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Influenza A virus neuraminidase protein (NA) is a tetrameric enzyme exposed on the surface of influenza virions as mushroom-shaped spikes, alongside hemagglutinin. NA is essential for efficient viral replication, mediating the cleavage of sialic acid residues from host and viral glycoproteins. This action is crucial for releasing newly formed viral particles from infected cells, preventing self-aggregation, and facilitating spread to new host cells. Nine subtypes of NA exist in influenza A, with N1 characteristic of H1N1. The protein's catalytic site is the target of widely used antivirals, with mutations in NA responsible for drug resistance and epidemiological shifts. NA structure consists of four functional domains: cytoplasmic tail, transmembrane region, stalk, and catalytic head. Its high mutation rate contributes to the emergence of new viral strains. NA plays a significant role in influenza disease dynamics and is continually studied for new therapeutic strategies and vaccine development.
Drugs competitively or covalently inhibit the active site of neuraminidase, blocking cleavage of sialic acid and impairing viral release from host cells
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