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J. Biol. Chem., Vol. 277, Issue 6, 4261-4270, February 8, 2002
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From the In mammalian tissue culture cells, the core
protein of hepatitis C virus (HCV) is located at the surface of lipid
droplets, which are cytoplasmic structures that store lipid. The
critical amino acid sequences necessary for this localization are in a region of core protein that is absent in flavi- and pestiviruses, which
are related to HCV. From our sequence comparisons, this region in HCV
core was present in the corresponding protein of GBV-B, another virus
whose genomic sequence has significant similarity to HCV. Expression of
the putative GBV-B core protein revealed that it also was directed to
lipid droplets. By extending the comparisons to cellular proteins,
there were amino acid sequence similarities between the domains for
lipid droplet association in HCV core and plant oleosin proteins. To
determine whether these similarities were related functionally, an
oleosin encoded by the Brassica napus bniii
gene was expressed in different mammalian cell lines, where it retained
the capacity to bind to lipid droplets. Analysis of deletion mutants
indicated that the critical region within the protein required for this
localization was the same for both plant and mammalian cells. A common
feature in the viral and plant sequences was a motif containing proline
residues. Mutagenesis of these residues in HCV core and plant oleosin
abolished lipid droplet association. Finally, the domain within HCV
core required for binding to lipid droplets could substitute for the
equivalent domain in oleosin, further indicating the functional
relatedness between the viral and plant sequences. These studies
identify common features in disparate proteins that are required for
lipid droplet localization.
The Domains Required to Direct Core Proteins of Hepatitis C Virus
and GB Virus-B to Lipid Droplets Share Common Features with Plant
Oleosin Proteins*
,¶
MRC Virology Unit, Institute of Virology,
Church Street, Glasgow G11 5JR and § School of Applied
Sciences, University of Glamorgan, Trefforrest,
Cardiff CF37 1DL, United Kingdom
*
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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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