Influenza A virus surface glycoprotein (HA/NA)

Influenza A virus surface glycoproteins primarily include hemagglutinin (HA) and neuraminidase (NA), which are essential for the viral life cycle (UniProt P03437, P03468). Hemagglutinin mediates the binding of the virus to sialic acid receptors on host cells and facilitates the subsequent fusion of the viral envelope with the host cell membrane for genome release (CDC, 2023). Neuraminidase functions as an enzyme that cleaves sialic acid residues from host cell receptors and viral glycoproteins, enabling the release of progeny virions from infected cells and preventing viral aggregation (StatPearls, 2023). These proteins are the primary targets for the host immune response and are the focus of most influenza vaccines and antiviral therapies (PubMed: 30135114). While HA is targeted by fusion inhibitors like umifenovir, NA is the target of widely used neuraminidase inhibitors such as oseltamivir and zanamivir (PubChem). Due to their high rate of mutation (antigenic drift) and occasional reassortment (antigenic shift), these glycoproteins are subject to constant surveillance for vaccine strain selection and drug resistance monitoring (NIH, 2023).

Other names

HemagglutininNeuraminidaseHANASialidaseHA0Surface glycoprotein

Neuraminidase inhibition to prevent viral progeny release; Hemagglutinin inhibition to block viral entry and membrane fusion.