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J Biol Chem, Vol. 273, Issue 29, 18594-18598, July 17, 1998

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

From the Laboratoire de Génétique des Virus, Gif sur Yvette, France

The Hepatitis B virus encodes the secreted e antigen (HBe) whose function in the viral life cycle is unknown. HBe derives from a 25-kDa precursor that is directed to the secretory pathway. After cleavage of the signal sequence, the resulting 22-kDa protein (P22) is processed in a post-endoplasmic reticulum compartment to mature HBe by removal of the 34-amino acid C-terminal domain. The efficiency of HBe secretion is specifically decreased in cells grown in the presence of tunicamycin, an inhibitor of N-glycosylation. Inasmuch as HBe precursor is not N-glycosylated, our data suggest that a cellular tunicamycin-sensitive protein increases the intracellular transport through the HBe secretory pathway. The study of the secretion of HBe derived from C-terminal-truncated precursors demonstrates that the tunicamycin-sensitive secretion absolutely requires a part of the C-terminal region that is removed to form mature HBe, indicating that the cellular tunicamycin-sensitive protein increases the efficiency of the intracellular transport of P22. We have also shown that the Escherichia coli -galactosidase can be secreted when fused to the HBe precursor signal sequence and that the P22 C-terminal domain renders the secretion of this reporter protein also tunicamycin-sensitive.

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				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]