Title Characterization of the rapamycin-inducible EBV LMP1 activation system
Author Sang Yong Kim, Jung-Eun Kim, Jiyeon Won, and Yoon-Jae Song*
Address Department of Life Science, Gachon University, Seongnam 13120, Republic of Korea
Bibliography Journal of Microbiology, 53(10),732-738, 2015,
DOI 10.1007/s12275-015-5455-z
Key Words Epstein-Barr virus, latent membrane protein 1, NF-κB
Abstract Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is required for EBV-mediated B lymphocyte transformation into proliferating lymphoblastoid cell lines (LCL). LMP1 oligomerizes spontaneously in membrane lipid rafts via its transmembrane domain and constitutively activates signal transduction pathways, including NF-κB, p38 Mitogen-Activated Protein Kinase (MAPK), and c-Jun N-terminal Kinase (JNK). Since LMP1 mimics the tumor necrosis factor receptor (TNFR), CD40, it may be effectively utilized to study the effects of constitutive activation of signal transduction pathways on cellular physiology. On the other hand, LMP1 presents a disadvantage in terms of determining the sequential events and factors involved in signaling pathways. A CD40-LMP1 chimeric molecule has been generated to overcome this limitation but does not represent the authentic and physiological nature of LMP1. In the current study, a ligand-dependent activation system for LMP1 using rapamycin-inducible dimerization was generated to delineate the LMP1 signaling pathway.