ArticleCommunications biology2023
Structural insights into the broad protection against H1 influenza viruses by a computationally optimized hemagglutinin vaccine.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Nanoemulsion adjuvanted COBRA HA vaccine enhances protective antibody titers against H1N1 and H3N2 influenza viruses.Human vaccines & immunotherapeutics · 2026Article
- An mRNA Vaccine with Tandem Mutated HA-NA Confers Protection Against Multiple Strains of H1N1 Influenza.Vaccines · 2026Article
- Human broadly neutralizing influenza B virus antibodies recognizing hemagglutinin computationally optimized broadly reactive antigens.Frontiers in immunology · 2026Article
- Assessing the structural boundaries of broadly reactive antibody interactions with diverse H3 influenza hemagglutinin proteins.Journal of virology · 2025Article
- Identification and characterization of a broadly neutralizing and protective nanobody against the HA1 domain of H5 avian influenza virus hemagglutinin.Journal of virology · 2025Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- Synthetic DNA co-immunization with vaccine-aligned common consensus nucleoprotein and hemagglutinin protects mice against lethal influenza infection with a single immunization.Frontiers in immunology · 2025Article
- Unlocking the potential ofFrontiers in bioinformatics · 2025Review
- Leveraging large language models to predict antibody biological activity against influenza A hemagglutinin.Computational and structural biotechnology journal · 2025Article
- Structural basis for the broad antigenicity of the computationally optimized influenza hemagglutinin X6.Structure (London, England : 1993) · 2024Article
- Assessing the Affinity Spectrum of the Antigen-Specific B Cell Repertoire via ImmunoSpotMethods in molecular biology (Clifton, N.J.) · 2024Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Influenza virus poses an ongoing human health threat with pandemic potential. Due to mutations in circulating strains, formulating effective vaccines remains a challenge. The use of computationally optimized broadly reactive antigen (COBRA) hemagglutinin (HA) proteins is a promising vaccine strategy to protect against a wide range of current and future influenza viruses. Though effective in preclinical studies, the mechanistic basis driving the broad reactivity of COBRA proteins remains to be elucidated. Here, we report the crystal structure of the COBRA HA termed P1 and identify antigenic and glycosylation properties that contribute to its immunogenicity. We further report the cryo-EM structure of the P1-elicited broadly neutralizing antibody 1F8 bound to COBRA P1, revealing 1F8 to recognize an atypical receptor binding site epitope via an unexpected mode of binding.
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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.