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• W4383314293 endingPage "e3002182" @default.
• W4383314293 startingPage "e3002182" @default.
• W4383314293 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." @default.
• W4383314293 created "2023-07-07" @default.
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• W4383314293 date "2023-07-06" @default.
• W4383314293 modified "2023-10-18" @default.
• W4383314293 title "Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells" @default.
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• W4383314293 doi "https://doi.org/10.1371/journal.pbio.3002182" @default.
• W4383314293 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37410798" @default.
• W4383314293 hasPublicationYear "2023" @default.
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