ArticlemBio2016
Cryo-electron Microscopy Structures of Chimeric Hemagglutinin Displayed on a Universal Influenza Vaccine Candidate.
Article in mBio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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Who cites it
30 citing papers in PubMed, 36 citations in OpenAlex.
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- Cryo-ET of IgG bivalent binding on SARS-CoV-2 provides structural basis for antibody avidity.Nature communications · 2026Article
- Subnanometer-resolution Structural Determination of Hemagglutinin from Cryo-electron Tomography of Influenza Viruses.Journal of visualized experiments : JoVE · 2025Article
- Virion-associated influenza hemagglutinin clusters upon sialic acid binding visualized by cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Structural characterization of influenza group 1 chimeric hemagglutinins as broad vaccine immunogens.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Disulfide-stabilized trimeric hemagglutinin ectodomains provide enhanced heterologous influenza protection.Emerging microbes & infections · 2024Article
- Structure-guided assembly of an influenza spike nanobicelle vaccine provides pan H1 intranasal protection.bioRxiv : the preprint server for biology · 2024Article
- Designed nanoparticles elicit cross-reactive antibody responses to conserved influenza virus hemagglutinin stem epitopes.PLoS pathogens · 2023Article
- Influenza chimeric hemagglutinin structures in complex with broadly protective antibodies to the stem and trimer interface.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Quantitative structural analysis of influenza virus by cryo-electron tomography and convolutional neural networks.Structure (London, England : 1993) · 2022Article
- Visualising Viruses.The Journal of general virology · 2022Review
- Next-Generation Influenza HA Immunogens and Adjuvants in Pursuit of a Broadly Protective Vaccine.Viruses · 2021Review
- Defining and Manipulating B Cell Immunodominance Hierarchies to Elicit Broadly Neutralizing Antibody Responses against Influenza Virus.Cell systems · 2020Article
- Cryo-EM Studies of Virus-Antibody Immune Complexes.Virologica Sinica · 2020Review
- Cross-Reactive Antibodies Binding to the Influenza Virus Subtype H11 Hemagglutinin.Pathogens (Basel, Switzerland) · 2019Article
- Cross-reactive antibodies binding to H4 hemagglutinin protect against a lethal H4N6 influenza virus challenge in the mouse model.Emerging microbes & infections · 2019Article
- Structural analysis of influenza vaccine virus-like particles reveals a multicomponent organization.Scientific reports · 2018Article
- Is It Possible to Develop a "Universal" Influenza Virus Vaccine? Potential for a Universal Influenza Vaccine.Cold Spring Harbor perspectives in biology · 2018Review
- Microbiology catches the cryo-EM bug.Current opinion in microbiology · 2018Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
unlabelledInfluenza viruses expressing chimeric hemagglutinins (HAs) are important tools in the quest for a universal vaccine. Using cryo-electron tomography, we have determined the structures of a chimeric HA variant that comprises an H1 stalk and an H5 globular head domain (cH5/1 HA) in native and antibody-bound states. We show that cH5/1 HA is structurally different from native HA, displaying a 60° rotation between the stalk and head groups, leading to a novel and unexpected "open" arrangement of HA trimers. cH5/1N1 viruses also display higher glycoprotein density than pH1N1 or H5N1 viruses, but despite these differences, antibodies that target either the stalk or head domains of hemagglutinins still bind to cH5/1 HA with the same consequences as those observed with native H1 or H5 HA. Our results show that a large range of structural plasticity can be tolerated in the chimeric spike scaffold without disrupting structural and geometric aspects of antibody binding. IMPORTANCE: Chimeric hemagglutinin proteins are set to undergo human clinical trials as a universal influenza vaccine candidate, yet no structural information for these proteins is available. Using cryo-electron tomography, we report the first three-dimensional (3D) visualization of chimeric hemagglutinin proteins displayed on the surface of the influenza virus. We show that, unexpectedly, the chimeric hemagglutinin structure differs from those of naturally occurring hemagglutinins by displaying a more open head domain and a dramatically twisted head/stalk arrangement. Despite this unusual spatial relationship between head and stalk regions, virus preparations expressing the chimeric hemagglutinin are fully infectious and display a high glycoprotein density, which likely helps induction of a broadly protective immune response.
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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.