ArticleNature communications2024
Engineered dityrosine-bonding of the RSV prefusion F protein imparts stability and potency advantages.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The trial behind it
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Who cites it
12 citing papers in PubMed, 12 citations in OpenAlex.
- A cavity-reduced prefusion RSV F bivalent vaccine elicits durable and protective immunity.EMBO molecular medicine · 2026Article
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- Optimally fixed F protein on the surface of RSV-infected cells for RSV binding and neutralizing assays.Frontiers in microbiology · 2026Article
- Immunofocusing design of a fusion glycoprotein monomer vaccine for respiratory syncytial virus.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- RSV Vaccines: Targeting Prefusion F and G Proteins from Structural Design to Clinical Application.Vaccines · 2025Review
- Stabilized Full-Length Measles Fusion Protein Elicits Potent Immunity and Protection In Vivo.bioRxiv : the preprint server for biology · 2025Article
- Hydrophobic residue substitutions enhance the stability andJournal of virology · 2025Article
- Recent advances in the prevention and treatment of respiratory syncytial virus disease.The Journal of general virology · 2025Review
- Advances in the structure-based design of protein vaccines for respiratory infectious diseases.Computational and structural biotechnology journal · 2025Review
- Rational design of uncleaved prefusion-closed trimer vaccines for human respiratory syncytial virus and metapneumovirus.Nature communications · 2024Article
- Mechanistic insights into structure-based design of a Lyme disease subunit vaccine.bioRxiv : the preprint server for biology · 2024Article
- Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 1 country.
Funding
Abstract
Viral fusion proteins facilitate cellular infection by fusing viral and cellular membranes, which involves dramatic transitions from their pre- to postfusion conformations. These proteins are among the most protective viral immunogens, but they are metastable which often makes them intractable as subunit vaccine targets. Adapting a natural enzymatic reaction, we harness the structural rigidity that targeted dityrosine crosslinks impart to covalently stabilize fusion proteins in their native conformations. We show that the prefusion conformation of respiratory syncytial virus fusion protein can be stabilized with two engineered dityrosine crosslinks (DT-preF), markedly improving its stability and shelf-life. Furthermore, it has 11X greater potency as compared with the DS-Cav1 stabilized prefusion F protein in immunogenicity studies and overcomes immunosenescence in mice with simply a high-dose formulation on alum.
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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.