Abstract
The complete (encoding 55 amino acids, aa) or partial (encoding aa 1–26) preS2 region gene of hepatitis B virus (HBV) was fused to the 3′-end of glutathion-S-transferase (GST) gene and expressed under the control of the inducible tac promoter in Escherichia coli at 37 °C. The fusion protein with the complete preS2 region was moderately expressed (8%) while the protein with the N-terminal 26 aa was expressed at a higher level, yielding about 20% of the total cellular proteins. The GST-preS2 (aa 1–26) protein, which contains the immunodominant epitope, was produced form the soluble protein fraction of the recombinant bacteria and purified by affinity chromatography using glutathione-agarose column. The purified preS2 fusion protein showed the antigenicity of preS2, as assessed by indirect and competitive ELISAs.
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Kang, Y.J., Kim, Y.S., Hur, H. et al. Efficient expression and characterization of hepatitis B virus preS2 antigen in Escherichia coli . Biotechnology Letters 21, 375–380 (1999). https://doi.org/10.1023/A:1005487105048
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DOI: https://doi.org/10.1023/A:1005487105048