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Neuraminidase of Influenza A virus subtype H1N1 is a tetrameric viral surface enzyme (sialidase) responsible for cleaving terminal sialic acids from host cell glycoproteins and glycolipids, a critical step for the release of newly formed viral particles. The enzyme consists of approximately 470 amino acids per monomer and forms a mushroom-like structure with a globular head and a stalk anchored in the viral membrane. The N1 neuraminidase, together with hemagglutinin, defines the H1N1 influenza subtype and contributes to viral infectivity, immune escape, and transmission. It is the target for several antiviral drugs—neuraminidase inhibitors—that block its enzymatic activity, thereby reducing viral spread. Its high mutation rate and the emergence of drug resistance remain major therapeutic and public health challenges.
Competitive inhibition of the neuraminidase active site; Blocking sialic acid cleavage, preventing viral progeny release from host cells, thereby limiting infection spread
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