INHIBITING H5N1 HAEMAGGLUTININ WITH SMALL MOLECULE LIGANDS

Mutations in the avian influenza virus can create new pathogenic strains, which can cause futurepandemics. Targeting the surface haemagglutinin can inhibit viral fusion and consequent entry. The effects of 27single and double point mutations on the properties of the H5 haemagglutinin were studied. These mutations werethen introduced individually in the PDB file of the H5, to generate mutants. 13 herbal and non-herbal lead inhibitorsof H5 were screened and docked with the wild type and mutant haemagglutinins to obtain a comparative dockingprofile. The nature of the interactions of the inhibitors were analysed, and the binding residues determined. Thelatter further revealed that certain mutations in HA might be affecting inhibitor binding