A full-length and a truncated gene for the core protein of hepatitis C virus (HCV) were linked to the gene for glutathione S-transferase (GST), and the expression of each GST-HCV core fusion protein was analyzed. The truncated GST-HCV core (1-123) fusion protein was expressed as a mostly soluble and partly insoluble form comprising more than 50% of the total protein in Escherichia coli after induction by isopropylthio-beta-D-galactoside (IPTG), while the full length GST-HCV core (1-191) fusion protein was not expressed, suggesting that the hydrophobic carboxy terminal region in the core protein affects its expression. In addition, the GST-HCV core (1-123) fusion protein purified by GST-agarose chromatography reacted specifically with an anti-HCV serum from a patient.
Journal of virological methods. 1996 May;59(1-2):13-21. doi: 10.1016/0166-0934(95)01995-2 Q41.62025
Overexpression and simple purification of a truncated, immunologically reactive GST-HCV core (1-123) fusion protein
截短的GST-HCV核心(1-123)融合蛋白的过表达及其简易纯化方法 翻译改进
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DOI: 10.1016/0166-0934(95)01995-2 PMID: 8793826
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Keywords：HCV core protein; gene fusion
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