ArticleProceedings of the National Academy of Sciences of the United States of America2022
A broad and potent neutralization epitope in SARS-related coronaviruses.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.
- Susceptibility of SARS-CoV-2 Omicron Variants to Therapeutic Monoclonal Antibodies: Systematic Review and Meta-analysis.Microbiology spectrum · 2022Pooled it
- Emergence of neutralizing RBD antibodies following Omicron infection with limited activity against ancestral SARS-CoV-2.iScience · 2026Article
- Variant-specific spike conformational dynamics shape memory B cell selection during recall.bioRxiv : the preprint server for biology · 2026Article
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- Prefusion-stabilized SARS-CoV-2 spike reshapes antigenic hierarchy and antibody targeting against conserved and occluded epitopes.NPJ vaccines · 2026Article
- Heterologous saRNA prime - multivalent protein boost strategy induces broad and durable immunity against SARS-CoV-2 and MERS-CoV.Scientific reports · 2026Article
- Isolation of neutralizing antibodies against SARS-CoV-2 through an epitope-guided negative screening by phage display.Journal of biomedical research · 2026Article
- Development of a Thermostable and Broadly Neutralizing Pan-Sarbecovirus Vaccine Candidate.ACS infectious diseases · 2026Article
- Clonal interference and changing selective pressures shape the escape of SARS-CoV-2 from hundreds of antibodies.Virus evolution · 2026Article
- Orphan broadly RBD-binding antibodies annotate three remaining conserved RBD epitopes along SARS-CoV-2 evolution.Nature communications · 2025Article
- Neutral Frustration Landscape Architecture of SARS-CoV-2 Spike-Antibody Interfaces Shapes Immune Evasion Mechanisms for Ultrapotent Neutralizing Antibodies and Determines Pathways of Viral Adaptation: Insights from Integrative Computational Approach.bioRxiv : the preprint server for biology · 2025Article
- Structural Insights into the SARS-CoV-2 Spike Protein and Its Implications for Antibody Resistance.Biomolecules · 2025Review
- Bat sarbecovirus WIV1-CoV bears an adaptive mutation that alters spike dynamics and enhances ACE2 binding.PLoS pathogens · 2025Article
- Article
- Broad neutralizing antibody response of a monomeric spike-based SARS-CoV-2 bivalent vaccine against diverse variants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and functional analysis of VYD222: a broadly neutralizing antibody against SARS-CoV-2 variants.bioRxiv : the preprint server for biology · 2025Article
- Efficient discovery of frequently co-occurring mutations in a sequence database with matrix factorization.PLoS computational biology · 2025Article
- Review
- Structural Immunology of SARS-CoV-2.Immunological reviews · 2025Review
- Distinct pathways for evolution of enhanced receptor binding and cell entry in SARS-like bat coronaviruses.PLoS pathogens · 2024Article
Corrections and comments
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Authors and funding
21 authors at 3 institutions in 1 country.
Funding
Abstract
Many neutralizing antibodies (nAbs) elicited to ancestral severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) through natural infection and vaccination have reduced effectiveness to SARS-CoV-2 variants. Here, we show that therapeutic antibody ADG20 is able to neutralize SARS-CoV-2 variants of concern (VOCs) including Omicron (B.1.1.529) as well as other SARS-related coronaviruses. We delineate the structural basis of this relatively escape-resistant epitope that extends from one end of the receptor binding site (RBS) into the highly conserved CR3022 site. ADG20 can then benefit from high potency through direct competition with ACE2 in the more variable RBS and interaction with the more highly conserved CR3022 site. Importantly, antibodies that are able to target this site generally neutralize a broad range of VOCs, albeit with reduced potency against Omicron. Thus, this conserved and vulnerable site can be exploited for the design of universal vaccines and therapeutic antibodies.
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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.