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The spliced variant of hepatitis B virus protein, HBSP, interacts with Bcl‐2/Bcl‐xl in vitro and induces apoptosis in HepG2 cells
Author(s) -
Lu Yi Wei,
Ren Yu Dan,
Bai Jing,
Chen Wei Ning
Publication year - 2008
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.108
Subject(s) - bcl xl , in vitro , apoptosis , gene , hepatitis b virus , virus , microbiology and biotechnology , gene product , biology , chemistry , virology , gene expression , programmed cell death , genetics
We have recently reported that the naturally occurring spliced variant of Hepatitis B virus protein, HBSP, displayed proapoptotic activity through its BH3 domain. To investigate whether the BH3 domain in HBSP interacted with Bcl‐2 family of proteins, HBSP and Bcl‐2 family of proteins were cloned and expressed in our mammalian two‐hybrid system. Interaction assays were carried out in HepG2 cells and measured by the activity of the reporter gene product luciferase. Our results indicated that HBSP interacted with Bcl‐2/Bcl‐xl in vitro and induced apoptosis in HepG2 cells. © 2008 IUBMB IUBMB Life, 60(10): 700–702, 2008