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- W2103566910 abstract "Receptor-binding specificity of HA, the major surface glycoprotein of influenza virus, primarily determines the host ranges that the virus can infect. Influenza type B virus almost exclusively infects humans and contributes to the annual “flu” sickness. Here we report the structures of influenza B virus HA in complex with human and avian receptor analogs, respectively. These structures provide a structural basis for the different receptor-binding properties of influenza A and B virus HA molecules and for the ability of influenza B virus HA to distinguish human and avian receptors. The structure of influenza B virus HA with avian receptor analog also reveals how mutations in the region of residues 194 to 196, which are frequently observed in egg-adapted and naturally occurring variants, directly affect the receptor binding of the resultant virus strains. Furthermore, these structures of influenza B virus HA are compared with known structures of influenza A virus HAs, which suggests the role of the residue at 222 as a key and likely a universal determinant for the different binding modes of human receptor analogs by different HA molecules." @default.
- W2103566910 created "2016-06-24" @default.
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- W2103566910 creator A5053873921 @default.
- W2103566910 creator A5071316360 @default.
- W2103566910 creator A5076174923 @default.
- W2103566910 date "2007-10-23" @default.
- W2103566910 modified "2023-09-23" @default.
- W2103566910 title "Structural basis for receptor specificity of influenza B virus hemagglutinin" @default.
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- W2103566910 doi "https://doi.org/10.1073/pnas.0708363104" @default.
- W2103566910 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2040455" @default.
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