期刊
VIROLOGY
卷 410, 期 1, 页码 161-169出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.11.005
关键词
Hepatitis B virus (HBV); Core protein truncated at residue 149 (Cp149); Host factor; Heat shock protein 90 (Hsp90); Encapsidation; Core assembly; Capsid dissociation
类别
资金
- Korea government, Korea [M10863000016-08N6300-01610]
- Ministry of Education and Human Resources Developments
The mechanism by which host factors contribute to hepatitis B virus (HBV) capsid formation during the viral life cycle remains unclear. This study analyzed the interaction between heat shock protein 90 (Hsp90), a host factor, and the HBV core protein. Hsp90 was found to bind to HBV core protein dimers, which was then encapsidated into the HBV capsid. Furthermore, activated Hsp90 may facilitate the formation of the human HBV capsid by catalyzing core assembly and reducing the degree of capsid dissociation at various temperatures, both in vitro and in vivo, and when subjected to detergent treatments in vitro. In addition, inhibition or downregulation of Hsp90 reduced HBV production in HepG2.2.15 cells. These results showed that Hsp90 plays an important role in HBV capsid stabilization and HBV formation. (C) 2010 Elsevier Inc. All rights reserved.
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