Electrostatic screening, acidic pH and macromolecular crowding increase the self-assembly efficiency of the minute virus of mice capsid in vitro

The hollow protein capsids from a number of different viruses are being considered for multiple biomedical or nanotechnological applications. In order to improve the applied potential of a given viral capsid as a nanocarrier or nanocontainer, specific conditions must be found for achieving its faith...

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Detalles Bibliográficos
Autores: Fuertes Villadangos, Miguel Ángel, López Mateos, Diego, Valiente Martínez-Sicluna, Luis, Rodríguez-Huete, Alicia, Valbuena Jiménez, Alejandro, García Mateu, Mauricio
Tipo de recurso: artículo
Fecha de publicación:2023
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/707938
Acceso en línea:http://hdl.handle.net/10486/707938
https://dx.doi.org/10.3390/v15051054
Access Level:acceso abierto
Palabra clave:Mice
Static Electricity
Hydrogen-Ion Concentration
Virus Assembly
Biología y Biomedicina / Biología
Descripción
Sumario:The hollow protein capsids from a number of different viruses are being considered for multiple biomedical or nanotechnological applications. In order to improve the applied potential of a given viral capsid as a nanocarrier or nanocontainer, specific conditions must be found for achieving its faithful and efficient assembly in vitro. The small size, adequate physical properties and specialized biological functions of the capsids of parvoviruses such as the minute virus of mice (MVM) make them excellent choices as nanocarriers and nanocontainers. In this study we analyzed the effects of protein concentration, macromolecular crowding, temperature, pH, ionic strength, or a combination of some of those variables on the fidelity and efficiency of self-assembly of the MVM capsid in vitro. The results revealed that the in vitro reassembly of the MVM capsid is an efficient and faithful process. Under some conditions, up to ~40% of the starting virus capsids were reassembled in vitro as free, non aggregated, correctly assembled particles. These results open up the possibility of encapsidating different compounds in VP2-only capsids of MVM during its reassembly in vitro, and encourage the use of virus-like particles of MVM as nanocontainers