*************** OWARI COMPLEX SEMINAR XLIII ***************

Title : Changes of Human Receptor Binding Affinity of H1N1
Hemagglutinins: Insights from Molecular Dynamics Simulation

Speaker : Nadtanet Nunthaboot (Faculty of Science, Mahasarakham University)

Date : Fri. May. 20th, 2:00 pm (Almost half an hour)

Place : 4F Seminar Room
            Graduate School of Information Science

Abstract: The binding of the viral glycoprotein, hemagglutinin (HA),
and the human-a2,6-linked sialopentasaccharide host cell
receptor (hHAR) is a critical step in the viral replication cycle.
Dynamical and structural properties of the four different HAs of
Spanish 1918 (H1-1918), swine 1930 (H1-1930), seasonal 2005
(H1-2005) and a novel 2009 (H1-2009) H1N1 bound to the hHAR,
were investigated by means of molecular dynamics simulations.
In all systems, major interactions between HA residues and hHAR
were obtained from Y95 and the conserved residues of the 130-
loop, 190-helix and 220-loop. Compared to the three previously
recognized H1N1 strains, introductions of K145 and E227, charged
residues, increased the HA-hHAR binding efficiency of 2009 HA
H1N1. In addition, changing of G225, the non-charged residue, to
D225, a negatively charged residue, provides a larger number of
hydrogen bonding interactions. The obtained information could
help the understanding of how different HAs effectively attach
and bind with the hHAR.

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