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- W2372183044 abstract "Objective To express HPV16 MuE6/E7 chimeric protein and study its immunogenicity and antitumor activity.MethodsTransform the constructed recombinant expression vector for MuE6/E7 protein to E.coli BL21(λDE3) for expression under induction of IPTG.The expressed product,in a form of inclusion body,was separated,purified,de-naturalized and re-naturalized,then further purified by ion exchange and molecular sieve chromatography,and identified by SDS-PAGE,Western blot,HPLC and mass spectrography.Immunize C57BL/6 mice with the purified protein to evaluate the immunogenicity and antitumor activity.Results The expressed product,with a relative molecular mass of about 21 000,contained about 23.06% of total somatic protein and reached a purity of 97.17% after purification.High titer specific antibody against HPV was induced in the mice immunized with 3 doses of purified MuE6/E7 protein.The antibody titer was positively related to the dosage of purified protein.The protein protected the immunized mice against challenge with TC-1 tumor cells and prolonged the survival time of mice with tumor caused by TC-1 cells.Conclusion Recombinant MuE6/E7 protein was expressed and purified and showed a certain curative effect on the mice with tumor caused by TC-1 cells,which laid a foundation of further development of therapeutic HPV vaccine." @default.
- W2372183044 created "2016-06-24" @default.
- W2372183044 creator A5039286166 @default.
- W2372183044 date "2008-01-01" @default.
- W2372183044 modified "2023-09-24" @default.
- W2372183044 title "Prokaryotic Expression,Purification and Immune Effect of HPV16 MuE6/E7 Chimeric Protein" @default.
- W2372183044 hasPublicationYear "2008" @default.
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