Influenza B virus neuraminidase (NA) (NA)

Influenza B virus neuraminidase (NA) is a tetrameric surface glycoprotein that acts as a glycosyl hydrolase, specifically an exo-alpha-sialidase (UniProt: P03474). Its primary biological function is to cleave terminal sialic acid residues from host cell receptors and viral hemagglutinin, which is essential for the release of newly formed virions from the surface of infected cells (PubMed: 22226115). By preventing the aggregation of progeny viruses, NA facilitates the spread of infection throughout the respiratory tract and helps the virus navigate through sialic acid-rich mucus (NCBI: NBK541092). In the context of disease, NA is a major antigenic determinant and a key therapeutic target for treating Influenza B infections. Neuraminidase inhibitors (NAIs), such as oseltamivir and zanamivir, competitively bind to the highly conserved active site of the enzyme, effectively halting viral dissemination (StatPearls: NBK539909). However, the emergence of resistance mutations, such as R152K or D198E, poses a significant challenge to the long-term efficacy of these treatments (PubMed: 25100868). Monitoring NA activity and genetic variations is critical for managing seasonal influenza outbreaks and ensuring the effectiveness of antiviral stockpiles.

Other names

NeuraminidaseSialidaseB/NAExo-alpha-sialidaseInfluenza B virus NA

Neuraminidase inhibitors competitively bind to the highly conserved active site of the enzyme, preventing the cleavage of terminal sialic acid residues from host cell receptors and viral glycoproteins, which traps newly formed virions on the host cell surface and prevents further infection (StatPearls: NBK539909).