Thermodynamic stability and kinetic control of capsid morphologies in hepatitis B virus
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arXiv
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| Auteurs principaux: | , , , , |
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| Format: | Preprint |
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2026
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| _version_ | 1866908783113928704 |
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| author | Yang, Kevin Gonzalez, Juana Martin Ramezani, Alireza van der Schoot, Paul Zandi, Roya |
| author_facet | Yang, Kevin Gonzalez, Juana Martin Ramezani, Alireza van der Schoot, Paul Zandi, Roya |
| contents | Polymorphism has been observed in viral capsid assembly, demonstrating the ability of identical protein dimers to adopt multiple geometries under the same solution conditions. A well-studied example is the hepatitis B virus (HBV), which forms two stable capsid morphologies both in vivo and in vitro. These capsids differ in diameter, containing either 90 or 120 protein dimers. Experiments have shown that their relative prevalence depends on the ionic conditions of the solution during assembly. We developed a model that incorporates salt effects by altering the intermolecular binding free energy between capsid proteins, thereby shifting the relative thermodynamic stability of the two morphologies. This model reproduces experimental results on the prevalence ratios of the large and small HBV capsids. We also constructed a kinetic model that captures the time-dependent ratio of the two morphologies under subcritical capsid concentrations, consistent with experimental data. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2601_05438 |
| institution | arXiv |
| publishDate | 2026 |
| record_format | arxiv |
| spellingShingle | Thermodynamic stability and kinetic control of capsid morphologies in hepatitis B virus Yang, Kevin Gonzalez, Juana Martin Ramezani, Alireza van der Schoot, Paul Zandi, Roya Biological Physics Polymorphism has been observed in viral capsid assembly, demonstrating the ability of identical protein dimers to adopt multiple geometries under the same solution conditions. A well-studied example is the hepatitis B virus (HBV), which forms two stable capsid morphologies both in vivo and in vitro. These capsids differ in diameter, containing either 90 or 120 protein dimers. Experiments have shown that their relative prevalence depends on the ionic conditions of the solution during assembly. We developed a model that incorporates salt effects by altering the intermolecular binding free energy between capsid proteins, thereby shifting the relative thermodynamic stability of the two morphologies. This model reproduces experimental results on the prevalence ratios of the large and small HBV capsids. We also constructed a kinetic model that captures the time-dependent ratio of the two morphologies under subcritical capsid concentrations, consistent with experimental data. |
| title | Thermodynamic stability and kinetic control of capsid morphologies in hepatitis B virus |
| topic | Biological Physics |
| url | https://arxiv.org/abs/2601.05438 |