Neuraminidase

[1] The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus.

[2] There are two major classes of neuraminidase that cleave exo or endo poly-sialic acids: Sialidases, also called neuraminidases, catalyze the hydrolysis of terminal sialic acid residues from the newly formed virions and from the host cell receptors.

[5] Sialidase activities include assistance in the mobility of virus particles through the respiratory tract mucus and in the elution of virion progeny from the infected cell.

It has a head consisting of four co-planar and roughly spherical subunits, and a hydrophobic region that is embedded within the interior of the virus' membrane.

It comprises a single polypeptide chain that is oriented in the opposite direction to the hemagglutinin antigen.

[10] Recent emergence of oseltamivir and zanamivir resistant human influenza A(H1N1) H274Y has emphasized the need for suitable expression systems to obtain large quantities of highly pure and stable, recombinant neuraminidase through two separate artificial tetramerization domains that facilitate the formation of catalytically active neuraminidase homotetramers from yeast and Staphylothermus marinus, which allow for secretion of FLAG-tagged proteins and further purification.

Because of the relative deep active site in which low-molecular-weight inhibitors can make multiple favorable interactions and approachable methods of designing transition-state analogues in the hydrolysis of sialosides, the sialidase becomes more attractive anti-influenza drug target than the haemagglutinin.