Molecular Chaperone GRP78/BiP Interacts with the Large Surface Protein of Hepatitis B Virus In Vitro and In Vivo
- 15 February 2003
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 77 (4) , 2784-8
- https://doi.org/10.1128/jvi.77.4.2784-2788.2003
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.Keywords
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