Neuraminidase protein Influenza B virus Yamagata lineage (NA (for neuraminidase is standard in virology, but not specific to lineage—use with caution))

Neuraminidase is one of two major surface glycoproteins of the Influenza B virus (the other being hemagglutinin), assembling as a tetramer with distinct head and stalk domains[2][4][7]. In the Yamagata lineage of Influenza B, this enzyme catalyzes the removal of terminal sialic acid residues from host cell glycoproteins and glycolipids[2][4][7]. This activity is crucial for viral replication: it facilitates the release of new virions from infected cells, prevents aggregation of viral particles, and enables penetration of mucus barriers by cleaving sialylated mucins[2][4]. Neuraminidase is the target of the only FDA-approved class of antiviral drugs for Influenza B—the neuraminidase inhibitors—making it a pivotal molecule in therapeutic intervention[1][4][3]. The Yamagata lineage is defined phylogenetically and antigenically, with amino acid substitutions in NA influencing drug susceptibility and immune responses[1][5]. Mutations in NA can confer resistance to inhibitors and modulate cross-lineage immunity, posing challenges for treatment and vaccine development[1][3][5].

Other names

Neuraminidase (NA)Influenza B neuraminidase Yamagata lineageNA protein IBV YamagataSialidase (less commonly)

Competitive inhibition of neuraminidase catalytic activity, preventing sialic acid cleavage, resulting in trapping of virus on host cell and blocking release of progeny virions