A CARBOXY-TERMINAL PORTION OF THE PRES1 DOMAIN OF HEPATITIS-B VIRUS (HBV) OCCASIONED RETENTION IN ENDOPLASMIC-RETICULUM OF HBV ENVELOPE PROTEINS EXPRESSED BY RECOMBINANT VACCINIA VIRUSES

被引：8

作者：

NEMECKOVA, S ^{[1
]}

KUNKE, D ^{[1
]}

PRESS, M ^{[1
]}

NEMECEK, V ^{[1
]}

KUTINOVA, L ^{[1
]}

机构：

[1] NATL INST PUBL HLTH,PRAGUE,CZECH REPUBLIC

来源：

VIROLOGY | 1994年 / 202卷 / 02期

关键词：

D O I：

10.1006/viro.1994.1431

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The large envelope glycoprotein (L protein) of Hepatitis B virus (HBV) contains the preS1 domain, which is responsible for retention of the protein in the endoplasmic reticulum. To identify sequences of the preS1 domain involved in this phenomenon we constructed vaccinia virus-HBV recombinants containing the gene for L protein in which the preS1 coding sequence had been partially deleted. The retention of L protein in the endoplasmic reticulum was found to be mediated by a sequence contained within a region of 35 amino acids of the preS1 C-terminus, and not exclusively by amino acid sequences of the N-terminus of the preS1 domain as proposed by Kuroki at al. (Mol. Cell. Biol. 9, 4459-4466, 1989). Our finding could be explained by a specifically W promoter sequence leading to exclusive synthesis of L or deleted (delta)L proteins, respectively. The ability of the coexpressed HBV S protein to facilitate export of the delta L proteins was demonstrated by coinfection experiments. (C) 1994 Academic Press, Inc.

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页码：1024 / 1027

页数：4

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