Human infection with H7 influenza subtypes usually resulted in mild disease with a rare mortalities, however, human infection with the avian low pathogenic H7N9 influenza virus resulted in about 38.6 % human fatality. Due to the new cross-species barrier of this virus subtype, there is an urgent need to better understand the susceptibility to commercially available antivirals and their relation to the structural changes of the viral neuraminidase. Neuraminidases derived from 2013 H7N9, H5N1 and H1N1 were subjected to a structural analysis of their catalytic and framework binding sites. The modeling structure of selected neuraminidases from H7N9 and influenza A subtypes were solved and the docking studies with oseltamivir, zanamivir, laninamivir and peramivir were conducted. The active site residues that are responsible for both binding and cleavage of the terminally linked sialic acid receptors were found conserved. Docking studies with oseltamivir, zanamivir, laninamivir and peramivir revealed that the laninamivir and peramivir showed superior energy binding activities in comparison to the commonly used oseltamivir and zanamivir. The results presented in the current study provide data that are useful for the future treatment of different influenza A subtypes including the recently emerged H7N9.
Keywords: H7N9; Influenza A virus; Molecular docking; Neuraminidase inhibitors.