Expression and Bioactivities Study on IFN-IgG Fc Fusion Protein in Lactobacillus casei

Abstract

Abstract: 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.

Key words: lactic acid bacteria, interferon, fusion protein, antivirus

GAO Xu-Wen, CHEN Hui, JIA Run-Qing, YAO Li-Hong, MA Chang-Wei, ZHANG Zhi-Qing. Expression and Bioactivities Study on IFN-IgG Fc Fusion Protein in Lactobacillus casei[J]. FOOD SCIENCE, 2007, 28(1): 205-208.

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Expression and Bioactivities Study on IFN-IgG Fc Fusion Protein in Lactobacillus casei

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