Receptor binding and pH stability — How influenza A virus hemagglutinin affects host-specific virus infection |
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| Authors: | Caroline M. Mair Kai Ludwig Andreas Herrmann Christian Sieben |
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| Affiliation: | 1. Group of Molecular Biophysics, Institute of Biology, Humboldt University Berlin, Invalidenstraße 42, 10115 Berlin, Germany;2. Research center of Electron Microscopy, Institute of Chemistry and Biochemistry, Free University Berlin, Fabeckstraße 36a, 14195 Berlin, Germany |
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| Abstract: | Influenza A virus strains adopt different host specificities mainly depending on their hemagglutinin (HA) protein. Via HA, the virus binds sialic acid receptors of the host cell and, upon endocytic uptake, HA triggers fusion between the viral envelope bilayer and the endosomal membrane by a low pH-induced conformational change leading to the release of the viral genome into the host cell cytoplasm. Both functions are crucial for viral infection enabling the genesis of new progeny virus. |
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| Keywords: | BHA, bromelain-cleaved hemagglutinin E&prime , vestigial esterase subdomain of the HA1 subunit of hemagglutinin F&prime , fusion subdomain of the HA1 subunit of hemagglutinin F, fusion subdomain of the HA2 subunit of hemagglutinin HA, hemagglutinin protein HA0, pre-cursor (uncleaved form) of the hemagglutinin protein HPAIV, highly pathogenic avian influenza virus LPAIV, low pathogenic avian influenza virus NA, neuraminidase of influenza virus NP, nucleoprotein of influenza virus R, receptor binding domain of the HA1 subunit of hemagglutinin RBS, receptor binding site of hemagglutinin RNPs, ribonucleoproteins (viral RNA and NP) SA, N-acetyl-neuraminic acid generally termed as sialic acid SAα-2,3Gal, sialic acid linked to different carbohydrates by an α-2,3 glycosidic bond SAα-2,6Gal, sialic acid linked to different carbohydrates by an α-2,6 glycosidic bond TBHA2, BHA without HA1 at low pH |
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