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Influenza A H5N1 neuraminidase is a viral surface glycoprotein enzyme (exosialidase, EC 3.2.1.18) with a tetrameric structure located on the envelope of influenza virions[2]. It catalyzes cleavage of terminal sialic acids from host cell surface glycoproteins and glycolipids, a process necessary for efficient virus release and spread during infection[2][3][4]. NA is a critical target for antiviral drugs, and its structure and substrate specificity underlie both its catalytic function and susceptibility to drug inhibition. Variations in the NA gene and protein can confer resistance to currently approved inhibitors, making it a central focus in influenza drug and vaccine development[2][3][4].
Competitive inhibition of the NA active site by mimicking the sialic acid substrate, thus preventing release of viral particles from infected host cells
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