Influenza A virus N1 neuraminidase (NA) (NA)

Influenza A virus N1 neuraminidase is a critical surface glycoprotein found on the envelope of the H1N1 pandemic strain [UniProt: C3W5S7]. Its primary biological function is to act as a sialidase, cleaving terminal sialic acid residues from host cell receptors and viral hemagglutinin [PubMed: 22443928]. This enzymatic activity is essential for the release of progeny virions from the surface of infected cells and for preventing viral aggregation, thereby facilitating the spread of the infection throughout the respiratory tract [PubMed: 22443928]. In the context of the 2009 H1N1 pandemic, this specific N1 variant played a central role in viral fitness and transmission [UniProt: C3W5S7]. As a major therapeutic target, it is inhibited by a class of drugs known as neuraminidase inhibitors, including oseltamivir and zanamivir [PubChem: CID 65028]. These drugs mimic the transition state of sialic acid cleavage to competitively bind the active site, effectively halting the viral life cycle [PubMed: 22443928]. Monitoring for mutations like H275Y is vital, as they can significantly reduce drug efficacy and impact clinical outcomes [PubMed: 21148519].

Other names

Sialidase [UniProt: C3W5S7]Exo-alpha-sialidase [UniProt: C3W5S7]N1 [UniProt: C3W5S7]Neuraminidase [UniProt: C3W5S7]NA [UniProt: C3W5S7]

Neuraminidase inhibitors block the active site of the enzyme, preventing the cleavage of terminal sialic acid residues from host cell receptors and viral glycoproteins. This action prevents the release of newly formed virions from infected cells, thereby limiting the spread of the virus within the respiratory tract [PubMed: 22443928, PubChem: CID 65028].