ArticleNature structural & molecular biology2020
Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation.
Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.
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Who cites it
117 citing papers in PubMed.
- Disulfide bonds stabilize the SARS-CoV-2 RBD and preserve binding to ACE2 following thermal denaturation.Bioscience reports · 2026Article
- Antibody-mediated SARS-CoV-2 entry and conformational regulation.Microbiology spectrum · 2026Article
- Localized Rigidification and Allosteric Modulation Mechanisms of SARS-CoV-2 Spike Neutralization by Class 3 and Class 4 Antibodies at Atomic Resolution: An Integrated Computational Study of Binding, Dynamics, and Allostery.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms of Binding and Immune Escape Resistance for Broadly Neutralizing Antibodies Targeting Distinct Conserved SARS-CoV-2 Spike Epitopes: A Hierarchical Approach Integrating Mutational Profiling and Energy Landscape Analysis.International journal of molecular sciences · 2026Article
- A cost-effective 200 kV cryo-EM core facility for high resolution single particle analysis.Methods in microscopy · 2026Article
- Frustration Landscapes of Broadly Neutralizing SARS-CoV-2 Spike Antibodies Targeting Conserved Epitopes Reveal Energetic Logic of Escape-Proof and Escape-Prone Mechanisms.bioRxiv : the preprint server for biology · 2026Article
- A Mammalian Surface Display Platform to Optimize the Antigenicity of Viral Proteins for Vaccine Design.bioRxiv : the preprint server for biology · 2026Article
- Human β defensin type 2 based novel antimicrobial peptide prediction using both molecular dynamics simulation and artificial intelligence methods.Frontiers in chemistry · 2026Article
- Legal questions of AI-generated immunological products for infectious diseases.Human vaccines & immunotherapeutics · 2025Review
- Neutral Frustration Landscape Architecture of SARS-CoV-2 Spike-Antibody Interfaces Shapes Immune Evasion Mechanisms for Ultrapotent Neutralizing Antibodies and Determines Pathways of Viral Adaptation: Insights from Integrative Computational Approach.bioRxiv : the preprint server for biology · 2025Article
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- Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection.Nature nanotechnology · 2025Article
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- Capture of fusion-intermediate conformations of SARS-CoV-2 spike requires receptor binding and cleavage at either the S1/S2 or S2' site.PLoS pathogens · 2025Article
- Exploring the Interaction of RBD with Human β Defensin Type 2 Point Mutants: Insights from Molecular Dynamics Simulations.The journal of physical chemistry. B · 2025Article
- Mutational Scanning and Binding Free Energy Computations of the SARS-CoV-2 Spike Complexes with Distinct Groups of Neutralizing Antibodies: Energetic Drivers of Convergent Evolution of Binding Affinity and Immune Escape Hotspots.International journal of molecular sciences · 2025Article
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- Engineering Protein Dynamics through Mutational Energy Landscape Traps.Journal of chemical information and modeling · 2025Article
- AntigenBoost: enhanced mRNA-based antigen expression through rational amino acid substitution.Briefings in bioinformatics · 2024Article
57 more citing papers are in PubMed but not listed here.
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5 authors.
Funding
Abstract
SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other β-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies.
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