Electrostatic energy calculation on the pH-induced conformational change of influenza virus hemagglutinin

¹ Seoul National University
² Seoul national University

^* To whom correspondence should be addressed. E-mail: whjpoly{at}plaza.snu.ac.kr.

Submitted on July 12, 2005
Revised on August 23, 2005
Accepted on 6 March 2006

	Abstract

The pH-induced conformational change of influenza virus hemagglutinin (HA) has been investigated by calculating the change of electrostatic energy of the fragment of HA2 upon pH change. The average charge and electrostatic free energy are calculated as a function of pH for the fusion peptide (residues 1-20 of HA2) and the polypeptide of residues 54-77 of HA2 by using the finite difference Poisson-Boltzmann method. It is found that as pH decreases from 8 to 5, the electrostatic free energy of the fusogenic state is lowered by approximately 2 kcal/mol and the fusogenic state is less ionized compared to that of the native state for both polypeptides. For the fusion peptide at the fusogenic state, most of ionizable residues are neutral at acidic pH except Glu11. For the polypeptide of residues 54-77 at the fusogenic state, most of residues except Glu74 and His64 are fully charged between pH 5 and pH 8.

Key Words: Poisson-Boltzmann calculation, conformational change, electrostatic free energy, hemagglutinin, influenza virus, pH-induced

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