Cloning and Expression of Human Papillomavirus Type 6 L1 Gene

Objective:To express optimized-code fusion protein L1 of human papillomavirus type 6 (HPV6) in E.coli BL21 (DE3). Methods:HPV6 L1 gene was amplified by PCR and the optimized-code HPV6 mL1 gene was synthesized basing on sequencing and sequence comparison. The HPV6 mL1 gene was inserted into the prokaryotic vector pGEX4T-1 to construct the expression plasmid,and then the HPV6 mL1 protein was expressed after induction of IPTG in E.coli BL21(DE3). The fusion protein was determined by SDS-PAGE. Results:Restriction enzyme digestion analysis and DNA sequencing showed that the prokaryotic expression system of HPV6 mL1 gene was constructed successfully. When induced by 1 mmol / L IPTG lasted 4 h at 37℃,fusion protein HPV6 L1 was expressed in inclusion body form. SDS-PAGE showed that the molecular weight of fusion protein was 80 kD and was identical with predict size. Conclusion:Fusion protein HPV6 L1 was obtained,which provides a basis for further vaccine and functional assay.