Expression of E6 Protein Gene of Human Papillomavirus Type 11 in E.Coli

Objective To express the gene encoding E6 protein of Human Papillomavirus type 11(HPV11) and purify the E6 protein.Methods The HPV11 E6 gene was amplified from samples of condylome acumiuatum(CA) by PCR,cloned into vector pET32a to form pET32a/E6 plasmid and then transfected into the E.coli BL21.The thioredoxin-E6 fusion protein(Trx-E6) was expressed when induced by adding of IPTG and purified with 3S NTA Resin affinity column.SDS-PAGE and Western blotting were used to detect the expressed protein. Results The recombinant plasmid was identified and confirmed with enzyme digestion and sequencing.A high level expression of Trx-E6 fusion protein was obtained and purified successfully.SDS-PAGE and Western Blotting suggested that the recombinant fusion protein was a 36,000 Dalton molecular weight protein reacted with anti-His antibody.Conclusion Trx-E6 protein of HPV11 could be expressed with high efficiency in prokaryotic expression system.