Target intelligence / Profile preview

Influenza A H5N1 neuraminidase (NA)

Target
NA
Molecular classification
Enzyme, Glycoside hydrolase (exosialidase), Viral glycoprotein
01

Overview

Influenza A H5N1 neuraminidase is a viral surface glycoprotein enzyme (exosialidase, EC 3.2.1.18) with a tetrameric structure located on the envelope of influenza virions[2]. It catalyzes cleavage of terminal sialic acids from host cell surface glycoproteins and glycolipids, a process necessary for efficient virus release and spread during infection[2][3][4]. NA is a critical target for antiviral drugs, and its structure and substrate specificity underlie both its catalytic function and susceptibility to drug inhibition. Variations in the NA gene and protein can confer resistance to currently approved inhibitors, making it a central focus in influenza drug and vaccine development[2][3][4].

Other names
Neuraminidaseviral neuraminidaseNAInfluenza neuraminidaseExosialidase EC 3.2.1.18N1 subtype
02

Mechanism of action

Competitive inhibition of the NA active site by mimicking the sialic acid substrate, thus preventing release of viral particles from infected host cells

03

Biological functions

Catalyzes removal of terminal sialic acid residues from glycoproteins and glycolipidsFacilitates viral release/egress from host cellsPrevents viral particle aggregationModulates viral attachment and entry
04

Disease associations

Infection (essential for influenza virus infectivity and propagation)
05

Safety considerations

Emergence of drug-resistant NA mutations, compromising efficacy of neuraminidase inhibitorsPotential for allergic or hypersensitivity reactions to NA inhibitor drugsRapid viral evolution challenging vaccine and drug design
06

Interacting drugs

Oseltamivir (Tamiflu)

3 more in the full profile.

07

Biomarkers

NA activity assays can indicate viral proliferation or resistance to NA inhibitorsDetection/quantification of neuraminidase gene or protein (N1 subtype) in clinical samples

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