ArticleStructure (London, England : 1993)2024
Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain.
Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- Contrastive learning enables epitope overlap predictions for targeted antibody discovery.Patterns (New York, N.Y.) · 2026Article
- Innovation in active and passive immunisation of people who are immunocompromised: a call to action.The Lancet. Infectious diseases · 2026Review
- Early 2022 breakthrough infection sera from India target the conserved cryptic class 5 epitope to counteract immune escape by SARS-CoV-2 variants.Journal of virology · 2025Article
- Affinity maturation endows potent activity onto class 6 SARS-CoV-2 broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Comprehensive analysis of SARS-CoV-2 Spike evolution: epitope classification and immune escape prediction.Virus evolution · 2025Article
- Structural Immunology of SARS-CoV-2.Immunological reviews · 2025Review
- Broadening sarbecovirus neutralization with bispecific antibodies combining distinct conserved targets on the receptor binding domain.Human vaccines & immunotherapeutics · 2024Article
- Automated and virus variant-programmable surrogate test qualitatively compares to the gold standard SARS-CoV-2 neutralization assay.Npj viruses · 2024Article
- "Outlaw" mutations in quasispecies of SARS-CoV-2 inhibit replication.Emerging microbes & infections · 2024Article
- Discovery, recognized antigenic structures, and evolution of cross-serotype broadly neutralizing antibodies from porcine B-cell repertoires against foot-and-mouth disease virus.PLoS pathogens · 2024Article
- Comprehensive Overview of Broadly Neutralizing Antibodies against SARS-CoV-2 Variants.Viruses · 2024Review
- Article
Corrections and comments
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Authors and funding
45 authors at 6 institutions in 1 country.
Funding
Abstract
Given the continuous emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs), immunotherapeutics that target conserved epitopes on the spike (S) glycoprotein have therapeutic advantages. Here, we report the crystal structure of the SARS-CoV-2 S receptor-binding domain (RBD) at 1.95 Å and describe flexibility and distinct conformations of the angiotensin-converting enzyme 2 (ACE2)-binding site. We identify a set of SARS-CoV-2-reactive monoclonal antibodies (mAbs) with broad RBD cross-reactivity including SARS-CoV-2 Omicron subvariants, SARS-CoV-1, and other sarbecoviruses and determine the crystal structures of mAb-RBD complexes with Ab246 and CR3022 mAbs targeting the class IV site, WRAIR-2134, which binds the recently designated class V epitope, and WRAIR-2123, the class I ACE2-binding site. The broad reactivity of class IV and V mAbs to conserved regions of SARS-CoV-2 VoCs and other sarbecovirus provides a framework for long-term immunotherapeutic development strategies.
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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.