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Methodology for the Efficient Generation of Fluorescently Tagged Vaccinia Virus Proteins
Published on: January 17, 2014
[Purification and identification of recombinant varicella-zoster virus glycoprotein E]
Fu-min Li1, Yu-ping Ran, Qi Wu
1Department of Dermatology, West China Hospital, Sichuan University, Chengdu 610041, China.
Objective:
To purify and identify recombinant Varicella-Zoster Virus Glycoprotein E.
Methods:
The recombinant plasmid pGEX-VZVgE was induced by isopropyl-beta-D-thiogalactoside (IPTG), the fusion protein was purified with affinity chromatography column; then the purified fusion protein was cleaved by thrombin, and the product's antigenicity was examined by Western blot.
Results:
The product of pGEX-VZVgE induced by IPTG was separated from the mixture proteins by the affinity chromatography column, the expressed fusion protein's relative molecular mass was about 98 x 10(3). After cleavage, the obtained VZV Glycoprotein E's relative molecular mass was about 72 x 10(3); the purified fusion protein and VZV Glycoprotein E were single band by SDS-PAGE. The available antigenicity of Glycoprotein E was confirmed by Western blot.
Conclusion:
Purification of VZV Glycoprotein E with affinity chromatography is an effective method. It provides a foreground for studies on the application of VZV gE.
