ArticleScientific reports2023
Structural characterisation of hemagglutinin from seven Influenza A H1N1 strains reveal diversity in the C05 antibody recognition site.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026Article
- BCRInsight: an antibody language model to decode biological signals from BCR sequences.Briefings in bioinformatics · 2026Article
- Evolution of multivalent supramolecular assemblies of aptamers with target-defined spatial organization.Nature nanotechnology · 2025Article
- Dynamic adaptation mutations and pathogenic characterization of a mouse-adapted seasonal human H3N2 influenza virus.Virology journal · 2025Article
- Understanding the pandemic potential of the avian influenza Virus- key insights into pathogenesis, transmission, and host immunity.Archives of microbiology · 2025Review
- An intranasally administered IgM protects against antigenically distinct subtypes of influenza A viruses.Nature communications · 2025Article
- Challenges in Humoral Immune Response to Adeno-Associated Viruses Determination.International journal of molecular sciences · 2025Review
- Evolutionary dynamics and molecular epidemiology of H1N1 pandemic 2009 influenza A viruses across swine farms in Denmark.Virus evolution · 2025Article
- Co-injection with inactivatedFrontiers in microbiology · 2025Article
- Use of equine H3N8 hemagglutinin as a broadly protective influenza vaccine immunogen.NPJ vaccines · 2024Article
- A predicted model-aided reconstruction algorithm for X-ray free-electron laser single-particle imaging.IUCrJ · 2024Article
- Role of homologous recombination/recombineering on human adenovirus genome engineering: Not the only but the most competent solution.Engineering microbiology · 2024Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Influenza virus (IV) causes several outbreaks of the flu each year resulting in an economic burden to the healthcare system in the billions of dollars. Several influenza pandemics have occurred during the last century and estimated to have caused 100 million deaths. There are four genera of IV, A (IVA), B (IVB), C (IVC), and D (IVD), with IVA being the most virulent to the human population. Hemagglutinin (HA) is an IVA surface protein that allows the virus to attach to host cell receptors and enter the cell. Here we have characterised the high-resolution structures of seven IVA HAs, with one in complex with the anti-influenza head-binding antibody C05. Our analysis revealed conserved receptor binding residues in all structures, as seen in previously characterised IV HAs. Amino acid conservation is more prevalent on the stalk than the receptor binding domain (RBD; also called the head domain), allowing the virus to escape from antibodies targeting the RBD. The equivalent site of C05 antibody binding to A/Denver/57 HA appears hypervariable in the other H1N1 IV HAs. Modifications within this region appear to disrupt binding of the C05 antibody, as these HAs no longer bind the C05 antibody by analytical SEC. Our study brings new insights into the structural and functional recognition of IV HA proteins and can contribute to further development of anti-influenza vaccines.
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