Effect of amino acid site modification on stability of foot-and-mouth disease virus-like particles / 生物工程学报
Chinese Journal of Biotechnology
; (12): 2435-2442, 2021.
Article
em Zh
| WPRIM
| ID: wpr-887809
Biblioteca responsável:
WPRO
ABSTRACT
The stability of virus-like particles (VLPs) is currently the main factor affecting the quality of foot-and-mouth disease VLPs vaccines. In order to further improve the quality of the VLPs vaccine of foot-and-mouth disease (FMD), three amino acid modification sites were designed and screened through kinetic analysis software, based on the three-dimensional structure of FMDV. The three mutant recombinant plasmids were successfully prepared by the point mutation kit, transformed into Escherichia coli strain BL21 and expressed in vitro. After purification by Ni ion chromatography column, SDS-PAGE proved that the three amino acid mutations did not affect the expression of the target protein. The results of the stability study of three FMD mutant VLPs obtained by in vitro assembly show that the introduction of internal hydrophobic side chain amino acids made the morphology of VLPs more uniform (N4017W), and their stability was significantly improved compared to the other two VLPs. The internal hydrophobic force of the capsid contributes to the formation of VLPs and helps to maintain the stability of the capsid, providing new experimental ideas for improving the quality of VLPs vaccines, and helping to promote the development of VLPs vaccines.
Palavras-chave
Texto completo:
1
Base de dados:
WPRIM
Assunto principal:
Vacinas Virais
/
Cinética
/
Vírus da Febre Aftosa
/
Proteínas do Capsídeo
/
Vacinas de Partículas Semelhantes a Vírus
/
Febre Aftosa
/
Aminoácidos
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2021
Tipo de documento:
Article