Expression and purification of rabies virus protein P: production and characterization of anti-P polyclonal antibodies

Authors

  • Yan Pan
  • Xian-Ming Meng
  • Xian-Kai Wei
  • Jun Li
  • Zhuan-Ling Lu
  • Hai-Bo Tang
  • Jing-Jing Liang
  • Ting Rong Luo

Keywords:

rabies virus, P protein, protein expression and purification, polyclonal antibodies

Abstract

Rabies virus (RV) phosphoprotein (P) is a multifunctional protein. However, the functions of this protein are
not fully understood. To further investigate this question, the P protein was expressed and used to raise monospecific
polyclonal antibodies. The gene coding for P protein was cloned into expression vector pET-32a (+) to yield pET-32a
(+)-P. His-tagged P protein was expressed in E. coli BL21 cells and analyzed by SDS-PAGE. After purification by nickel
affinity chromatography under native conditions, the recombinant P protein was used to raise anti-P polyclonal
antibodies in mice. Western blot analysis showed that the P protein was recognized by the polyclonal antibodies.
Immunofluorescence assays also showed that the antibody was able to recognize the native P protein in RV-infected
cells.

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Published

2018-08-02

How to Cite

Pan, Y., Meng, X.-M., Wei, X.-K., Li, J., Lu, Z.-L., Tang, H.-B., Liang, J.-J., & Luo, T. R. (2018). Expression and purification of rabies virus protein P: production and characterization of anti-P polyclonal antibodies. The Thai Journal of Veterinary Medicine, 48(2), 257–264. Retrieved from https://he01.tci-thaijo.org/index.php/tjvm/article/view/137830

Issue

Section

Original Articles