ArticlePLoS biology2023
Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells.
Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- The receptor landscape of influenza A viruses.Journal of virology · 2026Review
- H5N1 influenza binding and cell entry via human class II MHC, and blocking by cross-reactive antibodies.bioRxiv : the preprint server for biology · 2026Article
- Defining the molecular interaction between influenza hemagglutinin and MHC-II.bioRxiv : the preprint server for biology · 2026Article
- MHC class II functions as a host-specific entry receptor for representative human and swine H3N2 influenza A viruses.Nature communications · 2026Article
- A new path to spillover: MHC-II entry of influenza A viruses.PLoS biology · 2025Article
- The bat influenza A virus subtype H18N11 induces nanoscale MHCII clustering upon host cell attachment.Nature communications · 2025Article
- Review
- MHC class II proteins mediate sialic acid independent entry of human and avian H2N2 influenza A viruses.Nature microbiology · 2024Article
- H19 influenza A virus exhibits species-specific MHC class II receptor usage.Cell host & microbe · 2024Article
- Deciphering bat influenza H18N11 infection dynamics in male Jamaican fruit bats on a single-cell level.Nature communications · 2024Article
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II (MHC-II) for cell entry. MHC-II proteins from various vertebrate species can facilitate infection with the bat IAV H18N11. Yet, it has been difficult to biochemically determine the H18:MHC-II binding. Here, we followed a different approach and generated MHC-II chimeras from the human leukocyte antigen DR (HLA-DR), which supports H18-mediated entry, and the nonclassical MHC-II molecule HLA-DM, which does not. In this context, viral entry was supported only by a chimera containing the HLA-DR α1, α2, and β1 domains. Subsequent modeling of the H18:HLA-DR interaction identified the α2 domain as central for this interaction. Further mutational analyses revealed highly conserved amino acids within loop 4 (N149) and β-sheet 6 (V190) of the α2 domain as critical for virus entry. This suggests that conserved residues in the α1, α2, and β1 domains of MHC-II mediate H18-binding and virus propagation. The conservation of MHC-II amino acids, which are critical for H18N11 binding, may explain the broad species specificity of this virus.
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