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The Influenza A virus H1N1 neuraminidase (NA, N1 subtype) is a tetrameric glycoprotein enzyme on the viral envelope surface, consisting of four identical ~470-amino-acid subunits with cytoplasmic tail, transmembrane, stalk, and catalytic head domains. Its active site, a conserved cavity formed by residues like Arg118, Asp151, Arg152, Arg224, Glu276, Arg292, Arg371, and Tyr406, hydrolyzes α2-3- and α2-6-linked sialic acids (Neu5Ac). This enables virion release from infected cells by preventing HA-mediated aggregation, aids penetration through sialylated respiratory mucins, and may contribute to entry via receptor clearance. Group 1 NAs like N1 feature a dynamic 150-loop creating a secondary cavity near the active site. NA balances HA function for viral fitness and is a key antiviral target.
Competitive inhibition of sialic acid cleavage by mimicking the transition state of the hydrolysis reaction
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