Expression and Bioactivities Study on IFN-IgG Fc Fusion Protein in Lactobacillus casei
GAO Xu-wen1,2,CHEN Hui3,JIA Rui-qing2,YAO Li-hong2,MA Chang-wei1,ZHANG Zhi-qing2, (1.College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China; 2.Institute for Virus Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China; 3.Capital Medical University, Beijing 100069, China)
Expressing bioactive polypeptide by using gene modified LAB is one of the most popular researches in the world. It has a good potential to develop new functional food. IFN-α-2b and IgG Fc gene were PCR amplified and linked by a flexible hinge to code for a fusion protein IFN-IgG Fc. The fusion gene was cloned to pSC111 AE vector and electro-transformed into Lactobacillus casei ATCC393. We studied the biological activities of the expression product in vitro. The results showed that we can detect the fusion protein in the supernatant by Western-Blot. The results of ELISA showed that there is no effect on conformation and biological activity between the two proteins. We found that supernatant of recombinant LAB can introduce the antiviral activity in WISH cells and the anti-viral activity of the product is about 1.71×103IU/ml. The study laid a foundation for further use of modified LAB in the domains of food technology and drug development.
【CateGory Index】：
Q789
CAJViewer7.0 supports all the CNKI file formats; AdobeReader only supports the PDF format.