CHARACTERIZATION AND BIOSYNTHESIS OF THE WOODCHUCK HEPATITIS-VIRUS E-ANTIGEN

被引:13
作者
CARLIER, D
OLIVIER, JJ
ROSSIGNOL, JM
机构
[1] CNRS,UPR 272,F-94802 VILLEJUIF,FRANCE
[2] CNRS,GENET VIRUS LAB,UPR 2431,F-91198 GIF SUR YVETTE,FRANCE
关键词
D O I
10.1099/0022-1317-75-1-171
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:171 / 175
页数:5
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