In this study, two FRET-based probes are constructed to research oligomerization of Epstein-Barr virus Oncoprotein LMP1 in live cells. The images of wide-field fluorescence microscopy display that the majority of two LMP1-associated probes co-localized in internal perinuclear membranes. Furthermore, the fluorescence spectra of single cell co-expressed two probes indicated that the ratio of two emission peaks is around one, and the fluorescence spectra changed insignificantly during an hour observation. These findings indicated that LMP1/LMP1 interacted stably in live cells.
Adenosine plays important roles in the pain signal transduction by activating adenosine receptors of two subtypes of A<sub>1</sub> and A<sub>2</sub><sub>A</sub>. In this study, FRET system based independent emission -spectral spectral spectral unmixing method (Iem-spFRET) was set up and used to measure the energy transfer from A<sub>1</sub>R to A<sub>2A</sub>R. The energy transfer efficiency calculated by Iem-spFRET is about 17.44%. All the above date and results demonstrate that FRET with special designed fluorescence proteins could be used to investigate the interaction between adenosine receptors.