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J Gen Virol. 2000 Aug;81(Pt 8):1913-25.

Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein.

Author information

1
MRC Virology Unit, Division of Virology, University of Glasgow, Church Street, Glasgow G11 5JR, UK.

Abstract

From analysis of the primary sequence of the hepatitis C virus (HCV) core protein, we have identified three separable regions based on hydrophobicity and clustering of basic amino acids within the protein. Comparison with capsid proteins of related pesti- and flaviviruses suggested that HCV core has a unique central domain (domain 2). Previous findings have revealed that core protein can associate with lipid droplets which are intracellular storage sites for triacylglycerols and cholesterol esters. Confocal analysis of variant forms lacking regions of core indicated that most residues within the unique region are necessary for association of the protein with lipid droplets. A segment within domain 2 (from residues 125 to 144) also was required for stability of the protein and a polypeptide lacking these sequences was degraded apparently by the proteasome. In cells depleted of lipid droplets, core protein remained located in the cytoplasm. Moreover, cleavage of the protein at the maturation site and stability were not affected by inability to bind to lipid droplets.

PMID:
10900028
DOI:
10.1099/0022-1317-81-8-1913
[Indexed for MEDLINE]

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