S-Space College of Natural Sciences (자연과학대학) Dept. of Biological Sciences (생명과학부) Journal Papers (저널논문_생명과학부)
Interaction between nucleophosmin and HBV core protein increases HBV capsid assembly
- Jeong, Heewon; Cho, Min-Hyung; Park, Sung-Gyoo; Jung, Guhung
- Issue Date
- FEBS Letters, Vol.588 No.6, pp. 851-858
- 자연과학; Hepatitis B virus (HBV); Core protein truncated at residue 149
(Cp149); Core assembly; Encapsidation; Host factor; Nucleophosmin (B23)
- Host factors are involved in Hepatitis B virus (HBV) genome replication and capsid formation during the viral life cycle. A host factor, nucleophosmin (B23), was found to bind to HBV core protein dimers, but its functional role has not been studied. This interaction promoted HBV capsid assembly and decreased the degree of capsid dissociation when subjected to denaturant treatments in vitro. In addition, inhibition of B23 reduced intracellular capsid formation resulting in a decrease of HBV production in HepG2.2.15 cells. These results provide important evidence that B23 acts on core capsid assembly via its interaction with HBV core dimers.Structured summary of protein interactions:B23 and Cp149 colocalize by cosedimentation through density gradient (View interaction)Cp149 physically interacts with B23 by anti bait coimmunoprecipitation (1, 2)B23 and B23 bind by blue native page (View interaction)Cp149 and B23 bind by cosedimentation through density gradient (View interaction)B23 binds to Cp149 by anti bait coimmunoprecipitation (1, 2, 3, 4) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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