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.
School of Chemical and Biomedical Engineering, Nanyang Technological University, 62 Nanyang Drive, Singapore 637459.
Yi Wei
YW
Lu
Yu Dan
YD
Ren
Jing
J
Bai
Wei Ning
WN
Chen
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