ArticleCell reports2021
Paired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses.
Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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.
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Who cites it
53 citing papers in PubMed, 60 citations in OpenAlex.
- The evolution of display technologies for antibody drug discovery.Trends in biotechnology · 2026Review
- The adaptive immune receptors in a big data world.ImmunoHorizons · 2026Review
- Potent Monoclonal Antibodies Against Circulating Yellow Fever Virus Strains from Donors Immunized with the 17D Vaccine.The American journal of tropical medicine and hygiene · 2026Article
- Structural and Functional Characterization of Anti-SARS-CoV-2 Spike Monoclonal Antibodies Produced via Bicistronic Expression in CHO Cells.Antibodies (Basel, Switzerland) · 2025Article
- Comparative Analysis of Mammalian Adaptive Immune Loci Revealed Spectacular Divergence and Common Genetic Patterns.Molecular biology and evolution · 2025Article
- Retrospective SARS-CoV-2 human antibody development trajectories are largely sparse and permissive.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Optimized single-cell gates for yeast display screening.Protein engineering, design & selection : PEDS · 2025Article
- Beyond Single Clones: High-Throughput Sequencing in Antibody Discovery.Cold Spring Harbor protocols · 2025Article
- Backstage Heroes-Yeast in COVID-19 Research.International journal of molecular sciences · 2024Review
- Current development of severe acute respiratory syndrome coronavirus 2 neutralizing antibodies (Review).Molecular medicine reports · 2024Review
- Two-dimensional high-throughput on-cell screening of immunoglobulins against broad antigen repertoires.Communications biology · 2024Article
- Structural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies.Cell reports. Medicine · 2024Article
- Fusing Peptide Epitopes for Advanced Multiplex Serological Testing for SARS-CoV-2 Antibody Detection.ACS bio & med chem Au · 2024Article
- Studying SARS-CoV-2 interactions using phage-displayed receptor binding domain as a model protein.Scientific reports · 2024Article
- Breakthrough infection elicits hypermutated IGHV3-53/3-66 public antibodies with broad and potent neutralizing activity against SARS-CoV-2 variants including the emerging EG.5 lineages.PLoS pathogens · 2023Article
- Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site.Nature communications · 2023Article
- Cell activation-based screening of natively paired human T cell receptor repertoires.Scientific reports · 2023Article
- Broadly neutralizing antibodies to SARS-CoV-2 and other human coronaviruses.Nature reviews. Immunology · 2023Review
- Large-scale antibody immune response mapping of splenic B cells and bone marrow plasma cells in a transgenic mouse model.Frontiers in immunology · 2023Article
- Monoclonal antibody therapies against SARS-CoV-2.The Lancet. Infectious diseases · 2022Review
Corrections and comments
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Authors and funding
34 authors at 7 institutions in 3 countries.
Funding
Abstract
Understanding mechanisms of protective antibody recognition can inform vaccine and therapeutic strategies against SARS-CoV-2. We report a monoclonal antibody, 910-30, targeting the SARS-CoV-2 receptor-binding site for ACE2 as a member of a public antibody response encoded by IGHV3-53/IGHV3-66 genes. Sequence and structural analyses of 910-30 and related antibodies explore how class recognition features correlate with SARS-CoV-2 neutralization. Cryo-EM structures of 910-30 bound to the SARS-CoV-2 spike trimer reveal binding interactions and its ability to disassemble spike. Despite heavy-chain sequence similarity, biophysical analyses of IGHV3-53/3-66-encoded antibodies highlight the importance of native heavy:light pairings for ACE2-binding competition and SARS-CoV-2 neutralization. We develop paired heavy:light class sequence signatures and determine antibody precursor prevalence to be ∼1 in 44,000 human B cells, consistent with public antibody identification in several convalescent COVID-19 patients. These class signatures reveal genetic, structural, and functional immune features that are helpful in accelerating antibody-based medical interventions for SARS-CoV-2.
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What OpenQuestion holds
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.