On the effect of thermodynamic equilibrium on the assembly efficiency of complex multi-layered virus-like particles (VLP): the case of rotavirus VLP.

PLoS Computational Biology
António RoldãoR Oliveira

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...Continue Reading

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Citations

Nov 19, 2013·PLoS Computational Biology·Guido PollesCristian Micheletti
Feb 19, 2013·Expert Review of Vaccines·Fabiana FernandesPaula M Alves
Dec 19, 2013·Biotechnology and Bioengineering·Linda H L LuaAnton P J Middelberg
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Jan 1, 2019·Biotechnology and Bioengineering·Hayley K Charlton HumeLinda H L Lua
Jul 6, 2019·Frontiers in Plant Science·Ahmad IbrahimRichard Kormelink

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Methods Mentioned

BETA
light scattering
X-ray
protein

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