Neuraminidase (N2) of influenza A virus (N2)

Neuraminidase (N2) is a tetrameric surface glycoprotein enzyme (EC 3.2.1.18) of influenza A virus, consisting of four ~470-amino-acid monomers with cytoplasmic tail, transmembrane, stalk, and catalytic head domains. It cleaves α-ketosidic linkages of terminal N-acetylneuraminic acid (sialic acid) from glycans, aiding virus entry by clearing respiratory mucins, promoting membrane fusion, and enabling efficient release of progeny virions from host cells by preventing HA-mediated aggregation. The active site features a conserved inner shell of eight residues (e.g., Arg118, Arg152, Glu276, Tyr406 using N2 numbering) for sialic acid binding and catalysis, plus framework residues for structure. N2 belongs to group 2 NA subtypes with specific activity toward α2-3 and α2-6 sialyl linkages, varying by host and isolate. It is a validated antiviral target with inhibitors binding the active site.

Other names

Influenza A virus N2 neuraminidaseN2 neuraminidaseInfluenza neuraminidase subtype N2

Competitive inhibition of sialic acid cleavage by mimicking transition state of hydrolysis, Binding to active site residues blocking substrate access