[Purification and identification of recombinant varicella-zoster virus glycoprotein E].
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.


CONCLUSIONS
Purification of VZV Glycoprotein E with affinity chromatography is an effective method. It provides a foreground for studies on the application of VZV gE.
Li
Fu-min
FM
Department of Dermatology, West China Hospital, Sichuan University, Chengdu 610041, China.
Ran
Yu-ping
YP
Wu
Qi
Q
Duan
De-jian
DJ
Zhao
Xiu-hong
XH
Chen
Ju-ping
JP
Zhou
Guang-ping
GP
D015153:Blotting, Western; D002846:Chromatography, Affinity; D014645:Herpesvirus 3, Human; D006801:Humans; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000302:isolation & purification; D014759:Viral Envelope Proteins / Q000032:analysis* / Q000302:isolation & purification*
D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins; C056913:glycoprotein E, varicella-zoster virus