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

J. Biol. Chem., Vol. 278, Issue 2, 891-895, January 10, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/2/891    most recent M207634200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Messageot, F. Articles by Rossignol, J.-M. Search for Related Content PubMed PubMed Citation Articles by Messageot, F. Articles by Rossignol, J.-M. Social Bookmarking                      What's this?

Proteolytic Processing of the Hepatitis B Virus e Antigen Precursor
CLEAVAGE AT TWO FURIN CONSENSUS SEQUENCES^*

Fabienne Messageot, Samia Salhi^§, Patricia Eon, and Jean-Michel Rossignol^¶

From the Laboratoire de Génétique des Virus, Gif sur Yvette, 91198 France, and Laboratoire de Génétique et Biologie Cellulaire, Université de Versailles St. Quentin en Yvelines, 78035 France

The Hepatitis B virus P22 protein is a nonstructural protein that is the precursor of the 17-kDa secreted e antigen (HBeAg). The mature HBeAg is obtained after the removal of the C-terminal region of P22, a process which involves a proprotein convertase. Our studies show first that the protease could cleave P22 at the C-terminal side of Arg¹⁶⁷ or Arg¹⁵⁴ and second, that the maturation process can be either done in one step or in two steps with the generation of a processing intermediate (P20). Our data also demonstrate that the removal of the P22 C terminus, which occurs mainly in the trans-Golgi network, can also be achieved after exocytosis. Keeping in mind this characteristic and the amino acid sequence of the cleavage sites, we concluded that furin is involved in the maturation of the HBeAg. In addition, we show that in our experimental system, the HBeAg is a 164-amino acid protein and not a 159-amino acid protein as previously reported.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				K. Ito, K.-H. Kim, A. S.-F. Lok, and S. Tong Characterization of Genotype-Specific Carboxyl-Terminal Cleavage Sites of Hepatitis B Virus e Antigen Precursor and Identification of Furin as the Candidate Enzyme J. Virol., April 15, 2009; 83(8): 3507 - 3517. [Abstract] [Full Text] [PDF]

				M. Duriez, J.-M. Rossignol, and D. Sitterlin The Hepatitis B Virus Precore Protein Is Retrotransported from Endoplasmic Reticulum (ER) to Cytosol through the ER-associated Degradation Pathway J. Biol. Chem., November 21, 2008; 283(47): 32352 - 32360. [Abstract] [Full Text] [PDF]

				M. Fugere, J. Appel, R. A. Houghten, I. Lindberg, and R. Day Short Polybasic Peptide Sequences Are Potent Inhibitors of PC5/6 and PC7: Use of Positional Scanning-Synthetic Peptide Combinatorial Libraries as a Tool for the Optimization of Inhibitory Sequences Mol. Pharmacol., January 1, 2007; 71(1): 323 - 332. [Abstract] [Full Text] [PDF]

				T. Kimura, N. Ohno, N. Terada, A. Rokuhara, A. Matsumoto, S. Yagi, E. Tanaka, K. Kiyosawa, S. Ohno, and N. Maki Hepatitis B Virus DNA-negative Dane Particles Lack Core Protein but Contain a 22-kDa Precore Protein without C-terminal Arginine-rich Domain J. Biol. Chem., June 10, 2005; 280(23): 21713 - 21719. [Abstract] [Full Text] [PDF]

				S. Laine, A. Thouard, J. Derancourt, M. Kress, D. Sitterlin, and J.-M. Rossignol In Vitro and In Vivo Interactions between the Hepatitis B Virus Protein P22 and the Cellular Protein gC1qR J. Virol., December 1, 2003; 77(23): 12875 - 12880. [Abstract] [Full Text] [PDF]