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

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Title
Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo
Author(s)
Dae Yeon Cho; Gi Hyeok Yang; Chun Jeih Ryu; Hyo Jeong Hong
Bibliographic Citation
Journal of Virology, vol. 77, no. 4, pp. 2784-2788
Publication Year
2003
Abstract
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.
ISSN
0022-538X
Publisher
Amer Soc Microb
DOI
http://dx.doi.org/10.1128/JVI.77.4.2784-2788.2003
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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