Expression of hepatitis C virus subunit fusion protein and analysis of its immunogenicity.
- Author:
Feng QIU
1
;
Zhi-Yuan JIA
;
Min-Zhuo GUO
;
Si-Yong CHEN
;
Yao YI
;
Li-Ping SHEN
;
Tao YU
;
Yong-Liang FEI
;
Yu GUO
;
Sheng-Li BI
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Enzyme-Linked Immunosorbent Assay; Escherichia coli; genetics; metabolism; Hepacivirus; genetics; metabolism; Immunoassay; Rabbits; Recombinant Fusion Proteins; genetics; immunology; metabolism; Viral Proteins; genetics; immunology; metabolism
- From: Chinese Journal of Experimental and Clinical Virology 2010;24(2):113-115
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVEObtain the hepatitis C virus high purified subunit fusion protein and detect its immunogenicity.
METHODSWith the vector of pET-11d, fusion protein was expressed in Escherichia coli BL21 (DE3) after induced by IPTG. The protein was then purified by DEAE negative ion exchange chromatography and Ni2+ affinity chromatography. Western Blot analysis was used to detect the antigenicity of the fusion protein. At the same time, the sera were collected and prepared from the immunized experimental animals in order to investigate the immunogenicity of the protein by EIA.
RESULTSHigh purified hepatitis C virus subunit fusion protein was obtained successfully. The EIA indicated that the fusion protein could elicit specific antibodies in the animals with very high titers.
CONCLUSIONThe hepatitis C virus subunit fusion protein expressed in prokaryotic system was proved to have strong immunogenicity. It could provide some helpful and useful information to the hepatitis C virus prophylactic and therapeutic vaccine development.
