Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins
By S. Gamblin, J. Skehel. Journal of Biological Chemistry, 2010
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Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target cells is mediated by hemagglutinin, which acquires characteristic changes in its receptor-binding site to switch its host from avian species to humans. Anti-influenza drugs mimic the natural sialic acid substrate of the virus neuraminidase enzyme but utilize the much tighter binding of the drugs for efficacy. Resistance to one of the two main antiviral drugs is differentially acquired by the two distinct subsets of neuraminidase as a consequence of structural differences in the enzyme active site between the two phylogenetic groups.
Subfields: Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/ac3bf46fa9aeb57357da223a1332a667d1979460
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Citations in the corpus
- Glycan repositioning of influenza hemagglutinin stem facilitates the elicitation of protective cross-group antibody responses (2020, unknown): “3, 4 ).”
- New World Bats Harbor Diverse Influenza A Viruses (2013, background): “In contrast, H18 HA has a dramatic alteration of the binding site residues (Fig.”
- A Hemagglutinin Stem Vaccine Designed Rationally by AlphaFold2 Confers Broad Protection against Influenza B Infection (2022, background): “It plays a vital role in the life cycle of the influenza virus by engaging sialic acid receptors on host cell surface to mediate viral attachment, virus–host membrane fusion and infection [7].”