Influenza A virus neuraminidase subtype 2 (Neuraminidase N2 (NA2))

Influenza A virus neuraminidase subtype 2 is an enzyme present on the surface of influenza A viruses, classified as a glycoside hydrolase that catalyzes the removal of terminal sialic acid residues from both host cell receptors and viral glycoproteins. This activity is essential for the release of newly formed viral particles from infected host cells and for preventing self-aggregation of virions, thereby enhancing viral spread. Neuraminidase is a tetrameric protein comprising several domains (cytoplasmic, transmembrane, head, stem) and the N2 subtype is one of nine known for influenza A virus, grouped phylogenetically into two classes[1][3][4]. As a major target for antiviral drug development, N2 is inhibited by several licensed drugs, though resistance through specific mutations (notably H274Y) presents ongoing therapeutic challenges[2][4]. The understanding of neuraminidase’s structure and function underpins rational inhibitor design and monitoring for resistance determinants in clinical virology.

Other names

NA (N2)Influenza A neuraminidase N2Viral neuraminidase N2

Drugs bind to the active site of neuraminidase, inhibiting its enzymatic activity and blocking the release of new virions from infected cells[2][4] Resistance mutations (notably H274Y) can decrease drug binding and efficacy[4]