High level soluble expression and one-step purification of IBDV VP2 protein in Escherichia coli.
Biotechnol Lett
; 38(6): 901-8, 2016 Jun.
Article
em En
| MEDLINE
| ID: mdl-27003577
ABSTRACT
OBJECTIVES:
To improve the expression of soluble IBDV VP2 protein by using different tagged vectors in Escherichia coli.RESULTS:
Fusion tags, Grifin, MBP, SUMO, thioredoxin, γ-crystallin, ArsC and PpiB, enhanced the expression and solubility of VP2 protein. The fusion proteins were purified by Ni-NTA chromatography, MBP-VP2 showed the highest purity about 90 %. After removing the MBP tag, VP2 self-assembled into virus-like particles, ~25 nm diam. Results from AGP suggested the recombinant IBDV VP2 protein identified by reference serum like IBDV.CONCLUSION:
All the seven tags enhanced the expression and solubility of IBDV VP2 protein. The recombinant protein self-assembly into virus like particles and possess antigenicity as reference IBDV.Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Recombinantes de Fusão
/
Engenharia de Proteínas
/
Proteínas Estruturais Virais
/
Escherichia coli
Limite:
Animals
Idioma:
En
Revista:
Biotechnol Lett
Ano de publicação:
2016
Tipo de documento:
Article