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KMID : 0578319940040020189
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Molecules and Cells
1994 Volume.4 No. 2 p.189 ~ p.193
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Expression, Purification and Characterization of hepatitis B Virus preS1 Fusion Protein in Escherichia coli
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Rhyum, sun Boon
Jin, Byung Rae/ryu, Chun Jeij/Hong, Hyo Jeong
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Abstract
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The preS1 region gene fragment encoding the N-terminal 90 amino acid of hepatitis B virus (HBV, adr subtype), which encodes B- and T-cell epitopes and a hepatocyte receptor binding site, was synthesized by polymerase chain reaction (PCR) and fused to the 3´-end of the WE gene encoding maltose-binding protein (MBP) to yield expression plasmid pMalpreSl-90. The expression plasmid was introduced into E coli BL21 (DE3) and expressed at 37 C under the control of the inducible tac promoter. The resulting preSI fusion protein with the partially degraded form was highly expressed in soluble form, about 38% of total cellular proteins. The fusion protein did not bind to an amylose resin column and thus was purified by ammonium sulfate fractionation, anion-exchange chromatography and gel filtration to homogeneity. Characterization of the purified fusion proteins showed that they displayed the antigenicity and immunogenicity of the preSI antigen.
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KEYWORD
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