Abstract
1 Laboratoire de Génétique des Virus, UPR 2431-CNRS, Avenue de la Terrasse, 91198 Gif sur Yvette cedex
2 Département de Biologie, Ecole Normale Supérieure, 46 rue d'Ulm, 75230 Paris cedex 05, France
and3 Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie, Hamburg, Germany
The hepatitis B virus (HBV) e antigen (HBeAg) is a 15 kDa soluble antigen derived from a precursor protein (precore protein) by two processing events, cleavage of the N-terminal signal peptide and cleavage of the C-terminal 34 amino acids. So far, the role of the C-terminal sequences in secretion has not been analysed in full. In this study deletion of the last 60 amino acids was found to abrogate HBeAg secretion whereas deletions of the last 10, 25 or 39 amino acids decreased its secretion rate. These data demonstrate that C-terminal precore protein sequences are crucial for HBe secretion and determine its secretion rate.
* Author for correspondence. Fax +33 1 69 82 43 08. e-mail ROSSIGNOL_JM@CIT12.FR