ArticlePLoS pathogens2024
Dual-role epitope on SARS-CoV-2 spike enhances and neutralizes viral entry across different variants.
Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Update and reuse: Structure-guided nanobody evolution against SARS-CoV-2 escape.PLoS pathogens · 2026Article
- Article
- A highly potent and broadly accessible bispecific nanobody for the treatment of ebola virus infections.PLoS pathogens · 2026Article
- A SARS-CoV-2 entry inhibitor trimerizes to lock the spike protein in a closed conformation.bioRxiv : the preprint server for biology · 2025Article
- Long-Circulating Nanobody Confers Durable Prophylaxis against Severe Acute Respiratory Syndrome Coronavirus 2 Omicron Infection.Advanced nanobiomed research · 2025Article
- Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1.Communications biology · 2025Article
- Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection.PLoS pathogens · 2024Article
- Discovery of Nanosota-9 as anti-Omicron nanobody therapeutic candidate.PLoS pathogens · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Grasping the roles of epitopes in viral glycoproteins is essential for unraveling the structure and function of these proteins. Up to now, all identified epitopes have been found to either neutralize, have no effect on, or enhance viral entry into cells. Here, we used nanobodies (single-domain antibodies) as probes to investigate a unique epitope on the SARS-CoV-2 spike protein, located outside the protein's receptor-binding domain. Nanobody binding to this epitope enhances the cell entry of prototypic SARS-CoV-2, while neutralizing the cell entry of SARS-CoV-2 Omicron variant. Moreover, nanobody binding to this epitope promotes both receptor binding activity and post-attachment activity of prototypic spike, explaining the enhanced viral entry. The opposite occurs with Omicron spike, explaining the neutralized viral entry. This study reveals a unique epitope that can both enhance and neutralize viral entry across distinct viral variants, suggesting that epitopes may vary their roles depending on the viral context. Consequently, antibody therapies should be assessed across different viral variants to confirm their efficacy and safety.
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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.