ArticleJournal of virology2013
Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Trimeric hemagglutinin vaccine provides chickens complete protection against lethal H5 subtype avian influenza virus from clade 2.3.4.4b.Emerging microbes & infections · 2026Article
- Evaluation of an ESAT-6 Recombinant Skin Test Reagent for Bovine Tuberculosis Diagnosis in Guinea Pigs and Cattle.International journal of molecular sciences · 2026Article
- Enhancing Vaccine Immunogenicity of H9N2 Influenza HA by Locking Its Pre-Fusion Conformation via Cleavage Site Engineering.Veterinary sciences · 2026Article
- A Recombinant Mosaic HAs Influenza Vaccine Elicits Broad-Spectrum Immune Response and Protection of Influenza a Viruses.Vaccines · 2024Article
- Effect of Antigen Structure in Subunit Vaccine Nanoparticles on Humoral Immune Responses.ACS biomaterials science & engineering · 2023Article
- Trimeric, APC-Targeted Subunit Vaccines Protect Mice against Seasonal and Pandemic Influenza.Journal of virology · 2023Article
- An ELISA-based assay for determining haemagglutinin potency in egg, cell, or recombinant protein derived influenza vaccines.Frontiers in immunology · 2023Article
- Surfactant protein A alters endosomal trafficking of influenza A virus in macrophages.Frontiers in immunology · 2023Article
- Structural Stability and Antigenicity of Universal Equine H3N8 Hemagglutinin Trimer upon Release from Polyanhydride Nanoparticles and Pentablock Copolymer Hydrogels.ACS biomaterials science & engineering · 2022Article
- Influenza Hemagglutinin Head Domain Mimicry by Rational Design.The protein journal · 2020Article
- Influenza Hemagglutinin and Neuraminidase: Yin⁻Yang Proteins Coevolving to Thwart Immunity.Viruses · 2019Review
- Article
- Eliciting unnatural immune responses by activating cryptic epitopes in viral antigens.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Oligomerization of bacterially expressed H1N1 recombinant hemagglutinin contributes to protection against viral challenge.Scientific reports · 2018Article
- IFITM3 requires an amphipathic helix for antiviral activity.EMBO reports · 2017Article
- Conformational modulation of influenza virus hemagglutinin: characterization and in vivo efficacy of monomeric form.Scientific reports · 2017Article
- Article
- Complete mapping of viral escape from neutralizing antibodies.PLoS pathogens · 2017Article
- Influenza A virus hemagglutinin specific antibodies interfere with virion neuraminidase activity via two distinct mechanisms.Virology · 2017Article
- Broadly-Reactive Neutralizing and Non-neutralizing Antibodies Directed against the H7 Influenza Virus Hemagglutinin Reveal Divergent Mechanisms of Protection.PLoS pathogens · 2016Article
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Authors and funding
8 authors.
Funding
Abstract
Influenza A virus (IAV) remains an important human pathogen largely because of antigenic drift, the rapid emergence of antibody escape mutants that precludes durable vaccination. The most potent neutralizing antibodies interact with cognate epitopes in the globular "head" domain of hemagglutinin (HA), a homotrimeric glycoprotein. The H1 HA possesses five distinct regions defined by a large number of mouse monoclonal antibodies (MAbs), i.e., Ca1, Ca2, Cb, Sa, and Sb. Ca1-Ca2 sites require HA trimerization to attain full antigenicity, consistent with their locations on opposite sides of the trimer interface. Here, we show that full antigenicity of Cb and Sa sites also requires HA trimerization, as revealed by immunofluorescence microscopy of IAV-infected cells and biochemically by pulse-chase radiolabeling experiments. Surprisingly, epitope antigenicity acquired by HA trimerization persists following acid triggering of the globular domains dissociation and even after proteolytic release of monomeric heads from acid-treated HA. Thus, the requirement for HA trimerization by trimer-specific MAbs mapping to the Ca, Cb, and Sa sites is not dependent upon the bridging of adjacent monomers in the native HA trimer. Rather, complete antigenicity of HA (and, by inference, immunogenicity) requires a final folding step that accompanies its trimerization. Once this conformational change occurs, HA trimers themselves would not necessarily be required to induce a highly diverse neutralizing response to epitopes in the globular domain.
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