Neuraminidase (Influenza A virus H1N1) (NA)

Neuraminidase (NA) is a major surface glycoprotein and essential enzyme of the Influenza A H1N1 virus, functioning as a mushroom-shaped homotetramer on the viral envelope [1, 12, 14]. Its primary biological role is to catalyze the cleavage of terminal sialic acid residues from viral and cellular glycoconjugates, which is critical for the release of progeny virions from infected host cells and the prevention of viral self-aggregation [1, 13, 19]. Additionally, NA facilitates the movement of the virus through the respiratory tract by degrading sialic acids in the protective mucus layer, thereby promoting infection of the underlying epithelial cells [1, 14, 18]. As a key therapeutic target, NA is the focus of neuraminidase inhibitors like oseltamivir and zanamivir, which competitively bind to its highly conserved active site to halt viral propagation [8, 10, 15]. Beyond its enzymatic function, NA is a significant antigen that elicits protective antibodies, making it a vital component in the development of seasonal and pandemic influenza vaccines [6, 9, 11]. However, the clinical utility of NA-targeting drugs is constantly challenged by the emergence of resistant strains, such as those carrying the H275Y mutation, which necessitates ongoing genomic surveillance and the development of next-generation antivirals [13, 16, 18].

Other names

SialidaseExo-alpha-sialidaseN1 neuraminidaseNAReceptor-destroying enzyme

Neuraminidase inhibitor [8, 13, 17]