›› 2013, Vol. 40 ›› Issue (4): 36-39.

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Prokaryotic Expression and Purification of Matrix Protein of BD-06 Strain Rabies Virus and Preparation of its Polyclonal Antibody

ZHAO Xue-chao1,2, ZHANG Xue-wei1, ZHANG Shou-feng2, LIU Ye2, MI Li-juan2, HU Rong-liang2   

  1. 1. Department of Animal Science,Tianjin Agricultural University,Tianjin 300384,China;
    2. Institute of Military Veterinary,Academy of Military Medical Sciences,Changchun 130122,China
  • Received:2012-12-18 Online:2013-04-20 Published:2013-04-19

Abstract: The objective of this study was to obtain polyclonal antibody against the matrix protein of rabies virus in order to provide materials for further study on the function of matrix protein. The full sequence of the matrix protein gene from the BD-06 strain rabies virus was successfully cloned and inserted into the expression vector pET28a. The results of restriction enzyme digesting and sequencing proved that the matrix protein gene was correctly inserted into pET28a. After the expression plasmid was transformed into E.coli Rosetta and induced by 0.5 mmol/L IPTG, 27 ku M protein was obtained. After the matrix protein was purified and vaccinated the rabbit,the polyclonal antibody was obtained. The results of Western blotting and IFA showed that the antibody could react with the rabies virus. The matrix protein in the BHK-21 cell affected by BD-06 strain rabies virus was positioned by using the polyclonal antibody. The results indicated that the polyclonal antibody against the matrix protein of rabies virus was successfully prepared, which laid a foundation for further study on matrix protein of rabies virus.

Key words: rabies virus; matrix protein; prokaryotic expression; polyclonal antibody

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