The spliced variant of hepatitis B virus protein, HBSP, interacts with Bcl-2/Bcl-xl in vitro and induces apoptosis in HepG2 cells.
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.
Lu
Yi Wei
YW
School of Chemical and Biomedical Engineering, Nanyang Technological University, 62 Nanyang Drive, Singapore 637459.
Ren
Yu Dan
YD
Bai
Jing
J
Chen
Wei Ning
WN
D017398:Alternative Splicing; D017209:Apoptosis / Q000502:physiology*; D002460:Cell Line; D006515:Hepatitis B virus / Q000378:metabolism*; D006801:Humans; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D051020:bcl-X Protein / Q000235:genetics / Q000378:metabolism*
C478361:HBSP protein, Hepatitis B virus; D020033:Protein Isoforms; D019253:Proto-Oncogene Proteins c-bcl-2; D014764:Viral Proteins; D051020:bcl-X Protein