ArticlemBio2021
An Engineered Receptor-Binding Domain Improves the Immunogenicity of Multivalent SARS-CoV-2 Vaccines.
Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 28 citations in OpenAlex.
- Amplifying immune responses via a parenteral prime-intranasal boost strategy using a lipidated chitosan nanoparticle-based multi-epitope COVID-19 vaccine.Scientific reports · 2026Article
- Review
- A highly divergent cryptic SARS-CoV-2 lineage exhibits strong receptor binding and immune evasion.medRxiv : the preprint server for health sciences · 2025Article
- SARS-CoV-2 spike protein: structure, viral entry and variants.Nature reviews. Microbiology · 2025Review
- Innovation in mRNA Vaccines and RNAi via Protein Nanocages.Vaccines · 2025Review
- MHCI trafficking signal-based mRNA vaccines strengthening immune protection against RNA viruses.Bioengineering & translational medicine · 2025Article
- Rethinking Optimal Immunogens to Face SARS-CoV-2 Evolution Through Vaccination.Influenza and other respiratory viruses · 2025Review
- Article
- SARS-CoV-2 Spike Protein Enhances Carboxypeptidase Activity of Angiotensin-Converting Enzyme 2.International journal of molecular sciences · 2024Article
- Efficient signal sequence of mRNA vaccines enhances the antigen expression to expand the immune protection against viral infection.Journal of nanobiotechnology · 2024Article
- In vivo affinity maturation of mouse B cells reprogrammed to express human antibodies.Nature biomedical engineering · 2024Article
- Article
- Review
- Nucleic acid-based vaccine platforms against the coronavirus disease 19 (COVID-19).Archives of microbiology · 2023Review
- Ferritin nanocages as efficient nanocarriers and promising platforms for COVID-19 and other vaccines development.Biochimica et biophysica acta. General subjects · 2023Review
- A novel heterologous receptor-binding domain dodecamer universal mRNA vaccine against SARS-CoV-2 variants.Acta pharmaceutica Sinica. B · 2023Article
- Impact of mutations on the plant-based production of recombinant SARS-CoV-2 RBDs.Frontiers in plant science · 2023Article
- Improved interface packing and design opportunities revealed by CryoEM analysis of a designed protein nanocage.Heliyon · 2022Article
- A dual-antigen self-amplifying RNA SARS-CoV-2 vaccine induces potent humoral and cellular immune responses and protects against SARS-CoV-2 variants through T cell-mediated immunity.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Article
- Nanoparticle and virus-like particle vaccine approaches against SARS-CoV-2.Journal of microbiology (Seoul, Korea) · 2022Review
Corrections and comments
- Update of
Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S) protein mediates viral entry into cells expressing angiotensin-converting enzyme 2 (ACE2). The S protein engages ACE2 through its receptor-binding domain (RBD), an independently folded 197-amino-acid fragment of the 1,273-amino-acid S-protein protomer. The RBD is the primary SARS-CoV-2 neutralizing epitope and a critical target of any SARS-CoV-2 vaccine. Here, we show that this RBD conjugated to each of two carrier proteins elicited more potent neutralizing responses in immunized rodents than did a similarly conjugated proline-stabilized S-protein ectodomain. Nonetheless, the native RBD is expressed inefficiently, limiting its usefulness as a vaccine antigen. However, we show that an RBD engineered with four novel glycosylation sites (gRBD) is expressed markedly more efficiently and generates a more potent neutralizing responses as a DNA vaccine antigen than the wild-type RBD or the full-length S protein, especially when fused to multivalent carriers, such as a
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What OpenQuestion holds
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.