Thermodynamic and Kinetic Modeling of Polymorphism in Viral Capsid Assembly
ORAL
Abstract
Polymorphism in viral capsids poses a key problem in statistical physics: understanding how identical protein subunits assemble into distinct, stable structures under identical conditions. One example is the hepatitis B virus (HBV), forming two capsid morphologies containing 90 or 120 protein dimers. Experiments show that their relative abundance depends sensitively on ionic strength. We developed a model that incorporates salt effects by modulating the intermolecular binding free energy, thereby tuning the thermodynamic stability landscape. We reproduce experimentally observed morphology ratios across salt concentrations. A complementary kinetic model captures the time-dependent evolution of the two capsid forms, linking energetics, stoichiometry, and assembly pathways to reveal general physical principles governing viral polymorphism.
*This material is based upon work supported by the National Science Foundation under Grant No. NSF DMR-2131963 and Grant No. MCB/PHY-2413062. PvdS received support from the Institute of Complex Molecular Systems of Eindhoven University of Technology during the period that the work was done.
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Presenters
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Kevin Yang
- University of California, Riverside