ArticleJournal of virology2010
Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 108 citations in OpenAlex.
- Codon-optimized filovirus DNA vaccines delivered by intramuscular electroporation protect cynomolgus macaques from lethal Ebola and Marburg virus challenges.Human vaccines & immunotherapeutics · 2015Trial
- Mapping Immunological, Host Receptor Binding Determinants, and Cathepsin Cleavage Site of EBOV Glycoprotein Utilizing the Qubevirus Platform.ACS omega · 2025Article
- Treatment of Ebola Virus Disease: From Serotherapy to the Use of Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2025Review
- Targeting host O-linked glycan biosynthesis affects Ebola virus replication efficiency and reveals differential GalNAc-T acceptor site preferences on the Ebola virus glycoprotein.Journal of virology · 2024Article
- A viral vaccine design harnessing prior BCG immunization confers protection against Ebola virus.Frontiers in immunology · 2024Article
- Bis-Benzylisoquinoline Alkaloids Inhibit Porcine Epidemic Diarrhea Virus by Disrupting Virus Entry.Pathogens (Basel, Switzerland) · 2023Article
- A Naturally Occurring Polymorphism in the Base of Sudan Virus Glycoprotein Decreases Glycoprotein Stability in a Species-Dependent Manner.Journal of virology · 2021Article
- Virus-Mediated Cell-Cell Fusion.International journal of molecular sciences · 2020Review
- Expression of a Large Single-Chain 13F6 Antibody with Binding Activity against Ebola Virus-Like Particles in a Plant System.International journal of molecular sciences · 2020Article
- Designs and Characterization of Subunit Ebola GP Vaccine Candidates: Implications for Immunogenicity.Frontiers in immunology · 2020Article
- Analysis of Resistance of Ebola Virus Glycoprotein-Driven Entry Against MDL28170, An Inhibitor of Cysteine Cathepsins.Pathogens (Basel, Switzerland) · 2019Article
- Dendritic Cells/Macrophages-Targeting Feature of Ebola Glycoprotein and its Potential as Immunological Facilitator for Antiviral Vaccine Approach.Microorganisms · 2019Review
- Identification of Ebola Virus Inhibitors Targeting GP2 Using Principles of Molecular Mimicry.Journal of virology · 2019Article
- Vaccine nanoparticles displaying recombinant Ebola virus glycoprotein for induction of potent antibody and polyfunctional T cell responses.Nanomedicine : nanotechnology, biology, and medicine · 2019Article
- Structure-Based in Silico Screening Identifies a Potent Ebolavirus Inhibitor from a Traditional Chinese Medicine Library.Journal of medicinal chemistry · 2019Article
- Review
- Structural basis of broad ebolavirus neutralization by a human survivor antibody.Nature structural & molecular biology · 2019Article
- Review
- Antibody-mediated protection against Ebola virus.Nature immunology · 2018Review
- Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop.Nature communications · 2018Article
14 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
Ebola virus (EBOV) cellular attachment and entry is initiated by the envelope glycoprotein (GP) on the virion surface. Entry of this virus is pH dependent and associated with the cleavage of GP by proteases, including cathepsin L (CatL) and/or CatB, in the endosome or cell membrane. Here, we characterize the product of CatL cleavage of Zaire EBOV GP (ZEBOV-GP) and evaluate its relevance to entry. A stabilized recombinant form of the EBOV GP trimer was generated using a trimerization domain linked to a cleavable histidine tag. This trimer was purified to homogeneity and cleaved with CatL. Characterization of the trimeric product by N-terminal sequencing and mass spectrometry revealed three cleavage fragments, with masses of 23, 19, and 4 kDa. Structure-assisted modeling of the cathepsin L-cleaved ZEBOV-GP revealed that cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding. The CatL-cleaved ZEBOV-GP intermediate bound with high affinity to a neutralizing antibody, KZ52, and also elicited neutralizing antibodies, supporting the notion that the processed intermediate is required for viral entry. Together, these data suggest that CatL cleavage of EBOV GP exposes its receptor-binding domain, thereby facilitating access to a putative cellular receptor in steps that lead to membrane fusion.
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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.