Open AccessMolecular 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
Publication year - 2003
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.77.4.2784-2788.2003
Subject(s) - endoplasmic reticulum , biology , chaperone (clinical) , microbiology and biotechnology , protein folding , in vitro , in vivo , viral envelope , hepatitis b virus , viral protein , virology , virus , biochemistry , genetics , medicine , pathology
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.