[Construction, Expression, Purification and Antiviral Activity of Fused Interferon-BLA (IFN-BLA).].
A fusion protein, Interferon-BLA (IFN-BLA), was constructed with IFN-beta-1b and IFN-alpha-2b separating by a linker -GGGS-. The laboratory-scale expression conditions in E.coli BL21 CodonPlus (DE3)-RIL had been optimized and IFN-BLA was expressed higher than 35% of total protein in the cells mainly as inclusion body. The inclusion body of IFN-BLA was denatured and refolded by dialysis and purified by ion-exchange chromatography. The overall yield of IFN-BLA was about 45 mg/L with purity higher than 90%. Antiviral activity assay suggested that this newly fused protein may have synergetic or additive antiviral activities.
Ma
Wen-Zhe
WZ
Shanghai CASB Biotechnology Co., Chinese Academy of Scieneces, Shanghai 200233, China, Email: wzma@sibs.ac.cn.
Shen
Qiong
Q
Han
Wei
W
Lu
Chen-Yi
CY
Yang
Sheng-Li
SL
Gong
Yi
Y
D000998:Antiviral Agents; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D011994:Recombinant Proteins
D000998:Antiviral Agents; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins