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• W3098851311 abstract "Abstract Objective To purify the Human Papillomavirus 16 (HPV-16) L1 protein encoded by a cloned L1 gene from a sample of cervical cancer from a Cuban patient and fused to a histidine tag at its carboxyl end (L1-His) from E. coli SHuffle® T7. Methods The strain E. coli SHuffle® T7 with the plasmid pETHPV16L1myc-His was used to obtain the HPV-16 L1-His protein, grown under autoinduction conditions. L1-His protein was purified by Ni2+ ion-chelated affinity chromatography (Ni2+-IMAC), after extraction of the inclusion bodies (IB) with 8 M urea and subsequent refolding by an inverse dilution method. The molecular size of the refolded HPV-16 L1-His protein was analyzed by native polyacrilamide gel electrophoresis and molecular exclusion chromatography. Results The HPV-16 L1-His protein accumulated in IB in E. coli SHuffle® T7 and represented ∼12% of total proteins. After its extraction with 8 M urea from IB was purified by Ni2+-IMAC, with an ∼90% purity and an ∼40% yield. Renaturation of purified L1-His allowed obtaining ∼9 mg of pentamers/L of culture, with a final recovery of ∼62%. Conclusions For the first time it was described the purification of pentamers of HPV-16 L1-His protein encoded by a cloned L1 gene from a Cuban patient from E. coli SHuffle® T7´s IB. The developed strategy could be an alternative for obtaining L1-His protein capsomers for developing a vaccine candidate against HPV-16.’" @default.
• W3098851311 created "2020-11-23" @default.
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• W3098851311 date "2020-07-01" @default.
• W3098851311 modified "2023-10-01" @default.
• W3098851311 title "Purification of the human papillomavirus 16 L1 protein from E. coli SHuffle® T7" @default.
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• W3098851311 doi "https://doi.org/10.1016/j.vacune.2020.10.003" @default.
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