Expression, purification and characterization of Hepatitis B virus preS1 fusion protein in Escherichia coli

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Title
Expression, purification and characterization of Hepatitis B virus preS1 fusion protein in Escherichia coli
Author(s)
Sun Boon Rhyum; Byung Rae Jin; Chun Jeih Ryu; Hyo Jeong Hong
Bibliographic Citation
Molecules and Cells, vol. 4, no. 2, pp. 189-193
Publication Year
1994
Abstract
The complete (encoding 119 aminon acids, aa) or partial (encoding the N-terminal 90 aa) preS1 region gene of hepatitis B virus (HBV) was fused to the 3-end of glutathione-S-transferase (GST) gene and expressed at 37 C under the control of the inducible tac promoter in E. coli. The results showed that the fusion protein with the full length of preS1 was moderately expressed, about 10% of total cellular proteins, while the protein with the partial preS1 was highly expressed, about 33% of total cellular proteins but the half was degraded into the protein with about N-terminal 60 aa of preS1. Accordingly, GST fusion protein containing the N-terminal 56 aa of the preS1, which still encodes B-and T-cell epitopes and a hepatocyte receptor binding site, was expressed under the same induction conditions and was shown to be highly and stably expressed, about 37% of total cellular proteins. The fusion protein with the full length or N-terminal 56 aa of preS1 and the peptides were simply and successfully purified by affinity chromatography and were demonstrated to exhibit the antigenicity and immunogenicity of the preS1 antigen.
ISSN
1016-8478
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.1007/BF00129021
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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