A molecular thermodynamic model for the stability of hepatitis B capsids

Self-assembly of capsid proteins and genome encapsidation are two critical steps in the life cycle of most plant and animal viruses. A theoretical description of such processes from a physiochemical perspective may help better understand viral replication and morphogenesis thus provide fresh insight...

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Bibliographic Details
Published in:The Journal of chemical physics 2014-06, Vol.140 (23), p.235101-235101
Main Authors: Kim, Jehoon, Wu, Jianzhong
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
ANIMALS
Capsid Proteins - chemistry
Dimorphism
ENTROPY
FORECASTING
FORMATION FREE ENERGY
HEPATITIS
Hepatitis B
Hepatitis B - genetics
Hepatitis B - virology
Hepatitis B virus - chemistry
Hepatitis B virus - genetics
Hydrophobic and Hydrophilic Interactions
IN VITRO
IN VIVO
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
INTERACTIONS
LIFE CYCLE
Life cycle engineering
Models, Theoretical
Molecular Dynamics Simulation
PARTICLES
Physics
Physiochemistry
Predictions
PROTEINS
RNA - chemistry
Self-assembly
STABILITY
THERMODYNAMIC MODEL
Thermodynamic models
Thermodynamics
Virus Assembly
VIRUSES
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Summary:Self-assembly of capsid proteins and genome encapsidation are two critical steps in the life cycle of most plant and animal viruses. A theoretical description of such processes from a physiochemical perspective may help better understand viral replication and morphogenesis thus provide fresh insights into the experimental studies of antiviral strategies. In this work, we propose a molecular thermodynamic model for predicting the stability of Hepatitis B virus (HBV) capsids either with or without loading nucleic materials. With the key components represented by coarse-grained thermodynamic models, the theoretical predictions are in excellent agreement with experimental data for the formation free energies of empty T4 capsids over a broad range of temperature and ion concentrations. The theoretical model predicts T3/T4 dimorphism also in good agreement with the capsid formation at in vivo and in vitro conditions. In addition, we have studied the stability of the viral particles in response to physiological cellular conditions with the explicit consideration of the hydrophobic association of capsid subunits, electrostatic interactions, molecular excluded volume effects, entropy of mixing, and conformational changes of the biomolecular species. The course-grained model captures the essential features of the HBV nucleocapsid stability revealed by recent experiments.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.4882068