PMID: 9725668Sep 2, 1998Paper

Secretion and purification of HCV E1 protein forms as glutathione-S-transferase fusion in the baculovirus insect cell system

Virus Research
A R CiccaglioneM Rapicetta


We have expressed the E1 protein of Hepatitis C Virus (HCV) in a new recombinant form by using a baculovirus transfer vector directing the expression of proteins fused to the carboxy-terminus of glutathione-S-transferase (GST). The E1 domain was expressed varying at its carboxy terminus in order to retain (GST-E1) or delete (GST-E1b) the C-terminal hydrophobic region that may be involved in membrane association. Following infection with the recombinant virus, GST-E1b was efficiently secreted into the culture media and could be purified in a single step with the minimum of denaturation by glutathione affinity chromatography. The purified product was specifically immunoprecipitated by HCV positive human sera suggesting the maintenance of an immuno-relevant tertiary structure despite removal of the hydrophobic anchor. By contrast, cells infected with a recombinant baculovirus expressing GST-E1 gave a fusion protein with an appropriate molecular weight but also a series of polypeptides of lower molecular weight consistent with cleavage at the C-terminus of E1. GST-E1 was not secreted into the medium and was associated predominantly with the membrane fraction following cell disruption; the lower molecular weight forms were soluble a...Continue Reading


Jul 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·M HijikataK Shimotohno
Mar 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·R H Miller, R H Purcell
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May 1, 1996·The Journal of General Virology·A Fournillier JacobC Wychowski

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