Expression and purification of EBV-LMP2 protein.
- Author:
Zhan WANG
1
;
Jing MA
;
Ling ZHOU
;
Xiao-Guang ZHANG
;
Hai-Jun DU
;
Song-Mei YANG
;
Yi ZENG
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Baculoviridae; genetics; pathogenicity; Blotting, Western; Electrophoresis, Polyacrylamide Gel; Genetic Vectors; Herpesvirus 4, Human; genetics; isolation & purification; metabolism; Insecta; cytology; Membrane Proteins; genetics; isolation & purification; metabolism; Recombinant Proteins; genetics; metabolism; Viral Matrix Proteins; genetics; isolation & purification; metabolism
- From: Chinese Journal of Experimental and Clinical Virology 2010;24(3):168-170
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo obtain a second Epstein-Barr virus membrane protein (LMP2) in insect cells.
METHODSThe full length EBV-LMP2 gene was inserted into baculovirus expression transfer vector pFastBac HT B to obtain the recombinant baculoviruses Bac-LMP2. And generation of recombinant baculoviruses was followed by transfection of the recombinant Bac-LMP2 into insect cells, then the recombinant LMP2 protein was recognized by SDS-PAGE and western blot. The expressed LMP2 protein was purified by one step with Ni-NTA metal chelation chromatography.
RESULTSThe expressed LMP2 protein was confirmed by SDS-PAGE and western blot. The purity of purified LMP2 protein is up to 86% by HPLC analysis.
CONCLUSIONThe EBV-LMP2 was expressed in insect cells, and the purified LMP2 protein was obtained.
