ArticleProceedings of the National Academy of Sciences of the United States of America2022
Universal stabilization of the influenza hemagglutinin by structure-based redesign of the pH switch regions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- A group 1 hemagglutinin stem vaccine elicits broad humoral responses against influenza in phase 1/2a study.Nature communications · 2026Trial
- In silico analysis of pH stabilising mutations of hemagglutinin of influenza A virus H5N1 clade 2.3.4.4b.Npj viruses · 2026Review
- Symmetry-breaking antibody binding reveals extensive capsid malleability in pandemic human norovirus.Research square · 2026Article
- Aligning protein-generative models to experimental fitness with ProteinDPO.Nature methods · 2026Article
- Single-component self-assembling protein nanoparticles displaying stabilized prefusion-closed hemagglutinin trimers for influenza vaccine development.Nature communications · 2026Article
- An In Vitro Screen Identifies H1 Influenza Hemagglutinin Substitutions That Alter mRNA-LNP Vaccine Responses Against the Stalk Domain.Vaccines · 2026Article
- Defining the molecular interaction between influenza hemagglutinin and MHC-II.bioRxiv : the preprint server for biology · 2026Article
- New determinant of influenza hemagglutinin cleavability identified through random mutagenesis for acid-stabilizing mutations.Microbiology spectrum · 2026Article
- Stabilized mosaic hemagglutinin immunogens as novel universal influenza virus vaccines.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- Structure-Guided Glycosylation of Hemagglutinin Enhances Stability and Modulates Immunogenicity of Influenza Vaccines.Vaccines · 2026Article
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Stabilization of the H5 clade 2.3.4.4b hemagglutinin improves vaccine-elicited neutralizing antibody responses in mice.Science translational medicine · 2026Article
- Panzootic H5 influenza viruses acquired resistance to human head interface antibodies.PLoS pathogens · 2026Article
- HERMES: Holographic Equivariant neuRal network model for Mutational Effect and Stability prediction.bioRxiv : the preprint server for biology · 2026Article
- Article
- Protective and pathogenic antibody responses from a primate Shigella outbreak inform vaccine design.bioRxiv : the preprint server for biology · 2025Article
- Host switching mutations in H5N1 influenza hemagglutinin suppress site-specific activation dynamics.Nature communications · 2025Article
- H5N1 influenza virus stability and transmission risk in raw milk and cheese.Nature medicine · 2025Article
- Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B.Nature microbiology · 2025Article
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For an efficacious vaccine immunogen, influenza hemagglutinin (HA) needs to maintain a stable quaternary structure, which is contrary to the inherently dynamic and metastable nature of class I fusion proteins. In this study, we stabilized HA with three substitutions within its pH-sensitive regions where the refolding starts. An X-ray structure reveals how these substitutions stabilize the intersubunit β-sheet in the base and form an interprotomeric aliphatic layer across the stem while the native prefusion HA fold is retained. The identification of the stabilizing substitutions increases our understanding of how the pH sensitivity is structurally accomplished in HA and possibly other pH-sensitive class I fusion proteins. Our stabilization approach in combination with the occasional back mutation of rare amino acids to consensus results in well-expressing stable trimeric HAs. This repair and stabilization approach, which proves broadly applicable to all tested influenza A HAs of group 1 and 2, will improve the developability of influenza vaccines based on different types of platforms and formats and can potentially improve efficacy.
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