ABSTRACT
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.
