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Influenza A virus neuraminidase N1 is a tetrameric surface glycoprotein enzyme belonging to group 1 NA subtypes, featuring a globular head domain with a conserved active site formed by eight inner shell residues (Arg118, Asp151, Arg152, Arg224, Glu276, Arg292, Arg371, Tyr406) that directly interact with sialic acid substrates and framework residues for structural stability. It includes a flexible 150-loop (residues 147-152) creating an additional cavity adjacent to the active site, calcium-binding sites for stability, and N-linked glycosylation sites. N1 cleaves terminal sialic acids from viral and cellular glycoconjugates, enabling virion release from host cells, preventing aggregation via hemagglutinin-sialic acid interactions, and facilitating virus penetration through respiratory mucins during infection.
Competitive inhibition of sialic acid cleavage by mimicking transition state of hydrolysis
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