Objective: To amplify HCV P7 gene and clone it into several prokaryotic expression systems

then investigate the effects of these working systems and harvest HCV P7 protein with biologic activity.Methods: Design Special primers were designed for the amplification of HCV P7 complete DNA sequence and amplify P7 DNA fragments were amplified with H/FL plasmid as template by PCR.The obtained P7 DNA fragments were directly cloned into pQE30

pGEX 4T-2 and pET32a(+) prokaryotic expression vectors and transform these recombinant plasmids were transformed into E coli.strain BL21(DE3) pLysS or SG13009(PREP4)

and IPTG was added to induce recombinant E coli.expression.The expression products were identified with SDS-PAGE and Western blot.Results: There was no track of non-fusion HCV P7 protein expression from recombinant E coli

including pQE30/HCV P7 or pET32a(+)-Nde/HCV P7 plasmid.But the study succeeded in the expression and purification of recombinant HCV P7 proteins

Both are all soluble and biologic activity

and are expected to use extensively in anti-HCV virus research.