Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo

被引：52

作者：

Cho, DY ^{[1
]}

Yang, GH ^{[1
]}

Ryu, CJ ^{[1
]}

Hong, HJ ^{[1
]}

机构：

[1] Korea Res Inst Biosci & Biotechnol, Immunol Lab, Antibody Engn Res Unit, Taejon 305600, South Korea

来源：

JOURNAL OF VIROLOGY | 2003年 / 77卷 / 04期

关键词：

D O I：

10.1128/JVI.77.4.2784-2788.2003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The proper folding and assembly of viral envelope proteins are mediated by host chaperones. In this study, we demonstrated that an endoplasmic reticulum luminal chaperone GRP78/BiP bound specifically to the pre-S1 domain of the L protein in vitro and in vivo where complete viral particles were secreted, suggesting that GRP78/BiP plays an essential role in the proper folding of the L protein and/or assembly of viral envelope proteins.

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页码：2784 / 2788

页数：5

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