loop mutant. Moreover, mild reduction inactivates pseudovirion infection, suggesting that reduction can also trigger 19-kDa GP on virus particles. Our results support the hypothesis that priming of EBOV GP, specifically to the 19-kDa core, potentiates GP to undergo subsequent fusion-relevant conformational changes. Our findings also indicate that low pH and an additional endosomal factor (possibly reduction or possibly a process mimicked by reduction) act as fusion triggers.
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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.