Influenza A virus neuraminidase (N1 subtype) (NA (N1))

Influenza A virus neuraminidase (N1 subtype) is a major surface glycoprotein and enzyme essential for the life cycle of the influenza A virus. It functions as a sialidase, specifically cleaving terminal sialic acid residues from host cell receptors and newly synthesized viral glycoproteins. This enzymatic activity is crucial for the release of progeny virions from the surface of infected cells, preventing the virus from aggregating and allowing it to spread to uninfected cells within the respiratory tract [UniProt: P03468, PubMed: 21707955]. Additionally, neuraminidase helps the virus navigate through the mucus layer of the respiratory epithelium by degrading sialic acid-containing decoys. Because of its indispensable role in viral dissemination, the N1 subtype is a primary target for antiviral drugs known as neuraminidase inhibitors, such as oseltamivir and zanamivir [NCBI: NBK539909]. These drugs mimic the transition state of sialic acid cleavage to block the enzyme's active site. However, the clinical utility of these treatments is frequently challenged by the development of resistance mutations, most notably the H275Y substitution, which significantly reduces drug binding affinity [PubMed: 24506157].

Other names

SialidaseExo-alpha-sialidaseN1 neuraminidaseNeuraminidase N1Acetylneuraminyl hydrolase

Neuraminidase inhibitors act as transition-state analogues that competitively bind to the enzyme's active site, preventing the cleavage of terminal sialic acid residues on host cell receptors and viral glycoproteins, which traps progeny virions at the cell surface and inhibits further infection spread [StatPearls: NBK539909, PubMed: 22543518].