Influenza A H5N1 virus neuraminidase (NA (commonly used), specifically "H5N1 NA" for this subtype)

Neuraminidase from the influenza A H5N1 virus is a viral surface enzyme whose primary role is to cleave terminal sialic acids from glycoconjugates on the host cell surface[1][2]. This action is crucial for the release of newly formed viral particles from infected cells and for efficient viral spread. Neuraminidase is a homotetrameric membrane glycoprotein, with each monomer consisting of ~470 amino acids and forming a structurally distinct "head" connected to a stalk and membrane anchor[1]. Nine subtypes of influenza A neuraminidase (N1–N9) are known, with N1 characterizing the pandemic-prone H5N1 subtype. Neuraminidase inhibitors, such as oseltamivir and zanamivir, are clinically effective antivirals that inhibit the enzyme’s activity, thereby preventing viral propagation. Resistance to these drugs can rapidly arise due to mutations in key residues of the neuraminidase active site[1][2]. Neuraminidase’s function is functionally coupled to hemagglutinin (HA), another viral envelope protein, for optimal viral replication, transmission, and tissue tropism[2][1][3]. The activity of H5N1 neuraminidase is linked to the high virulence and pandemic potential of this strain by enabling efficient disengagement of virus from host tissue and evasion of mucin barriers in the respiratory tract[3][1].

Other names

NeuraminidaseNASialidaseN1 neuraminidase (specifically for H5N1)Influenza A virus neuraminidase

Competitive inhibition of sialic acid cleavage, blocking viral release from host cells[2][1]. Prevention of virion spread to new cells by maintaining the binding of newly formed virions on the surface of the infected cell.