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Influenza virus neuraminidase (NA) and other split-virion proteins, such as hemagglutinin (HA), represent the primary antigenic and therapeutic targets of the influenza virus. Neuraminidase is a membrane-bound enzyme that cleaves terminal sialic acid residues from host cell glycoproteins, a process essential for the release of newly formed viral particles from the host cell surface (UniProt P03468). Hemagglutinin is responsible for binding the virus to sialic acid receptors on host cells and mediating membrane fusion during viral entry (PubMed PMID: 22226608). In split-virion vaccines, the virus is chemically disrupted by detergents to expose these surface and internal proteins, which then serve as the active components to stimulate the production of protective antibodies (CDC, 2023). Therapeutic interventions typically involve neuraminidase inhibitors, such as oseltamivir and zanamivir, which block the enzyme's active site to prevent the spread of the virus within the respiratory tract (StatPearls NBK539909).
Inhibition of viral neuraminidase to prevent progeny release and induction of neutralizing antibodies against hemagglutinin and neuraminidase to prevent viral entry and spread.
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