Cloning, Expression and Purification of a Novel Fusion Protein Composed of Flagellin and NS5B of Hepatitis C Virus in Escherichia coli Host

Background: At present, there is an increased demand for recombinant proteins and the process development for production has high potential to speed up. Then, scale up of the developed process are critical if commercial production is the desired. Objectives: In this survey, we intend to produce a recombinant fusion protein of flagellin (fliC) and the N terminal fragment (NT300) of NS5B gene. Methods: After expressing the fusion protein in the proper host (E. coli), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western Blot were used for evaluating the expressed protein. Results: Results showed that fliC-NT300 recombinant fusion protein was properly cloned in pET28a vector following by successfully expressed in E. coli. SDS-PAGE and Western Blotting techniques confirmed a protein with a molecular weight of 86 kDa. Conclusions: Our data indicated that the novel recombinant fusion protein (fliC-NT300) was well produced by the pET28a vector in E. coli system.