Study of the mechanism of protonated histidine-induced conformational changes in the Zika virus dimeric envelope protein using accelerated molecular dynamic simulations

[Display omitted] •The bilayer could lead to a curvature induced by the transmembrane region of the Zika virus envelope protein.•The low pH condition could weaken the interactions and correlations in the envelope protein.•The highly conserved residues, His249, His288, His323 and His446 play key role...

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Bibliographic Details
Published in:Journal of molecular graphics & modelling 2017-06, Vol.74, p.203-214
Main Authors: Sun, Jixue, Li, Yang, Liu, Pi, Lin, Jianping
Format: Article
Language:English
Subjects:
Accelerated dynamic simulations
Amino Acid Sequence
Conformational change
Conserved Sequence
Envelope protein
Histidine - chemistry
Hydrogen Bonding
Molecular Dynamics Simulation
Protein Conformation, alpha-Helical
Protein Domains
Protein Structure, Quaternary
Thermodynamics
Viral Envelope Proteins - chemistry
Zika virus
Zika Virus - chemistry
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Summary:[Display omitted] •The bilayer could lead to a curvature induced by the transmembrane region of the Zika virus envelope protein.•The low pH condition could weaken the interactions and correlations in the envelope protein.•The highly conserved residues, His249, His288, His323 and His446 play key roles in driving the fusion process. The Zika virus has drawn worldwide attention because of the epidemic diseases it causes. It is a flavivirus that has an icosahedral protein shell constituted by an envelope glycoprotein (E-protein) and membrane protein (M-protein) in the mature virion. The multistep process of membrane fusion to infect the host cell is pH-induced. To understand the mechanism of the conformational changes in the (E-M)2 protein homodimer embedded in the membrane, two 200-ns accelerated dynamic simulations were performed under different pH conditions. The low pH condition weakens the interactions and correlations in both E-protein monomers and in the E-M heterodimer. The highly conserved residues, His249, His288, His323 and His446, are protonated under low pH conditions and play key roles in driving the fusion process. The analysis and discussion in this study may provide some insight into the molecular mechanism of Zika virus infection.
ISSN:1093-3263
1873-4243
DOI:10.1016/j.jmgm.2017.04.009