ArticlePLoS computational biology2012
On the effect of thermodynamic equilibrium on the assembly efficiency of complex multi-layered virus-like particles (VLP): the case of rotavirus VLP.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Rapid, Scalable, and Cost-Effective Manufacturing of Uniform Non-Enveloped, Tag-Free Virus-Like Particles.Current protocols · 2026Article
- Overcoming dengue vaccine challenges through next-generation virus-like particle immunization strategies.Frontiers in cellular and infection microbiology · 2025Review
- Tailored Viral-like Particles as Drivers of Medical Breakthroughs.International journal of molecular sciences · 2024Review
- Advances in virus-like particle-based SARS-CoV-2 vaccines.Frontiers in cellular and infection microbiology · 2024Review
- Platforms, advances, and technical challenges in virus-like particles-based vaccines.Frontiers in immunology · 2023Review
- Size-selective downstream processing of virus particles and non-enveloped virus-like particles.Frontiers in bioengineering and biotechnology · 2023Review
- Complete and cooperative in vitro assembly of computationally designed self-assembling protein nanomaterials.Nature communications · 2021Article
- Synthetic biology for bioengineering virus-like particle vaccines.Biotechnology and bioengineering · 2019Review
- Plant Viruses in Plant Molecular Pharming: Toward the Use of Enveloped Viruses.Frontiers in plant science · 2019Review
- Exploiting virus-like particles as innovative vaccines against emerging viral infections.Journal of microbiology (Seoul, Korea) · 2017Review
- Allosteric Control of Icosahedral Capsid Assembly.The journal of physical chemistry. B · 2016Article
- Virus-like particles: the future of microbial factories and cell-free systems as platforms for vaccine development.Current opinion in biotechnology · 2013Review
- Mechanical and assembly units of viral capsids identified via quasi-rigid domain decomposition.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have reported the production of malformed virus-like-particles (VLP) in recombinant host systems. Here we computationally investigate the case of a large triple-layered rotavirus VLP (RLP). In vitro assembly, disassembly and reassembly data provides strong evidence of microscopic reversibility of RLP assembly. Light scattering experimental data also evidences a slow and reversible assembly untypical of kinetic traps, thus further strengthening the fidelity of a thermodynamically controlled assembly. In silico analysis further reveals that under favourable conditions particles distribution is dominated by structural subunits and completely built icosahedra, while other intermediates are present only at residual concentrations. Except for harshly unfavourable conditions, assembly yield is maximised when proteins are provided in the same VLP protein mass composition. The assembly yield decreases abruptly due to thermodynamic equilibrium when the VLP protein mass composition is not obeyed. The latter effect is more pronounced the higher the Gibbs free energy of subunit association is and the more complex the particle is. Overall this study shows that the correct formation of complex multi-layered VLPs is restricted to a narrow range of association energies and protein concentrations, thus the choice of the host system is critical for successful assembly. Likewise, the dynamic control of intracellular protein expression rates becomes very important to minimize wasted proteins.
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