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J. Biol. Chem., Vol. 275, Issue 39, 30605-30609, September 29, 2000
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From the CNRS-Unité Mixte de Recherche 8526, Institut
de Biologie de Lille/Institut Pasteur de Lille, 59021 Lille Cedex and
the § CNRS-UMR8576, Université des Sciences et
Technologies de Lille, 59655, Villeneuve d'Ascq Cedex, France
The addition of N-linked
oligosaccharides to Asn-X-(Ser/Thr) sites is catalyzed by
the oligosaccharyltransferase, an enzyme closely associated with the
translocon and generally thought to have access only to nascent chains
as they emerge from the ribosome. However, the presence of the sequon
does not automatically ensure core glycosylation because many proteins
contain sequons that remain either nonglycosylated or glycosylated to a
variable extent. In this study, hepatitis C virus (HCV) envelope
protein E1 was used as a model to study the efficiency of
N-glycosylation. HCV envelope proteins, E1 and E2, were
released from a polyprotein precursor after cleavage by host signal
peptidase(s). When expressed alone, E1 was not efficiently
glycosylated. However, E1 glycosylation was improved when expressed as
a polyprotein including full-length or truncated forms of E2. These
data indicate that glycosylation of E1 is dependent on the presence of
polypeptide sequences located downstream of E1 on HCV polyprotein.
Glycosylation of the Hepatitis C Virus Envelope Protein E1 Is
Dependent on the Presence of a Downstream Sequence on the Viral
Polyprotein*
,
*
This work was supported by the CNRS, the Institut Pasteur de
Lille, a European Regional Development Fund (ERDF) and Grant 9736 from
the Association Pour la Recherche sur le Cancer.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Equipe Hépatite
C, CNRS-UMR8526, Institut de Biologie de Lille & Institut Pasteur de
Lille, 1 rue Calmette, BP447, 59021 Lille cedex, France. Tel.: 33-3-20-87 11-60; Fax: 33-3-20-87-11-11; E-mail:
jean.dubuisson@ibl.fr.
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