ArticleCell reports2023
The evolution and determinants of neutralization of potent head-binding antibodies against Ebola virus.
Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Computational mining of B cell receptor repertoires reveals antigen-specific and convergent responses to Ebola vaccination.Frontiers in immunology · 2024Trial
- Pan-Ebolavirus nanoparticle vaccine provides protection in rodents from lethal infection by Zaire and Sudan viruses.Nature communications · 2026Article
- A tool of the trade for a newly identified filovirus: pseudovirus-based system for Dehong virus entry and neutralization.Microbiology spectrum · 2025Article
- Structural stabilization of the intrinsically disordered SARS-CoV-2 N by binding to RNA sequences engineered from the viral genome fragment.Nature communications · 2025Article
- Fully human monoclonal antibodies against Ebola virus possess complete protection in a hamster model.Emerging microbes & infections · 2024Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Monoclonal antibodies against the Ebola virus (EBOV) surface glycoprotein are effective treatments for EBOV disease. Antibodies targeting the EBOV glycoprotein (GP) head epitope have potent neutralization and Fc effector function activity and thus are of high interest as therapeutics and for vaccine design. Here we focus on the head-binding antibodies 1A2 and 1D5, which have been identified previously in a longitudinal study of survivors of EBOV infection. 1A2 and 1D5 have the same heavy- and light-chain germlines despite being isolated from different individuals and at different time points after recovery from infection. Cryoelectron microscopy analysis of each antibody in complex with the EBOV surface GP reveals key amino acid substitutions in 1A2 that contribute to greater affinity, improved neutralization potency, and enhanced breadth as well as two strategies for antibody evolution from a common site.
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