Down-regulation of phosphatase and tensin homolog by hepatitis C virus core 3a in hepatocytes triggers the formation of large lipid droplets

Hepatology ◽  
2011 ◽  
Vol 54 (1) ◽  
pp. 38-49 ◽  
Author(s):  
Sophie Clément ◽  
Marion Peyrou ◽  
Andrea Sanchez-Pareja ◽  
Lucie Bourgoin ◽  
Pierluigi Ramadori ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Lipid Droplets ◽  
Down Regulation ◽  
Phosphatase And Tensin Homolog ◽  
Tensin Homolog ◽  
Virus Core

scholarly journals Structural Determinants That Target the Hepatitis C Virus Core Protein to Lipid Droplets

2006 ◽  
Vol 281 (31) ◽  
pp. 22236-22247 ◽  
Author(s):  
Steeve Boulant ◽  
Roland Montserret ◽  
R. Graham Hope ◽  
Maxime Ratinier ◽  
Paul Targett-Adams ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Lipid Droplets ◽  
Core Protein ◽  
Structural Determinants ◽  
Virus Core

Dynamics of lipid droplets induced by the hepatitis C virus core protein

2010 ◽  
Vol 399 (4) ◽  
pp. 518-524 ◽  
Author(s):  
Rodney K. Lyn ◽  
David C. Kennedy ◽  
Albert Stolow ◽  
Andrew Ridsdale ◽  
John Paul Pezacki
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Lipid Droplets ◽  
Core Protein ◽  
Virus Core

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

2000 ◽  
Vol 81 (8) ◽  
pp. 1913-1925 ◽  
Author(s):  
R. Graham Hope ◽  
John McLauchlan
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Lipid Droplets ◽  
Core Protein ◽  
Sequence Motifs ◽  
Primary Sequence ◽  
Unique Region ◽  
Virus Core ◽  
Hcv Core Protein ◽  
Intracellular Storage

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.

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