title: Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo.
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.
authors.affiliation: Antibody Engineering Research Unit, Laboratory of Immunology, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon 305-600, Korea.
authors.forename: Dae-Yeon
authors.initials: DY
authors.lastname: Cho
authors.forename: Gi-Hyeok
authors.initials: GH
authors.lastname: Yang
authors.forename: Chun Jeih
authors.initials: CJ
authors.lastname: Ryu
authors.forename: Hyo Jeong
authors.initials: HJ
authors.lastname: Hong
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D002352:Carrier Proteins / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D006515:Hepatitis B virus / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D011817:Rabbits; D014407:Tumor Cells, Cultured; D014759:Viral Envelope Proteins / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; C000717247:HSPA5 protein, human; D006360:Heat-Shock Proteins; C096362:L protein, hepatitis B virus; D018832:Molecular Chaperones; D014759:Viral Envelope Proteins