Processing of hepatitis C viral polyprotein in Escherichia coli.
Gene
; 145(2): 221-6, 1994 Aug 05.
Article
em En
| MEDLINE
| ID: mdl-8056335
ABSTRACT
Two proteinase activities, encoded by hepatitis C virus (HCV), Cpro-1 and Cpro-2. Cpro-1 and Cpro-2 appear to process the precursor polyprotein from which they originate. Mutant HCV polypeptides containing the region for these proteinases were produced in Escherichia coli as fusion proteins. The N- and C-terminal ends of the HCV polypeptides were fused with the E. coli maltose-binding protein (MBP) and E. coli dihydrofolate reductase (DHFR), respectively. The proteinase activities cleaved the fusion polypeptides by the same processing pathway used in eukaryotic protein production systems. The N-terminal amino acid (aa) sequences of the processed fusion proteins were determined. A comparison of those N-terminal sequences with the aa sequence of the HCV precursor polyprotein showed that the N-terminal and C-terminal cleavage sites of p70(NS3), one of the HCV nonstructural (NS) proteins, were the same as those identified in other processing studies cleavages were estimated to be between aa 1026 and 1027 and between aa 1657 and 1658 of the HCV precursor protein, which are known to be cleaved by Cpro-1 and Cpro-2, respectively. Cpro-1 and Cpro-2 both functioned in E. coli and possessed authentic characteristic features.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Proteínas de Transporte de Monossacarídeos
/
Processamento de Proteína Pós-Traducional
/
Proteínas não Estruturais Virais
/
Hepacivirus
/
Transportadores de Cassetes de Ligação de ATP
/
Proteínas de Escherichia coli
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Gene
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
Japão