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

文献类型： 外文期刊

作者： Chen, Yumei 1 ; Liu, Yunchao 2 ; Zhang, Gaiping 1 ; Wang, Aiping 4 ; Dong, Ziming 1 ; Qi, Yanhua 4 ; Wang, Jucai 3 ; Zhao 1 ;

作者机构： 1.Zhengzhou Univ, Coll Basic Med Sci, Zhengzhou 450001, Peoples R China

2.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

3.Henan Agr Univ, Coll Anim Sci & Vet Med, Zhengzhou 450002, Peoples R China

4.Zhengzhou Univ, Sch Life Sci, Zhengzhou 450001, Peoples R China

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

期刊名称：VIRUS RESEARCH （ 影响因子：3.303； 五年影响因子：3.445 ）

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收录情况： SCI

摘要： 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 260 mg/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-gamma 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. (C) 2016 Elsevier B.V. All rights reserved.

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