Influenza B virus neuraminidase (NA (for neuraminidase))

Influenza B virus neuraminidase is a viral surface enzyme (glycoprotein) essential for the propagation of Influenza B virus. It catalyzes the removal of terminal sialic acid residues from host glycoproteins and glycolipids, which is critical for efficient release of new virus particles from infected cells and for the spread of infection within the respiratory tract[1][3][4][5][6]. Neuraminidase is a homotetrameric protein with a well-conserved active site, making it a principal target of several antiviral drugs (neuraminidase inhibitors) used for both treatment and prevention of influenza[2][3][6][8]. Monoclonal antibodies and novel drug conjugates targeting this protein are under investigation to overcome current therapeutic challenges, such as resistance. Neuraminidase is also a key antigenic determinant of influenza viruses used in classification and is less prone to genetic drift compared to hemagglutinin, but mutations do arise that can compromise drug effectiveness or immune recognition[1][4][6].

Other names

Influenza B neuraminidaseIBV neuraminidaseNA (Influenza B)Sialidase (in enzymology, but less commonly used specifically for Influenza B NA)

Competitive inhibition of neuraminidase active site by sialic acid analogues (NA inhibitors), preventing cleavage of sialic acid and inhibiting release of progeny virions. Monoclonal antibodies block enzymatic activity and interfere with viral egress, also mediate immune-effector functions (e.g., ADCC).