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Virus Res. 2016 Jul 15;220:97-103. doi: 10.1016/j.virusres.2016.04.017. Epub 2016 Apr 20.

Human papillomavirus L1 protein expressed in Escherichia coli self-assembles into virus-like particles that are highly immunogenic.

Author information

1
College of Basic Medical Science, Zhengzhou University, Zhengzhou 450001, China; Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China.
2
Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China.
3
College of Basic Medical Science, Zhengzhou University, Zhengzhou 450001, China; Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China; College of Animal Science and Veterinary Medicine, Henan Agricultural University, Zhengzhou 450002, China. Electronic address: zhanggaiping2003@163.com.
4
School of Life Sciences, Zhengzhou University, Zhengzhou 450001, China. Electronic address: pingaw@126.com.
5
College of Basic Medical Science, Zhengzhou University, Zhengzhou 450001, China. Electronic address: dongzm@zzu.edu.cn.
6
School of Life Sciences, Zhengzhou University, Zhengzhou 450001, China.
7
College of Animal Science and Veterinary Medicine, Henan Agricultural University, Zhengzhou 450002, China.

Abstract

HPV vaccines based on L1 virus-like particles (VLPs) provided a high degree of protection against HPVs infection. In this study, the codon optimized HPV16 L1 gene were sub-cloned into five procaryotic expression vectors (pET-28a, pET-32a, pGEX-4T-2, pE-sumo and pHSIE), and fused with different protein tags. No recombinant proteins were expressed in pET-28a-L1 and pHSIE-L1, and the proteins expressed by pET-32a-L1 plasmid with TRX-tag were in the form of inclusion body. Only SUMO-tagged and GST-tagged L1 proteins expressed by pE-Sumo-L1 or pGEX-4T-L1 were soluble. The yield of SUMO-L1 protein reached 260mg/L fermentation medium in shake flask. After SUMO tags were eliminated, a 90% purity of L1 proteins was generated by ion-exchange and Ni-NTA affinity chromatography. The purified HPV16 L1 protein self-assembled into virus-like particles (VLPs) and showed a haemagglutination activity. High titers specific and neutralizing antibodies were detected in HPV 16 L1VLPs vaccinated mice. Cytokines such as IFN-γ and IL-2 showed significant higher in VLPs vaccinated mice compared with negative control (p<0.05, p=0.055). Thus, the expression of recombinant HPV16 L1 VLPs in Escherichia coli was feasible, which could potentially be used for a VLP-based HPV vaccine.

KEYWORDS:

Bacterial expression; Human papillomavirus; Neutralizing antibody; Splenic lymphocytes; Virus-like particles

PMID:
27107614
DOI:
10.1016/j.virusres.2016.04.017
[Indexed for MEDLINE]

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