Neuraminidase (subtype N1) (NA) (NA)

N1 neuraminidase is a major surface glycoprotein and essential enzyme of the Influenza A virus, particularly prominent in pandemic-associated subtypes such as H1N1 and H5N1 [1, 2]. As an exo-alpha-sialidase, it catalyzes the cleavage of terminal sialic acid residues from glycoproteins and glycolipids on the host cell surface and the viral envelope [2, 5]. This activity is crucial for the release of progeny virions from infected cells, as it prevents the hemagglutinin protein from rebinding to the cell surface and avoids viral self-aggregation [7, 11]. Furthermore, the enzyme facilitates viral movement through the respiratory tract by degrading sialic acid-rich mucins that would otherwise trap the virus [8, 10]. N1 neuraminidase is the primary target for several FDA-approved antiviral drugs, including oseltamivir and zanamivir, which act as competitive inhibitors to block viral spread [13, 14]. However, the clinical utility of these drugs is frequently challenged by the emergence of resistance mutations, such as the H275Y substitution, which significantly reduces drug binding affinity [11, 20].

Other names

SialidaseExo-alpha-sialidaseReceptor-destroying enzymeN1NA

Neuraminidase inhibition