[High expression of the foot-and-mouth disease's structural protein P1 in Escherichia coli and analysis of its biology activity].
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.
Yu
Xiao-Lan
XL
Laboratory of Animal Virology, College of Animal Science and Animal medicine, Huazhong Agriculture University, Wuhan 430070, China.
Xiao
Shao-Bo
SB
Fang
Liu-Rong
LR
Hu
Meng-Yu
MY
Yan
Lin
L
Dong
Xiao-Hui
XH
Chen
Huan-Chun
HC
D036022:Capsid Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000276:immunology; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029544:Foot-and-Mouth Disease Virus / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000276:immunology
D036022:Capsid Proteins; D011993:Recombinant Fusion Proteins; C442501:VP1 protein, Foot-and-mouth disease virus