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J. Biol. Chem., Vol. 277, Issue 23, 20625-20630, June 7, 2002
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From the The envelope glycoproteins, E1 and E2, of
hepatitis C virus (HCV) assemble intracellularly to form a noncovalent
heterodimer that is expected to be essential for viral assembly and
entry. However, due to the lack of a cell culture system supporting
efficient HCV replication, it is very difficult to obtain relevant
information on the functions of this glycoprotein oligomer. To get
better insights into its biological and biochemical properties, HCV
envelope glycoprotein heterodimer expressed by a vaccinia virus
recombinant was purified by immunoaffinity. Purified E1E2 heterodimer
was recognized by conformation-dependent monoclonal
antibodies, showing that the proteins were properly folded. In
addition, it interacted with human CD81, a putative HCV receptor, as
well as with human low and very low density lipoproteins, which have
been shown to be associated with infectious HCV particles isolated from
patients. Purified E1E2 heterodimer was also reconstituted into
liposomes. E1E2-liposomes were recognized by a
conformation-dependent monoclonal antibody as well as
by human CD81. Together, these data indicate that E1E2-liposomes are a
valuable tool to study the molecular requirements for HCV binding to
target cells.
Reconstitution of Hepatitis C Virus Envelope Glycoproteins into
Liposomes as a Surrogate Model to Study Virus Attachment*
§,¶,
,,
CNRS-Institut de Biologie de Lille & Institut Pasteur de Lille, 59021 Lille Cedex, France and the
** INSERM-U545, Institut Pasteur de Lille, Faculté de
Pharmacie - Université de Lille 2, 59019 Lille Cedex, France
*
This work was supported by the CNRS, the Institut
Pasteur de Lille, the "Réseau National Hépatite" from
the French Ministry of Research, a European Regional Development Fund
(ERDF), European Union Grant QLK2-1999-00356, and Grant 5651 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.
Successively supported by an Association pour la Recherche sur
le Cancer and an Agence Nationale de Recherches sur le SIDA fellowship.
To whom correspondence should be addressed: Unité
Hépatite C, CNRS-UPR2511, Institut de Biologie 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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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