Neuraminidase (NA) from Influenza A virus (H5N1) (NA)

Neuraminidase (NA) is a major surface glycoprotein of the Influenza A virus, specifically the H5N1 subtype, which is characterized by its high pathogenicity and potential for zoonotic transmission [UniProt: P0C6Y6]. The protein exists as a tetramer and functions as a sialidase, catalyzing the cleavage of terminal sialic acid residues from glycoproteins and glycolipids on the host cell surface and viral progeny [PubMed: 10646601]. This enzymatic activity is essential for the release of newly formed virions from the host cell, preventing their aggregation and facilitating their spread through the respiratory mucus [NCBI: NBK11449]. In the context of Virus-like Particles (VLPs), NA is a critical immunogen used to elicit protective antibodies that can neutralize the virus or inhibit its spread [PubMed: 25681234]. Pharmacologically, NA is the primary target for neuraminidase inhibitors such as oseltamivir and zanamivir, which bind to the active site and prevent viral egress, thereby limiting the severity and duration of the infection [StatPearls: NBK539909]. Resistance to these drugs can occur through specific mutations in the NA gene, such as the H275Y substitution, which poses a significant challenge to clinical management [PubMed: 21666151]. Monitoring NA activity and its inhibition remains a cornerstone of influenza surveillance and therapeutic efficacy assessment [WHO: Influenza].

Other names

SialidaseExo-alpha-sialidaseN1 neuraminidaseInfluenza A virus H5N1 neuraminidaseNA

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, thereby trapping new virions at the cell surface and halting viral spread [StatPearls: NBK539909].