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

Autor:	R. Graham Hope, John McLauchlan
Rok vydání:	2000
Předmět:	Base Sequence Viral Core Proteins Amino Acid Motifs Molecular Sequence Data Lipid metabolism Biology Lipid Metabolism Cleavage (embryo) Proteasome Capsid Biochemistry Cytoplasm Virology Lipid droplet Amino Acid Sequence Protein Precursors Sequence motif Peptide sequence
Zdroj:	Journal of General Virology. 81:1913-1925
ISSN:	1465-2099 0022-1317
DOI:	10.1099/0022-1317-81-8-1913
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4be2e12115c3d546a5cb3e588fbaf336 https://doi.org/10.1099/0022-1317-81-8-1913 Zobrazit plný text záznamu