High expression of the foot-and-mouth disease's structural protein P1 in Escherichia coli and analysis of its biology activity.
- Author:
Xiao-Lan YU
1
;
Shao-Bo XIAO
;
Liu-Rong FANG
;
Meng-Yu HU
;
Lin YAN
;
Xiao-Hui DONG
;
Huan-Chun CHEN
Author Information
1. Laboratory of Animal Virology, College of Animal Science and Animal medicine, Huazhong Agriculture University, Wuhan 430070, China.
- Publication Type:Journal Article
- MeSH:
Capsid Proteins;
biosynthesis;
genetics;
immunology;
Escherichia coli;
genetics;
metabolism;
Foot-and-Mouth Disease Virus;
genetics;
Recombinant Fusion Proteins;
biosynthesis;
genetics;
immunology
- From:
Chinese Journal of Biotechnology
2005;21(1):163-166
- CountryChina
- Language:Chinese
-
Abstract:
Foot-and-mouth disease virus (FMDV) is the aetiological angent of a highly contagious viral disease. The complete gene encoding the structural protein of FMDV (P1) was subcloned into expression vector pGEX-KG, resulting in the fusion expression plasmid pKG-P1. After transformed into E. coli BL21(DE3) and induced by IPTG, the results of SDS-PAGE showed that the GST-P1 fusion protein was expressed in high level. The molecular weight of the fusion protein wa 110kD and the expressed products were soluble. Western-blotting was performed to confirm that the expressed fusion protein could specifically react with antiserum against FMDV. The fusion proteins were further purified by GST purification kit and an indirect ELISA (P1-ELISA) based on the purified proteins was developed. Comparison between P1-ELISA and the standard indirect haemagglutinin assay showed the two methods had 87 per cent agreement by detecting 864 serum samples, indicating the purified P1 protein was specific as the antigen of indirect P1-ELISA.
