Regulation of the Epstein-Barr virus capsid protein BDLF1 by ubiquitination and sumoylation

• Main Authors: Shih-Wei Jing, 荊士瑋
• Other Authors: Li-kwan Chang
• Format: Others
• Language: zh-TW
• Published: 2017
• Online Access: http://ndltd.ncl.edu.tw/handle/9mkxsd

碩士 === 國立臺灣大學 === 生化科技學系 === 106 === Epstein-Barr virus　(EBV) is the first discovered oncogenic virus and infect human B cells. EBV contains an icosahedral nucleocapsid which is composed by 12 pentameric, 150 hexameric capsomers and 320 triplexes. These capsomers are composed by the major capsid protein, VCA, and connected by triplexes forming by two minor capsid proteins, BORF1 and BDLF1. A previous study indicated that BDLF1interacts with BORF1, and then the proteins were transported to the PML nuclear bodies in the nucleus for the capsid assembly. BDLF1 has also been shown to be modified by SUMO-1. This study further demonstrated that BDLF1 is modified by SUMO-2 and ubiquitin. The BDLF1 K124 is the main modification site of SUMO-2 and ubiquitin. Moreover, the SUMO-interacting motifs (SIMs) of BDLF1 are required for the sumoylation of BDLF1, but not the ubiquitination of BDLF1, which thereby increases the stability of BDLF1. Additionally, BDLF1 SIMs promote the interaction of BDLF1 with BORF1, which may facilitate capsid assembly and virus proliferation.