Autoproteolytic cleavage of recombinant 3C proteinase of hepatitis a virus
| Autor: | Dirk Jürgensen, Rainer Deutzmann, Verena Gauss-Müller |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Antigenicity
Proteolysis Molecular Sequence Data Restriction Mapping lac operon Biology law.invention Viral Proteins law Virology Complementary DNA medicine Amino Acid Sequence Hepatovirus Cloning Molecular Peptide sequence chemistry.chemical_classification medicine.diagnostic_test 3C Viral Proteases Proteins Molecular biology Fusion protein Recombinant Proteins Amino acid Cysteine Endopeptidases Biochemistry chemistry Recombinant DNA Peptides Protein Processing Post-Translational |
| Zdroj: | Virology. 182:861-864 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/0042-6822(91)90630-t |
| Popis: | A hepatitis A virus cDNA fragment coding for the viral proteinase 3C was expressed as a chimeric protein fused in-frame to the C-terminus of β-galactosidase. Following induction of the lac Z promoter, polypeptides of 150, 28, 26, and 16 kDa, all of which carry 3C antigenicity, were produced. The 28- and 26-kDa proteins were identified as autoproteolytic products of the fusion protein by determination of their N-terminal amino acid sequence. The 16-kDa protein arises from internal initiation. Following substitution of the 37 amino acids at the C-terminus of 3C, the autolytic activity was no longer observed. The recombinant proteinase did not show trans -activity when recombinant proteins of the P1 or P2 region were used as substrates. Antisera directed against recombinant 3C could not detect 3C or its precursors in HAV-infected cells. |
| Databáze: | OpenAIRE |
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