ArticleScience (New York, N.Y.)2022
Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 3 of them syntheses 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
125 citing papers in PubMed, 3 syntheses or guidelines pooled it.
- Unveiling protection: a meta-analysis of tixagevimab-cilgavimab prophylaxis in 28,950 transplant recipients and immunocompromised patients against COVID-19.Virology journal · 2025Pooled it
- SARS-CoV-2 neutralizing antibody bebtelovimab - a systematic scoping review and meta-analysis.Frontiers in immunology · 2023Pooled it
- Susceptibility of SARS-CoV-2 Omicron Variants to Therapeutic Monoclonal Antibodies: Systematic Review and Meta-analysis.Microbiology spectrum · 2022Pooled it
- Safety, Tolerability and Pharmacokinetics of Half-Life Extended Severe Acute Respiratory Syndrome Coronavirus 2 Neutralizing Monoclonal Antibodies AZD7442 (Tixagevimab-Cilgavimab) in Healthy Adults.The Journal of infectious diseases · 2023Trial
- AZD7442 (Tixagevimab/Cilgavimab) for Post-Exposure Prophylaxis of Symptomatic Coronavirus Disease 2019.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2023Trial
- Intramuscular AZD7442 (Tixagevimab-Cilgavimab) for Prevention of Covid-19.The New England journal of medicine · 2022Trial
- Canonical Antibodies Adopt Distinct Binding Modes to Recognize Viral Glycan Shields.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- Broad Neutralizing Activity of Monoclonal Antibodies Against the Omicron Variants Isolated From Patients With Early Severe Acute Respiratory Syndrome Coronavirus-2.Journal of medical virology · 2026Article
- Epitope-focused discovery of SARS-CoV-2 antibodies that potently neutralize Omicron variants.Nature microbiology · 2026Article
- Monoclonal antibodies from COVID-19 convalescent patients target cryptic epitopes for broad SARS-CoV-2 neutralization.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Exploring the diverse binding ability of SARS-CoV-2 variant RBDs to different antibody classes: a computational study.RSC advances · 2026Article
- IgG-Bridging-Seeded Synergistic Aggregation of SARS-CoV-2 Spikes Underlies Potent Neutralization by a Low-Affinity Antibody.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- SARS-CoV-2 variants: biology, pathogenicity, immunity and control.Nature reviews. Microbiology · 2026Review
- Structural Insights into the SARS-CoV-2 Spike Protein and Its Implications for Antibody Resistance.Biomolecules · 2025Review
- Mutation profiling, evolution analysis, molecular dynamics simulation, and functional characterization of Omicron sub-strains.Virus research · 2025Article
- Two cross-neutralizing antibodies isolated from a COVID-19 convalescent via single B cell sorting.Archives of virology · 2025Article
- Immune evasion, infectivity, and membrane fusion of the SARS-CoV-2 JN.1 variant.Virology journal · 2025Article
- Neutralization and spike stability of JN.1-derived LB.1, KP.2.3, KP.3, and KP.3.1.1 subvariants.mBio · 2025Article
- Balancing stability and function: impact of the surface charge of SARS-CoV-2 Omicron spike protein.Npj viruses · 2025Review
65 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
25 authors.
Funding
Abstract
The rapid spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.529 (Omicron) variant and its resistance to neutralization by vaccinee and convalescent sera are driving a search for monoclonal antibodies with potent neutralization. To provide insight into effective neutralization, we determined cryo-electron microscopy structures and evaluated receptor binding domain (RBD) antibodies for their ability to bind and neutralize B.1.1.529. Mutations altered 16% of the B.1.1.529 RBD surface, clustered on an RBD ridge overlapping the angiotensin-converting enzyme 2 (ACE2)-binding surface and reduced binding of most antibodies. Substantial inhibitory activity was retained by select monoclonal antibodies-including A23-58.1, B1-182.1, COV2-2196, S2E12, A19-46.1, S309, and LY-CoV1404-that accommodated these changes and neutralized B.1.1.529. We identified combinations of antibodies with synergistic neutralization. The analysis revealed structural mechanisms for maintenance of potent neutralization against emerging variants.
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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.