Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo
Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo
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DOI：
10.1128/jvi.77.4.2784-2788.2003
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发表时间：
2003-02-01
影响因子：
5.4
通讯作者：
Hong, HJ
中科院分区：
文献类型：
--
作者：
Cho, DY;Yang, GH;Hong, HJ
病毒包膜蛋白的正常折叠和组装是由宿主伴侣蛋白介导的。在这项研究中，我们证明了内质网腔内伴侣GRP78/BiP在体外和体内分泌完整病毒颗粒时特异性结合到L蛋白的pre-S1结构域，这表明GRP78/BiP在L蛋白的正确折叠和/或病毒包膜蛋白的组装中起着重要作用。
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.