ArticleNature microbiology2021
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail.
Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 207 papers, 1 of them a synthesis that pooled it.
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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
207 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Susceptibility of SARS-CoV-2 Omicron Variants to Therapeutic Monoclonal Antibodies: Systematic Review and Meta-analysis.Microbiology spectrum · 2022Pooled it
- Anti-SARS-CoV-2 glyco-humanized polyclonal antibody XAV-19: phase II/III randomized placebo-controlled trial shows acceleration to recovery for mild to moderate patients with COVID-19.Frontiers in immunology · 2024Trial
- 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
- Tixagevimab-cilgavimab for treatment of patients hospitalised with COVID-19: a randomised, double-blind, phase 3 trial.The Lancet. Respiratory medicine · 2022Trial
- Intramuscular AZD7442 (Tixagevimab-Cilgavimab) for Prevention of Covid-19.The New England journal of medicine · 2022Trial
- Responses to a Neutralizing Monoclonal Antibody for Hospitalized Patients With COVID-19 According to Baseline Antibody and Antigen Levels : A Randomized Controlled Trial.Annals of internal medicine · 2022Trial
- Trial
- R1-32-like public antibodies acquire tolerance to SARS-CoV-2 antigenic drift through somatic hypermutation.PLoS biology · 2026Article
- Functional and structural basis of Omicron BA.3.2.1 spike.Cell reports · 2026Article
- Genetic diversity of pangolin coronaviruses reveals a key immuno-evasive substitution at spike residue 519.Journal of virology · 2026Article
- Large-scale genomic surveillance reveals immunosuppression drives mutation dynamics in persistent SARS-CoV-2 infections.Nature communications · 2026Article
- SARS-CoV-2 saltational events are recurrent and trace to persistent human infections.bioRxiv : the preprint server for biology · 2026Article
- Systems-Scale Structural Modeling Reveals the Germline Architecture of Immunodominance.bioRxiv : the preprint server for biology · 2026Article
- Epistasis and background dependence in the evolution of Omicron variants of the SARS-CoV-2 spike protein.Molecular biology and evolution · 2026Article
- Epitope-focused discovery of SARS-CoV-2 antibodies that potently neutralize Omicron variants.Nature microbiology · 2026Article
- Transition from infectivity and immune escape to pure escape as an evolutionary strategy during the COVID-19 pandemic.bioRxiv : the preprint server for biology · 2026Article
- Discovery of Anti-SARS-CoV-2 XBB.1.5 and JN.1 Variant-Specific Monoclonal Single-Domain Antibodies from a Synthetic Library.Antibodies (Basel, Switzerland) · 2026Article
- SARS-CoV-2 variants: biology, pathogenicity, immunity and control.Nature reviews. Microbiology · 2026Review
- Modeling the Mutational Effects on Biochemical Phenotypes of SARS-CoV-2 Using Molecular Fields.Biomolecules · 2025Article
147 more citing papers are in PubMed but not listed here.
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Authors and funding
32 authors.
Funding
Abstract
Understanding the molecular basis for immune recognition of SARS-CoV-2 spike glycoprotein antigenic sites will inform the development of improved therapeutics. We determined the structures of two human monoclonal antibodies-AZD8895 and AZD1061-which form the basis of the investigational antibody cocktail AZD7442, in complex with the receptor-binding domain (RBD) of SARS-CoV-2 to define the genetic and structural basis of neutralization. AZD8895 forms an 'aromatic cage' at the heavy/light chain interface using germ line-encoded residues in complementarity-determining regions (CDRs) 2 and 3 of the heavy chain and CDRs 1 and 3 of the light chain. These structural features explain why highly similar antibodies (public clonotypes) have been isolated from multiple individuals. AZD1061 has an unusually long LCDR1; the HCDR3 makes interactions with the opposite face of the RBD from that of AZD8895. Using deep mutational scanning and neutralization escape selection experiments, we comprehensively mapped the crucial binding residues of both antibodies and identified positions of concern with regards to virus escape from antibody-mediated neutralization. Both AZD8895 and AZD1061 have strong neutralizing activity against SARS-CoV-2 and variants of concern with antigenic substitutions in the RBD. We conclude that germ line-encoded antibody features enable recognition of the SARS-CoV-2 spike RBD and demonstrate the utility of the cocktail AZD7442 in neutralizing emerging variant viruses.
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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.