ArticleNature communications2023
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Longitudinal analysis of immune responses to SARS-CoV-2 recombinant vaccine S-268019-b in phase 1/2 prime-boost study.Frontiers in immunology · 2025Trial
- Development of a recombinant single-cycle influenza viral vector as an intranasal vaccine against SARS-CoV-2.Scientific reports · 2026Article
- Prefusion-stabilized SARS-CoV-2 spike reshapes antigenic hierarchy and antibody targeting against conserved and occluded epitopes.NPJ vaccines · 2026Article
- Article
- The buried S2 apex of SARS-CoV-2 spike elicits an immunodominant germline-restricted public antibody response.bioRxiv : the preprint server for biology · 2026Article
- Characterization of the heterogeneity in SARS-CoV-2 fitness dynamics via graph representation learning.PLoS computational biology · 2026Article
- Phylogenetic Domain Adaption for Linear B-Cell Epitope Prediction.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Development of a Recombinant Single-Cycle Influenza Viral Vector as an Intranasal Vaccine against SARS-CoV-2 and SARS-like Betacoronaviruses.bioRxiv : the preprint server for biology · 2025Article
- 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
- SARS-CoV-2 RBD Scaffolded by AP205 or TIP60 Nanoparticles and Delivered as mRNA Elicits Robust Neutralizing Antibody Responses.Vaccines · 2025Article
- Article
- The Compensatory Effect of S375F on S371F Is Vital for Maintaining the Infectivity of SARS-CoV-2 Omicron Variants.Journal of medical virology · 2025Article
- Epitope-focused vaccine immunogens design using tailored horseshoe-shaped scaffold.Journal of nanobiotechnology · 2025Article
- Visual and High-Efficiency Secretion of SARS-CoV-2 Nanobodies withBiomolecules · 2025Article
- The molecular reach of antibodies crucially underpins their viral neutralisation capacity.Nature communications · 2025Article
- Structural Immunology of SARS-CoV-2.Immunological reviews · 2025Review
- Viral glycoprotein-mediated entry and antibody-mediated immunity in HIV-1 and SARS-CoV-2 infection.Frontiers in immunology · 2025Review
- Engineering a SARS-CoV-2 Vaccine Targeting the Receptor-Binding Domain Cryptic-Face via Immunofocusing.ACS central science · 2024Article
- Delineating the functional activity of antibodies with cross-reactivity to SARS-CoV-2, SARS-CoV-1 and related sarbecoviruses.PLoS pathogens · 2024Article
- EpiScan: accurate high-throughput mapping of antibody-specific epitopes using sequence information.NPJ systems biology and applications · 2024Article
Corrections and comments
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibody-mediated immunity plays a crucial role in protection against SARS-CoV-2 infection. We isolated a panel of neutralizing anti-receptor-binding domain (RBD) antibodies elicited upon natural infection and vaccination and showed that they recognize an immunogenic patch on the internal surface of the core RBD, which faces inwards and is hidden in the "down" state. These antibodies broadly neutralize wild type (Wuhan-Hu-1) SARS-CoV-2, Beta and Delta variants and some are effective against other sarbecoviruses. We observed a continuum of partially overlapping antibody epitopes from lower to upper part of the inner face of the RBD and some antibodies extend towards the receptor-binding motif. The majority of antibodies are substantially compromised by three mutational hotspots (S371L/F, S373P and S375F) in the lower part of the Omicron BA.1, BA.2 and BA.4/5 RBD. By contrast, antibody IY-2A induces a partial unfolding of this variable region and interacts with a conserved conformational epitope to tolerate all antigenic variations and neutralize diverse sarbecoviruses as well. This finding establishes that antibody recognition is not limited to the normal surface structures on the RBD. In conclusion, the delineation of functionally and structurally conserved RBD epitopes highlights potential vaccine and therapeutic candidates for COVID-19.
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