A Protein-protein Interaction of Virus-host Visualized by the BiMC Assay Technique

被引:0
|
作者
Yang, Jing [1 ]
Du, Shu-Juan [1 ]
Zuo, Lie-Lian [1 ]
Liu, Ling-Zhi [1 ]
Wu, Hong-Zhuan [2 ]
Li, Gui-Yuan [1 ]
Lu, Jian-Hong [1 ]
机构
[1] Cent S Univ, Xiangya Sch Basic Med Sci, Canc Res Inst, Changsha, Hunan, Peoples R China
[2] Alabama State Univ, Dept Biol Sci, Montgomery, AL 36101 USA
来源
2015 INTERNATIONAL CONFERENCE ON BIOMEDICAL ENGINEERING AND LIFE SCIENCE (BELS 2015) | 2015年
关键词
Bimolecular complementation; Cyclophilin A; Epstein-Barr virus; Visualized interaction; EPSTEIN-BARR-VIRUS; MOLECULAR-INTERACTIONS; CELLS;
D O I
暂无
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
The bimolecular complementation (BiMC) assay is a useful tool for a detection of protein-protein interaction, which locates in living cells and is able to be visualized under a fluorescent microscope. Cyclophilin A (CYPA) was found to be overexpressed in nasopharyngeal carcinoma in our previous study. The result also prompted us to explore the relationship between CYPA and Epstein-Barr virus nuclear antigen 1 (EBNA1). Here we identified their interaction by the BiMC assay. Plasmids expressing these two proteins fused with the C-or Y-terminus of YFP for this assay system were constructed firstly. After their co-transfection into 293T cells, specific nuclear fluorescence was observed. The results demonstrated that CYPA can bind to EBNA1, which deserved a further study of their functions.
引用
收藏
页码:263 / 268
页数:6
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