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Glycobiology, 2002, Vol. 12, No. 2 95-101
© 2002 Oxford University Press

Glycosylation of the hepatitis C virus envelope protein E1 occurs posttranslationally in a mannosylphosphoryldolichol-deficient CHO mutant cell line

Sandrine Duvet1,3, Anne Op De Beeck1,4, Laurence Cocquerel4, Czeslaw Wychowski4, René Cacan3 and Jean Dubuisson2,4

3CNRS-UMR 8576/USTL, 59655 Villeneuve d’Ascq Cedex, France; 4Unité Hépatite C, CNRS-FRE2369, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille Cedex, France

The addition of N-linked glycans to a protein is catalyzed by oligosaccharyltransferase, an enzyme closely associated with the translocon. N-glycans are believed to be transferred as the protein is being synthesized and cotranslationally translocated in the lumen of the endoplasmic reticulum. We used a mannosylphosphoryldolichol-deficient Chinese hamster ovary mutant cell line (B3F7 cells) to study the temporal regulation of N-linked core glycosylation of hepatitis C virus envelope protein E1. In this cell line, truncated Glc3Man5GlcNAc2 oligosaccharides are transferred onto nascent proteins. Pulse-chase analyses of E1 expressed in B3F7 cells show that the N-glycosylation sites of E1 are slowly occupied until up to 1 h after protein translation is completed. This posttranslational glycosylation of E1 indicates that the oligosaccharyltransferase has access to this protein in the lumen of the endoplasmic reticulum for at least 1 h after translation is completed. Comparisons with the N-glycosylation of other proteins expressed in B3F7 cells indicate that the posttranslational glycosylation of E1 is likely due to specific folding features of this acceptor protein.

1 These authors contributed equally to the results of this study.

2 To whom correspondence should be addressed


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