Influenza A virus N1 neuraminidase (NA)

Influenza A virus N1 neuraminidase (NA) is a major surface glycoprotein and essential enzyme of the influenza virus, particularly the H1N1 and H5N1 subtypes (1.2.1, 1.5.4). Its primary biological function is to act as a sialidase, cleaving terminal sialic acid residues from host cell receptors and viral glycoproteins (1.2.4, 1.5.1). This enzymatic activity is critical for the release of progeny virions from infected cells, preventing viral self-aggregation and facilitating movement through the respiratory mucus (1.2.3, 1.2.5). The NA protein is a primary target for antiviral drugs, specifically neuraminidase inhibitors like oseltamivir and zanamivir, which bind to the highly conserved catalytic site to block viral egress (1.3.2, 1.3.4). Beyond its catalytic function, the surrounding epitopes on the NA head domain are key targets for the host immune response and the development of broadly neutralizing antibodies and universal vaccines (1.1.2, 1.1.4). Therapeutic challenges include the emergence of drug-resistant mutations, such as the H274Y substitution, and the continuous antigenic drift of the protein's surface epitopes (1.3.2, 1.4.4).

Other names

SialidaseExo-alpha-sialidaseN1 neuraminidaseReceptor-destroying enzymeN-acylneuraminate glycohydrolase

Neuraminidase inhibition