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Journal of Virology, February 2003, p. 2784-2788, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2784-2788.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Molecular Chaperone GRP78/BiP Interacts with the Large Surface Protein of Hepatitis B Virus In Vitro and In Vivo

Dae-Yeon Cho, Gi-Hyeok Yang, Chun Jeih Ryu, and Hyo Jeong Hong*

Antibody Engineering Research Unit, Laboratory of Immunology, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon 305-600, Korea

Received 6 August 2002/ Accepted 24 October 2002

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.

* Corresponding author. Mailing address: Laboratory of Immunology, Korea Research Institute of Bioscience and Biotechnology, P.O. Box 115, Yusong, Taejon 305-600, Korea. Phone: 82-42-860-4122. Fax: 82-42-860-4597. E-mail: hjhong{at}kribb.re.kr.

Journal of Virology, February 2003, p. 2784-2788, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2784-2788.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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