Abstract
Objective To express and purify the glycoprotein extracellular domain (Ex-GP) of Rabies virus strain CTN in soluble form with high efficiency. Methods A recombinant expression plasmid containing the gene encoding the Ex-GP was constructed. Various expression conditions were screened to obtain an optimum prokaryotic expression system for Ex-GP in soluble form. The expressed target protein was purified using affinity chromatography and gel filtration chromatography. Results The target protein Ex-GP with high antigenicity was efficiently expressed in soluble form by using the recombinant PBCX expression system and effectively purified by using affinity and gel filtration chromatography. Conclusion The soluble form of Ex-GP is successfully expressed and purified in a simple and convenient way. This study paves the way for further researches on the biological functions of rabies virus glycoprotein, the pathogenic mechanism of rabies and the development of diagnostic reagent and vaccines for rabies virus. Key words: Rabies virus; Glycoprotein extracellular domain; Soluble protein expression
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