1Centre for Computational Biology and Bioinformatics, School of Information Technology, Jawaharlal Nehru University, New Delhi-110 067, India.
2Department of Biochemistry, School of Molecular and Microbial Sciences, University of Queensland, St. Lucia, Queensland 4072, Australia.
3Department of Microbiology and Parasitology, School of Molecular and Microbial Sciences, University of Queensland, St. Lucia, Queensland 4072, Australia.
Abstracts of the papers presented at the XVIII National Conference of Indian Virological Society at Post Graduate Institute of Medical Education and Research, Chandigarh, India, December 11–13, 2008.
In enveloped viruses, like flaviviruses, that enter cells via receptor-mediated endocytosis, fusion is initiated in low-pH of the endosomal vesicle. Upon appropriate triggering, the fusion protein interacts with the target membrane through a hydrophobic fusion peptide and undergoes a conformational change that drives the membrane fusion reaction1. The initial maturation of the virion and the later triggering of conformational changes that lead to membrane fusion require a pH range that suggests that the protonation of one or more histidine residues is critical in both processes2. In the current study we have studied the fusion trigger by performing molecular dynamics simulation of the envelope protein after insilico mutation of three histidines (His 244, His 261 and His 317) for 20 nanoseconds. Significant changes were seen in the salt-bridge behavior, Root mean square deviation and fluctuation and structural differences between the initial and end structures.
