HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Carlier, D. Articles by Rossignol, J.-M. Search for Related Content PubMed PubMed Citation Articles by Carlier, D. Articles by Rossignol, J.-M. Agricola Articles by Carlier, D. Articles by Rossignol, J.-M.

Characterization and biosynthesis of the woodchuck hepatitis virus e antigen

Olivier Jean-Jean

¹ UPR 272-CNRS, 7 rue Guy Môquet, 94802 Villejuif Cedex
and² Laboratoire de Génétique des Virus, UPR 2431-CNRS, Avenue de la Terrasse, 91198 Gif sur Yvette, France

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.

Present address: Départment de Biologie, Ecole Normale Supérieure, 46 rue d'Ulm, 75230 Paris Cedex 05, France.

Received 11 June 1993; accepted 2 August 1993.

This article has been cited by other articles:

				F. Messageot, S. Salhi, P. Eon, and J.-M. Rossignol Proteolytic Processing of the Hepatitis B Virus e Antigen Precursor. CLEAVAGE AT TWO FURIN CONSENSUS SEQUENCES J. Biol. Chem., January 3, 2003; 278(2): 891 - 895. [Abstract] [Full Text] [PDF]

				F. Messageot, D. Carlier, and J.-M. Rossignol The C Terminus of the Hepatitis B Virus e Antigen Precursor Is Required for a Tunicamycin-sensitive Step That Promotes Efficient Secretion of the Antigen J. Biol. Chem., July 17, 1998; 273(29): 18594 - 18598. [Abstract] [Full Text] [PDF]