Influenza A virus neuraminidase (H1N1) (NA)

Influenza A virus neuraminidase (H1N1) is a critical surface glycoprotein and enzyme essential for the life cycle of the H1N1 subtype of the influenza A virus [1.3.1, 1.4.2]. It functions as a sialidase, catalyzing the cleavage of terminal sialic acid residues from host cell receptors and viral glycoproteins [1.3.1, 1.4.1]. This enzymatic activity is vital for the release of newly formed progeny virions from infected cells, preventing their aggregation and allowing the virus to spread to uninfected cells [1.1.1, 1.2.1]. Additionally, neuraminidase facilitates the movement of the virus through the respiratory mucus by degrading sialic acid-containing mucins [1.2.1, 1.4.2]. As a primary therapeutic target, its activity is inhibited by a class of drugs known as neuraminidase inhibitors, such as oseltamivir and zanamivir, which effectively limit the spread of the infection [1.1.2, 1.2.2]. These drugs mimic the sialic acid transition state and bind to the active site of the enzyme, blocking its ability to cleave sialic acids [1.1.1, 1.1.4]. However, the emergence of drug-resistant strains, notably those carrying the H275Y mutation, remains a significant challenge in the clinical management of influenza [1.1.2, 1.2.4]. Understanding the structural and functional nuances of this target is essential for developing next-generation antivirals and vaccines [1.4.2, 1.4.5].

Other names

SialidaseExo-alpha-sialidaseAcetylneuraminyl hydrolaseN1 neuraminidaseNeuraminidase

Neuraminidase inhibition