2P031 Mechanism of glycan receptor recognition for influenza virus Hemagglutinins: Comparative molecular dynamis studies

The heamagglutinin (HA) of influenza viruses mediate receptor binding, the initial event in virus infection. The differences in receptor-binding specificity of human and avian viruses are determined by the amino acid residues in the HA receptor-binding pocket. Asp at position 190 and 225 of H1 HAs confer binding to human-type receptors, whereas E190 and G225 confer binding to avian-type receptors. However some isolated viruses have E190 or G225, and D190E/D225G substituted virus does not prefer avian-receptor always. To clarify the detail effects of changes on binding for different HAs, molecular dynamics simulations were performed for the H1HA-glycan receptor complexes which comprise wild type and one point amino acid substituted HAs at positions 190 or 225.