Abstract：In oeder to investigate the effects of C terminal SPRY domain of TRIM22 on its transcription, translation and subcellular localization, SPRY domain was deleted (ΔSPRY) and amplified through polymerase chain reaction (PCR) and was then inserted into the eukaryotic expression plasmid, pcDNA3.1. Plasmids expressing wild type TRIM22 or TRIM22-ΔSPRY were transfected into HepG2 cells. The mRNA expression level was determined by semiquantitative reverse transcriptase PCR (RT-PCR), the protein expression level was determined by Western blot analysis, and the subcellular localization was determined by immunofluorescence staining. The results showed that plasmid expressing TRIM22-ΔSPRY was successfully constructed. After transfection into HepG2 cells, the TRIM22-ΔSPRY showed no difference from the wild type TRIM22 at both mRNA and protein levels. However TRIM22-ΔSPRY was localized exclusively to the cytoplasm of HepG2 cells in contrast to the nuclear localization of wild type TRIM22. These results may be useful for studying the role of SPRY domain in TRIM22-mediated antiviral activities.
高波; 段志坚; 徐薇; 熊思东. 抗病毒固有免疫分子TRIM22C端SPRY结构域对其转录、翻译及亚细胞定位的影响[J]. 微生物与感染
, 2010, 5(1): 31-35 .
GAO Bo; DUAN Zhi-Jian; XU Wei; XIONG Si-Dong. The contribution of the C terminal SPRY domain of TRIM22 to its own transcription, translation, and subcellular localization. Journal of Microbes and Infections, 2010, 5(1): 31-35 .
2010, Vol. 5 
