Abstract
The contribution of protein folding and protein-nucleic acid interactions to virus assembly has been measured in several bacterial, plant and animal viruses, using hydrostatic pressure as thermodynamic variable. By comparing the pressure stability among native wild-type viruses, single-amino acid mutants or empty particles, we have gained new insights about virus assembly and disassembly. We find that the isolated capsid proteins and the assembly intermediates are not fully folded, and that association of 60 or more subunits into an icosahedral particle is coupled to progressive folding of the coat protein and also to changes in interactions with the nucleic acid. Using pressure, we have detected the presence of a ribonucleoprotein intermediate, where the coat protein is partially unfolded but bound to RNA. These intermediates are potential targets for antiviral compounds. Pressure studies on viruses have direct biotechnological applications. The ability of pressure to inactivate viruses has been evaluated with a view toward the applications of vaccine development and virus sterilization. We demonstrate that pressure causes virus inactivation while preserving the immunogenic properties. There are substantial evidence that a high pressure cycle traps a virus in the “fusion intermediate state”, not infectious but highly immunogenic. Pressure inactivation has been successful with viruses that cause disease in animals, especially foot-and-mouth disease virus (FMDV) and bovine rotavirus and humans, such as rhinoviruses, adenoviruses, alphaviruses, influenza and retroviruses.
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Oliveira, A.C. et al. (1999). Hydrostatic Pressure as a Tool to Study Virus Assembly: Pressure-Inactivation of Viruses by Formation of Fusion Intermediate States. In: Winter, R., Jonas, J. (eds) High Pressure Molecular Science. NATO Science Series, vol 358. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4669-2_25
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DOI: https://doi.org/10.1007/978-94-011-4669-2_25
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