Characterization and biosynthesis of the woodchuck hepatitis virus e antigen
| Autor: | Damien Carlier, Jean-Michel Rossignol, Olivier Jean-Jean |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Signal peptide
Glycosylation Recombinant Fusion Proteins viruses Molecular Sequence Data Biology medicine.disease_cause Virus Cell Line Antigen Virology medicine Hepatitis B Virus Woodchuck Humans Amino Acid Sequence Hepatitis B e Antigens Peptide sequence Hepatitis B virus Woodchuck hepatitis virus biochemical phenomena metabolism and nutrition biology.organism_classification Fusion protein Molecular biology digestive system diseases Hepadnaviridae Protein Processing Post-Translational |
| Zdroj: | Journal of General Virology. 75:171-175 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/0022-1317-75-1-171 |
| Popis: | The biosynthesis of the secretory core gene product of the woodchuck hepatitis virus (WHV) was studied in human cells. We have shown that the WHV e antigen was a N-glycosylated (most likely a diglycosylated) protein, with an apparent M(r) of 24K. To demonstrate that the WHV precore protein was correctly processed in human cells, we engineered chimeric proteins in which signal peptides or arginine-rich domains of WHV and hepatitis B virus (HBV) precore proteins were exchanged. Our results showed that both the signal peptide and the arginine-rich region of WHV precore protein were cleaved off during the secretion pathway, as previously reported for precore protein of human HBV and duck HBV. These observations demonstrate that the maturation process of the e antigen is conserved in hepadnaviruses. In addition, on the basis of inhibition experiments, we suggest that the cleavage of the carboxy terminus of the WHV precore protein occurred in a post-endoplasmic reticulum compartment, most likely beyond the medial Golgi, and that this cleavage was catalysed by an aspartyl protease. |
| Databáze: | OpenAIRE |
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