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Published on: June 26, 2020
[Prokaryotic expression and polyclonal antibody preparation of truncated duck hepatitis B virus core protein]
Chao Wang1, Yong-jun Tian, E-juan Zhang
1Division of Clinical Immunology, Tongji Hospital of Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China. celful60@yahoo.com.cn
Aim:
To construct a prokaryotic plasmid expressing truncated duck hepatitis B virus core protein (DHBc(1-214)), purify the recombinant protein, and to develop polyclonal antibodies against DHBc.
Methods:
DHBc(1-214) was cloned into vector pRSET-B, then expressed in E.coli Rosetta(DE3) pLacI induced by IPTG. The recombinant protein was purified using Ni-NTA spin column. Polyclonal antibody was developed by immunizing BALB/c mice with the purified recombinant protein, and their sensitivity and specificity were tested using enzyme-linked immunosorbent assay, immunohistochemical staining and Western blot analysis.
Results:
Recombinant plasmid expressing truncated DHBc(1-214) was successfully constructed. A protein of 28,000 was expressed and purified. Polyclonal serum antibody with a high specificity was obtained by immunizing BALB/c mice with the purified recombinant protein.
Conclusion:
The truncated recombinant DHBc(1-214) developed in this study is purified and shown strong antigenecity. The polyclonal antibody against DHBc protein is generated by regular immunization method, demonstrating both high sensitivity and specificity. The protein and the antibody can be used for further clinical examination and research of DHBV.
