Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and E1 proteins of hepatitis C virus strain J1
| Autor: | John McLauchlan, Marion McElwee, R. Graham Hope |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Signal peptide
chemistry.chemical_classification Signal peptidase Viral Core Proteins Molecular Sequence Data Mutant Hepacivirus Protein Sorting Signals Biology Cleavage (embryo) Virology Cell Line Amino acid NS2-3 protease Viral Envelope Proteins chemistry Biochemistry Animals Aspartic Acid Endopeptidases Humans Amino Acid Sequence Glycoprotein Signal peptide peptidase |
| Zdroj: | Journal of General Virology. 87:623-627 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/vir.0.81371-0 |
| Popis: | Maturation of hepatitis C virus (HCV) core protein requires cleavage by signal peptidase (SP) and signal peptide peptidase (SPP) at a signal peptide between core and the E1 glycoprotein. For HCV strain Glasgow, amino acids Ala180, Ser183 and Cys184 within the signal peptide have previously been shown to be essential for efficient SPP cleavage. By contrast, these residues apparently did not contribute to core maturation in HCV strain J1. In the present study, the source of this discrepancy has been analysed and it is concluded that interpretation of the strain J1 data was incorrect, due to the inability to separate wild-type and mutant forms of core on gels by using standard buffer systems. |
| Databáze: | OpenAIRE |
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