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Cloning and Expression of Truncated Human Papillomavirus Type 18 E6 Protein(HPV18 E6

Liqiang Fan

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Abstract

Objective To construct HPV18 E6* prokaryotic expression plasmid and optimize its expression.Methods HPV18 E6* gene was amplified by PCR with HeLa cell cDNA as template.After cloning it into expression vector pET-28a(+),HPV18 E6* protein was expressed by induction with IPTG in E.coli BL21(DE3) and detected by SDS-PAGE.Results Recombinant expression vector was constructed and SDS-PAGE showed that recombinant HPV18 E6* was about 20% of the total bacterial proteins,and was mainly expressed as inclusion bodies at 37 ℃ and soluble at 15 ℃.So the pure protein was obtained from inclusion bodies.Conclusion The highly expressed HPV18 E6* protein provides fundamental basis for the further study on HPV18 E6* mechanism as well as prevention and treatment of uterine cancer.

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What this paper is about

Objective To construct HPV18 E6* prokaryotic expression plasmid and optimize its expression.Methods HPV18 E6* gene was amplified by PCR with HeLa cell cDNA as template.After cloning it into expression vector pET-28a(+),HPV18 E6* protein was expressed by induction with IPTG in E.coli BL21(DE3) and detected by SDS-PAGE.Results Recombinant expression vector was constructed and SDS-PAGE showed that recombinant HPV18 E6* was about 20% of the total bacterial proteins,and was mainly expressed as inclusion bodies at 37 ℃ and soluble at 15 ℃.So the pure protein was obtained from inclusion bodies.Conclusion The highly expressed HPV18 E6* protein provides fundamental basis for the further study on HPV18 E6* mechanism as well as prevention and treatment of uterine cancer.

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Available abstract

Objective To construct HPV18 E6* prokaryotic expression plasmid and optimize its expression.Methods HPV18 E6* gene was amplified by PCR with HeLa cell cDNA as template.After cloning it into expression vector pET-28a(+),HPV18 E6* protein was expressed by induction with IPTG in E.coli BL21(DE3) and detected by SDS-PAGE.Results Recombinant expression vector was constructed and SDS-PAGE showed that recombinant HPV18 E6* was about 20% of the total bacterial proteins,and was mainly expressed as inclusion bodies at 37 ℃ and soluble at 15 ℃.So the pure protein was obtained from inclusion bodies.Conclusion The highly expressed HPV18 E6* protein provides fundamental basis for the further study on HPV18 E6* mechanism as well as prevention and treatment of uterine cancer.

Key concepts: Recombinant DNA, Cloning (programming), Complementary DNA, lac operon, Molecular biology, Expression vector, Inclusion bodies, Biology

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Cloning and Expression of Truncated Human Papillomavirus Type 18 E6 Protein(HPV18 E6 — Research Paper | ScholarLens