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The **Influenza B virus neuraminidase protein** is a tetrameric, surface-exposed glycoprotein enzyme critical to the life cycle of the influenza B virus. It catalyzes the removal of terminal sialic acid residues from glycoproteins and glycolipids on the surface of infected host cells. This enzymatic action allows new virions to be released from the host cell, thereby facilitating the spread of infection to other cells. Neuraminidase is a key determinant of viral infectivity and an essential target for antiviral drugs such as oseltamivir and zanamivir, which function by inhibiting its catalytic activity. Resistance to neuraminidase inhibitors can arise through mutation, posing challenges for disease management. The protein is antigenic and, along with hemagglutinin, is used for viral classification and subtype determination. Neuraminidase is a principle component of the host immune response to influenza, and genetic variation in this protein can contribute to immune escape and pandemic risk[1][2][3][7].
Competitive inhibition of neuraminidase active site, preventing cleavage of sialic acid and subsequent release of viral particles from host cells
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