Cloning and expression of human papillomavirus type16L1E7in E.coli

Objective:To study the expression of fusion protein of HPV16capsid protein L1and transforming protein E7in E.coli.Methods :HPV16L1E7DNA fragment was amplified by poly-merase chain reaction from recombinant pUC19L1E7,the fragment was then cloned into the pMD18-T.After being digested by BglⅡ,the HPV16L1E7was inserted into the expression vector pQE30,and was transformed into E.coli M15.The recombinant vector was induced by IPTG to express the fusion protein.The antigenicity of HPV16L1E7and the expression level were detected by Western blot.Re -sults:The expression protein could reactivate the anti-L1linear epitope antibody.Conclusion:The HPV16L1E7fusion gene can express the L1E7fusion protein in E.coli sucessfully and at high level,the L1E7takes up above25%of total cell protein.