Human neuraminidase (hNEU) shares many similar features with vNEU. The human genome has four different neuraminidase enzymes (NEU1, NEU2, NEU3, NEU4) and only one of them (NEU2) is not membrane-associated or in a membrane-complex and has been studied with X-ray crystallography. The three arginine residues that bind the C1 acid-group with salt bridges in vNEU are also present in hNEU. Active site topology and interactions with the substrate are very similar with the exception of the glycerol side chain which offers some strategic options in designing inhibitors targeting either vNEU or hNEU. In hNEU the glycerol hydroxyl-groups are bound via several tyrosine residues but in vNEU the main interaction is with a glutamic acid residue. These overall similarities have called for concerns over potential side effects from drugs targeting vNEU. Nevertheless, most of the well studied vNEU inhibitors have shown very little affinity for hNEU except for the influenza drug Zanamivir which is an effective inhibitor for hNEU2.