Expression in Escherichia coli and purification of biologically active L proteinase of foot-and-mouth disease virus.
Virus Res
; 35(3): 263-75, 1995 Mar.
Article
em En
| MEDLINE
| ID: mdl-7785315
ABSTRACT
The foot-and-mouth disease virus (FMDV) Lb gene was cloned into bacterial expression vectors under the control of a T7 RNA polymerase promoter. The Lb protein was expressed in both an in vitro transcription-translation system and in Escherichia coli. In vitro expression of a construct containing the Lb gene fused to a portion of the VP4 and 3D genes demonstrated cis cleavage activity that could be blocked by the thiol protease inhibitor E-64. Lb expressed in E. coli was purified from the soluble fraction by metal chelation chromatography. Purified Lb had trans cleavage activity at the L/P1 junction and cleaved the p220 component of the cap-binding protein complex.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Proteínas Virais
/
Aphthovirus
Limite:
Humans
Idioma:
En
Ano de publicação:
1995
Tipo de documento:
Article