Influenza hemagglutinin and neuraminidase membrane glycoproteins.

The Journal of biological chemistry (2010-06-12)
Steven J Gamblin, John J Skehel
RESUMEN

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.

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Sigma-Aldrich
Anti-HA−Alkaline Phosphatase antibody, Mouse monoclonal, clone HA-7, purified from hybridoma cell culture
Sigma-Aldrich
Anti-HA (Hemagglutinin) IgG (H+L), CF 594 antibody produced in rabbit, ~1 mg/mL, affinity isolated antibody