Construction of Recombinant Plasmid for Expression of HBV PreS2-MBP Fusion Protein in E.coli

Objective To express HBV PreS2-MBP fusion protein in E.coli then identify and purify the expressed product.Methods Clone the full length of HBV PreS2 gene into prokaryotic expression vector pMAL-P2x by recombinant DNA technique,then transform to E.coli for expression under induction of IPTG.Identify the expressed product by SDS-PAGE and Western blot then purify by anion-exchange and Amylose Resin affinity chromatography.Results Recombinant plasmid pMAL-P2x/S2 was successfully constructed.The MBP-labeled PreS2-MBP fusion protein with good antigenicity was expressed in a soluble form and successfully purified by Amylose Resion affinity chromatography.Conclusion HBV PreS2-MBP fusion protein was successfully expressed in pMAL-P2x system.