›› 2013, Vol. 40 ›› Issue (10): 61-64.

Previous Articles     Next Articles

Prokaryotic Expression and Purification of Glycoprotein Gene of Rabies Virus

FU Hong-qing1, YAO Zhi-lan1, LU Jiang1, LIU Jun-dong1, JIA Hong2   

  1. 1. Jiangsu Agri-animal Husbandry Vocational College, Taizhou 225300, China;
    2. Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China
  • Revised:2013-08-16 Online:2013-10-20 Published:2013-12-19

Abstract: In order to improve the expression level of glycoprotein gene of rabies virus (RV) in Escherichia coli BL21(DE3), the optimal conditions for expression of RV G fusion protein (GST-RVG) were analyzed by SDS-PAGE, including different temperatures, different inducing times and concentrations of IPTG. The protein was purified by GST-resin affinity column. The results showed that the expression level of fusion protein expressed in Escherichia coli BL21(DE3) at 30 ℃ for 6 h, and induced with 1 mmol/mL IPTG was highest.The fusion protein was about 36 ku,which was consistent with the expected. The result of Western blotting showed that the fusion protein had good immunogenicities and specificities. Optimizing the expression and purification of RV G fusion protein was benefit for developing sub-unit vaccine and neutralizing antibody of RV.

Key words: rabies virus; glycoprotein; fusion protein; purification

CLC Number: