+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Processing of the E1 glycoprotein of hepatitis C virus expressed in mammalian cells

Processing of the E1 glycoprotein of hepatitis C virus expressed in mammalian cells

Journal of General Virology 77: 1055-1064

The structural part of the hepatitis C virus (HCV) genome encodes a capsid protein, C, and two envelope glycoproteins, E1 and E2, released from the virus polyprotein precursor by signalase(s) cleavage(s). The processing of E1 was investigated by infecting simian cells with recombinant vaccinia viruses expressing parts of the HCV structural proteins. When the predicted E1 sequence was expressed alone (amino acid residues 174-370 of the polyprotein) or with the capsid protein gene (residues 1-370), it showed an apparent molecular mass of 35 kDa as measured by SDS-PAGE analysis. However, when El was expressed as part of a truncated C-E1-truncated E2 polypeptide (residues 132-383), the processed E1 product had the expected apparent molecular mass of 31 kDa, suggesting that flanking sequences are necessary for the generation of the mature 31 kDa E1 form. The N-terminal sequence of the two E1 forms was found to be the same. Analysis of the glycosylation pattern showed that, in both species, only four of the five potential N-linked glycosylation sites were recognized, indicating that glycosylation was not involved in the molecular mass difference. We showed that expression of E1 with or without the hydrophobic stretch of amino acids residues 371-383, defined as the E2 signal sequence, may be responsible for the difference in electrophoretic mobility of the two E1 species. In vitro translation assays and site-directed mutagenesis experiments suggest that this sequence remains part of the 31 kDa E1 mature protein.

Please choose payment method:

(PDF emailed within 0-6 h: $19.90)

Accession: 009248771

Download citation: RISBibTeXText

PMID: 8609471

DOI: 10.1099/0022-1317-77-5-1055

Related references

Processing of E1 and E2 glycoproteins of hepatitis C virus expressed in mammalian and insect cells. Virology 205(1): 141-150, 1994

E2 glycoprotein of genotype III Chinese isolates of hepatitis C virus expressed in mammalian cell as antigen for anti-E2 antibody detection. Chinese Medical Sciences Journal 13(2): 77-79, June, 1998

Binding of the coronavirus mouse hepatitis virus A59 to its receptor expressed from a recombinant vaccinia virus depends on posttranslational processing of the receptor glycoprotein. Journal of Virology 66(7): 4028-4039, 1992

Detection of B virus antibody in monkey sera using glycoprotein D expressed in mammalian cells. Journal of Clinical Microbiology 39(9): 3025-3030, 2001

Enzymatic characterization of hepatitis C virus NS3/4A complexes expressed in mammalian cells by using the herpes simplex virus amplicon system. Journal of Virology 70(7): 4261-4268, 1996

Investigation of interaction of preS1-addressed virus like particles with hepatitis B virus receptor NTCP expressed in mammalian cells. Journal of Biotechnology 231: S9-S10, 2016

Characterization of the hepatitis C virus E2/NS1 gene product expressed in mammalian cells. Virology 188(2): 819-830, 1992

Overcoming Challenges of Hepatitis C Virus Envelope Glycoprotein Production in Mammalian Cells. Methods in Molecular Biology 1911: 305-316, 2018

The hepatitis C virus E1 glycoprotein undergoes productive folding but accelerated degradation when expressed as an individual subunit in CHO cells. Plos One 6(8): E23838-E23838, 2012

Characterization of caprine herpesvirus 1 (CpHV1) glycoprotein E and glycoprotein I ectodomains expressed in mammalian cells. Veterinary Microbiology 164(3-4): 222-228, 2014

Intracellular localization of full-length and truncated hepatitis C virus core protein expressed in mammalian cells. Journal Of Hepatology. 20(6): 833-836, 1994

Establishment of a cell line constitutively expressing E2 glycoprotein of hepatitis C virus and humoral response of hepatitis C patients to the expressed protein. Journal of General Virology 76: 1223-1231, 1995

Expression of glycoprotein hepatitis C virus in mammalian cell and application of purified protein for detection of antibody against E2 in hepatitis C patients. Zhonghua Gan Zang Bing Za Zhi 7(4): 214-216, 2000

Mammalian phosphoglucomutase transiently expressed by a recombinant vaccinia virus is a glycoprotein. Molecular Biology of the Cell 4(SUPPL ): 309A, 1993

Expression of full length hepatitis E virus open reading frame 2 and processing of the major capsid protein in the endoplasmic reticulum of mammalian cells. Hepatology 24(4 PART 2): 412A, 1996