ArticleNature communications2021
Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Somatic Evolution of a Germline Antibody Expands its Breadth to Neutralize Early SARS-CoV-2 Omicron Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Comparison of Igκ and Igλ binding toward influenza virus hemagglutinin and SARS-CoV-2 Spike protein during primary viral infections in humans, mice, and pigs.Comparative immunology, microbiology and infectious diseases · 2026Article
- Affinity maturation and light-chain-mediated paratope diversification anticipates viral evolution.Cell reports · 2026Article
- Explore antibody repertoire in the era of AI.Acta biochimica et biophysica Sinica · 2025Article
- Mouse-adapted SARS-CoV-2 Omicron BA.5 infection induces post-acute lung fibrosis in BALB/c mice.Journal of virology · 2025Article
- Germinal center-mediated broadening of B cell responses to SARS-CoV-2 booster immunization.Science immunology · 2025Article
- Two cross-neutralizing antibodies isolated from a COVID-19 convalescent via single B cell sorting.Archives of virology · 2025Article
- Mouse Adapted Omicron BA.5 Induces A Fibrotic Lung Disease Phenotype in BALB/c Mice.bioRxiv : the preprint server for biology · 2025Article
- Structural Immunology of SARS-CoV-2.Immunological reviews · 2025Review
- Defining a highly conserved B cell epitope in the receptor binding motif of SARS-CoV-2 spike glycoprotein.bioRxiv : the preprint server for biology · 2024Article
- Deep immunoglobulin repertoire sequencing depicts a comprehensive atlas of spike-specific antibody lineages shared among COVID-19 convalescents.Emerging microbes & infections · 2024Article
- Structural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies.Cell reports. Medicine · 2024Article
- Functional and structural investigation of a broadly neutralizing SARS-CoV-2 antibody.JCI insight · 2024Article
- An ancestral SARS-CoV-2 vaccine induces anti-Omicron variants antibodies by hypermutation.Nature communications · 2024Article
- Evidence of antigenic drift in the fusion machinery core of SARS-CoV-2 spike.Proceedings of the National Academy of Sciences of the United States of America · 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
- SARS-CoV-2 antibodies from children exhibit broad neutralization and belong to adult public clonotypes.Cell reports. Medicine · 2023Article
- Broad SARS-CoV-2 neutralization by monoclonal and bispecific antibodies derived from a Gamma-infected individual.iScience · 2023Article
- SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain.Communications biology · 2023Article
- Broadly neutralizing human antibodies against Omicron subvariants of SARS-CoV-2.Journal of biomedical science · 2023Article
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13 authors.
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Abstract
Since the COVID-19 pandemic onset, the antibody response to SARS-CoV-2 has been extensively characterized. Antibodies to the receptor binding domain (RBD) on the spike protein are frequently encoded by IGHV3-53/3-66 with a short complementarity-determining region (CDR) H3. Germline-encoded sequence motifs in heavy chain CDRs H1 and H2 have a major function, but whether any common motifs are present in CDR H3, which is often critical for binding specificity, is not clear. Here, we identify two public clonotypes of IGHV3-53/3-66 RBD antibodies with a 9-residue CDR H3 that pair with different light chains. Distinct sequence motifs on CDR H3 are present in the two public clonotypes that seem to be related to differential light chain pairing. Additionally, we show that Y58F is a common somatic hypermutation that results in increased binding affinity of IGHV3-53/3-66 RBD antibodies with a short CDR H3. These results advance understanding of the antibody response to SARS-CoV-2.
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