ArticleThe Journal of biological chemistry2021
Structures of synthetic nanobody-SARS-CoV-2 receptor-binding domain complexes reveal distinct sites of interaction.
Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 2 of them syntheses that pooled it.
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Who cites it
28 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- Outlook of therapeutic and diagnostic competency of nanobodies against SARS-CoV-2: A systematic review.Analytical biochemistry · 2022Pooled it
- Research Progress and Applications of Multivalent, Multispecific and Modified Nanobodies for Disease Treatment.Frontiers in immunology · 2021Pooled it
- ACE2-fused nanobody targeting a cryptic RBD epitope broadly neutralizes SARS-like viruses.Journal of virology · 2026Article
- Rational design of a covalent ACE2 decoy receptor that broadly neutralizes SARS-CoV-2 variants.Protein science : a publication of the Protein Society · 2025Article
- MprF fromScience advances · 2025Article
- Facilitating and restraining virus infection using cell-attachable soluble viral receptors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A single-domain antibody library based on a stability-engineered human VH3 scaffold.Scientific reports · 2024Article
- Article
- Development of a bispecific nanobody conjugate broadly neutralizes diverse SARS-CoV-2 variants and structural basis for its broad neutralization.PLoS pathogens · 2023Article
- SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain.Communications biology · 2023Article
- Structure-Guided Development of Bivalent Aptamers Blocking SARS-CoV-2 Infection.Molecules (Basel, Switzerland) · 2023Article
- Design and Immunogenicity of SARS-CoV-2 DNA Vaccine Encoding RBD-PVXCP Fusion Protein.Vaccines · 2023Article
- SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain.Research square · 2023Article
- Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity.Nature communications · 2023Article
- Hetero-bivalent nanobodies provide broad-spectrum protection against SARS-CoV-2 variants of concern including Omicron.Cell research · 2022Article
- Determining the International Spread of B.1.1.523 SARS-CoV-2 Lineage with a Set of Mutations Highly Associated with Reduced Immune Neutralization.Microorganisms · 2022Article
- Passive Immunotherapy Against SARS-CoV-2: From Plasma-Based Therapy to Single Potent Antibodies in the Race to Stay Ahead of the Variants.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2022Review
- Biparatopic sybodies neutralize SARS-CoV-2 variants of concern and mitigate drug resistance.EMBO reports · 2022Article
- Structural and Computational Studies of the SARS-CoV-2 Spike Protein Binding Mechanisms with Nanobodies: From Structure and Dynamics to Avidity-Driven Nanobody Engineering.International journal of molecular sciences · 2022Review
- A structural view of the SARS-CoV-2 virus and its assembly.Current opinion in virology · 2022Review
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Combating the worldwide spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the emergence of new variants demands understanding of the structural basis of the interaction of antibodies with the SARS-CoV-2 receptor-binding domain (RBD). Here, we report five X-ray crystal structures of sybodies (synthetic nanobodies) including those of binary and ternary complexes of Sb16-RBD, Sb45-RBD, Sb14-RBD-Sb68, and Sb45-RBD-Sb68, as well as unliganded Sb16. These structures reveal that Sb14, Sb16, and Sb45 bind the RBD at the angiotensin-converting enzyme 2 interface and that the Sb16 interaction is accompanied by a large conformational adjustment of complementarity-determining region 2. In contrast, Sb68 interacts at the periphery of the SARS-CoV-2 RBD-angiotensin-converting enzyme 2 interface. We also determined cryo-EM structures of Sb45 bound to the SARS-CoV-2 spike protein. Superposition of the X-ray structures of sybodies onto the trimeric spike protein cryo-EM map indicates that some sybodies may bind in both "up" and "down" configurations, but others may not. Differences in sybody recognition of several recently identified RBD variants are explained by these structures.
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