ArticleJournal of virology2012
A virus-like particle that elicits cross-reactive antibodies to the conserved stem of influenza virus hemagglutinin.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 80 citations in OpenAlex.
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- Computationally designed stem-epitope mimetics elicit broadly reactive antibodies.bioRxiv : the preprint server for biology · 2025Article
- Administration of antigenically distinct influenza viral particle combinations as an influenza vaccine strategy.PLoS pathogens · 2025Article
- Headless hemagglutinin-containing influenza viral particles direct immune responses toward more conserved epitopes.Journal of virology · 2024Article
- Phase 1 dose-escalation trial evaluating a group 2 influenza hemagglutinin stabilized stem nanoparticle vaccine.NPJ vaccines · 2024Article
- Vaccination with antigenically complex hemagglutinin mixtures confers broad protection from influenza disease.Science translational medicine · 2024Article
- Designed nanoparticles elicit cross-reactive antibody responses to conserved influenza virus hemagglutinin stem epitopes.PLoS pathogens · 2023Article
- Flagellin-Fused Protein Targeting M2e and HA2 Induces Innate and T-Cell Responses in Mice of Different Genetic Lines.Vaccines · 2022Article
- Potential of conserved antigenic sites in development of universal SARS-like coronavirus vaccines.Frontiers in immunology · 2022Article
- Protein engineering strategies for rational immunogen design.NPJ vaccines · 2021Review
- Antibody Focusing to Conserved Sites of Vulnerability: The Immunological Pathways for 'Universal' Influenza Vaccines.Vaccines · 2021Review
- Comparative Analyses of the Antiviral Activities of IgG and IgA Antibodies to Influenza A Virus M2 Protein.Viruses · 2020Article
- Potential Role of Nonneutralizing IgA Antibodies in Cross-Protective Immunity against Influenza A Viruses of Multiple Hemagglutinin Subtypes.Journal of virology · 2020Article
- [Vaccine of the future].Revue francophone des laboratoires : RFL · 2019Article
- Synthetic biology for bioengineering virus-like particle vaccines.Biotechnology and bioengineering · 2019Review
- Article
- Epitope targeting with self-assembled peptide vaccines.NPJ vaccines · 2019Article
- Conformational Stability of the Hemagglutinin of H5N1 Influenza A Viruses Influences Susceptibility to Broadly Neutralizing Stem Antibodies.Journal of virology · 2018Article
- Protein cage assembly across multiple length scales.Chemical Society reviews · 2018Review
- Combination of M2e peptide with stalk HA epitopes of influenza A virus enhances protective properties of recombinant vaccine.PloS one · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The discovery of broadly neutralizing antibodies that recognize highly conserved epitopes in the membrane-proximal region of influenza virus hemagglutinin (HA) has revitalized efforts to develop a universal influenza virus vaccine. This effort will likely require novel immunogens that contain these epitopes but lack the variable and immunodominant epitopes located in the globular head of HA. As a first step toward developing such an immunogen, we investigated whether the 20-residue A-helix of the HA2 chain that forms the major component of the epitope of broadly neutralizing antibodies CR6261, F10, and others is sufficient by itself to elicit antibodies with similarly broad antiviral activity. Here, we report the multivalent display of the A-helix on icosahedral virus-like particles (VLPs) derived from the capsid of Flock House virus. Mice immunized with VLPs displaying 180 copies/particle of the A-helix produced antibodies that recognized trimeric HA and the elicited antibodies had binding characteristics similar to those of CR6261 and F10: they recognized multiple HA subtypes from group 1 but not from group 2. However, the anti-A-helix antibodies did not neutralize influenza virus. These results indicate that further engineering of the transplanted peptide is required and that display of additional regions of the epitope may be necessary to achieve protection.
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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.