ArticleFrontiers in immunology2021
Stabilization of the SARS-CoV-2 Spike Receptor-Binding Domain Using Deep Mutational Scanning and Structure-Based Design.
Article in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Pan-Ebolavirus nanoparticle vaccine provides protection in rodents from lethal infection by Zaire and Sudan viruses.Nature communications · 2026Article
- Epitope-focused discovery of SARS-CoV-2 antibodies that potently neutralize Omicron variants.Nature microbiology · 2026Article
- Immune-focused RBD nanoparticles induce cross-reactive, RBS-directed responses capable of variant-resistant SARS-CoV-2 neutralization.PLoS pathogens · 2026Article
- Improving the immunogenicity ofFrontiers in immunology · 2026Article
- Cavity-Filling Mutations as a Strategy to Stabilize Prefusion Viral Fusion Proteins for Vaccine Design.Computational and structural biotechnology journal · 2026Review
- The magnitude and cross reactivity of SARS-CoV-2 specific antibody responses in Sri Lankan children and association with the nutritional status.BMC infectious diseases · 2025Article
- Computationally designed mRNA-launched protein nanoparticle immunogens elicit protective antibody and T cell responses in mice.Science translational medicine · 2025Article
- Novel Strategies for Developing Next-Generation Vaccines to Combat Infectious Viral Diseases.Vaccines · 2025Review
- SARS-CoV-2 RBD Scaffolded by AP205 or TIP60 Nanoparticles and Delivered as mRNA Elicits Robust Neutralizing Antibody Responses.Vaccines · 2025Article
- Phylogeny-driven design of broadly protective sarbecovirus receptor-binding domain nanoparticle vaccines.bioRxiv : the preprint server for biology · 2025Article
- Article
- Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV.Cell reports · 2024Article
- Preventing future zoonosis: SARS-CoV-2 mutations enhance human-animal cross-transmission.Computers in biology and medicine · 2024Article
- Engineering a SARS-CoV-2 Vaccine Targeting the Receptor-Binding Domain Cryptic-Face via Immunofocusing.ACS central science · 2024Article
- Potent neutralization of SARS-CoV-2 variants by RBD nanoparticle and prefusion-stabilized spike immunogens.NPJ vaccines · 2024Article
- Influenza virus strains expressing SARS-CoV-2 receptor binding domain protein confer immunity in K18-hACE2 mice.Vaccine: X · 2024Article
- Deep mutational scanning of SARS-CoV-2 Omicron BA.2.86 and epistatic emergence of the KP.3 variant.bioRxiv : the preprint server for biology · 2024Article
- Engineering a SARS-CoV-2 vaccine targeting the RBD cryptic-face via immunofocusing.bioRxiv : the preprint server for biology · 2024Article
- Article
- Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
27 authors.
Funding
Abstract
The unprecedented global demand for SARS-CoV-2 vaccines has demonstrated the need for highly effective vaccine candidates that are thermostable and amenable to large-scale manufacturing. Nanoparticle immunogens presenting the receptor-binding domain (RBD) of the SARS-CoV-2 Spike protein (S) in repetitive arrays are being advanced as second-generation vaccine candidates, as they feature robust manufacturing characteristics and have shown promising immunogenicity in preclinical models. Here, we used previously reported deep mutational scanning (DMS) data to guide the design of stabilized variants of the RBD. The selected mutations fill a cavity in the RBD that has been identified as a linoleic acid binding pocket. Screening of several designs led to the selection of two lead candidates that expressed at higher yields than the wild-type RBD. These stabilized RBDs possess enhanced thermal stability and resistance to aggregation, particularly when incorporated into an icosahedral nanoparticle immunogen that maintained its integrity and antigenicity for 28 days at 35-40°C, while corresponding immunogens displaying the wild-type RBD experienced aggregation and loss of antigenicity. The stabilized immunogens preserved the potent immunogenicity of the original nanoparticle immunogen, which is currently being evaluated in a Phase I/II clinical trial. Our findings may improve the scalability and stability of RBD-based coronavirus vaccines in any format and more generally highlight the utility of comprehensive DMS data in guiding vaccine design.
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