Neuraminidase (Influenza A virus H5N1 Indonesia strain) (NA)

Neuraminidase (NA) is a major surface glycoprotein and essential enzyme of the H5N1 influenza virus, specifically the highly pathogenic Indonesia strain (e.g., A/Indonesia/5/2005) [1, 9]. It functions as a sialidase, cleaving terminal sialic acid residues from host cell receptors and viral glycoproteins to facilitate the release of progeny virions from infected cells and prevent viral aggregation [5, 14, 15]. This enzymatic activity is crucial for the spread of the virus throughout the respiratory tract and is the primary target for antiviral drugs known as neuraminidase inhibitors, such as oseltamivir, zanamivir, peramivir, and laninamivir [7, 18]. In Indonesian H5N1 clades, specific mutations like N294S and H274Y have been identified that significantly reduce susceptibility to these treatments, posing a major challenge for clinical management and pandemic preparedness [2, 6, 13]. Understanding the structural and functional nuances of the H5N1 Indonesia neuraminidase is vital for the design of more resilient therapeutic agents and for monitoring the zoonotic threat posed by this virus [14, 18]. The protein exists as a tetramer on the viral envelope and its active site is highly conserved, though group-1 neuraminidases like N1 possess a unique 150-cavity that may be exploited for drug design [17]. Surveillance of this target is a global priority due to the high mortality rate associated with H5N1 infections in humans [19, 20].

Other names

SialidaseExo-alpha-sialidaseN1 neuraminidaseNA

Neuraminidase inhibitor