The core protein of hepatitis C virus induces hepatocellular carcinoma in transgenic mice

10.1038/2053 ◽  
1998 ◽  
Vol 4 (9) ◽  
pp. 1065-1067 ◽  
Author(s):  
Kyoji Moriya ◽  
Hajime Fujie ◽  
Yoshizumi Shintani ◽  
Hiroshi Yotsuyanagi ◽  
Takeya Tsutsumi ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transgenic Mice ◽  
Core Protein ◽  
The Core

Prevalence of antibody against the core protein of hepatitis C virus in patients with hepatocellular carcinoma

1991 ◽  
Vol 48 (3) ◽  
pp. 340-343 ◽  
Author(s):  
Yushiro Watanabe ◽  
Shizuko Harada ◽  
Izumu Saito ◽  
Tatsuo Miyamura
Keyword(s):  
Hepatocellular Carcinoma ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Core Protein ◽  
The Core

scholarly journals Hepatitis C virus core protein modulates several signaling pathways involved in hepatocellular carcinoma

2019 ◽  
Vol 25 (1) ◽  
pp. 42-58 ◽  
Author(s):  
Shahab Mahmoudvand ◽  
Somayeh Shokri ◽  
Reza Taherkhani ◽  
Fatemeh Farshadpour
Keyword(s):  
Hepatocellular Carcinoma ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signaling Pathways ◽  
Core Protein ◽  
Virus Core

scholarly journals Proteasomal Turnover of Hepatitis C Virus Core Protein Is Regulated by Two Distinct Mechanisms: a Ubiquitin-Dependent Mechanism and a Ubiquitin-Independent but PA28γ-Dependent Mechanism

2008 ◽  
Vol 83 (5) ◽  
pp. 2389-2392 ◽  
Author(s):  
Ryosuke Suzuki ◽  
Kohji Moriishi ◽  
Kouichirou Fukuda ◽  
Masayuki Shirakura ◽  
Koji Ishii ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Core Protein ◽  
Loss Of Function ◽  
Proteasome Activator ◽  
Binding Partner ◽  
The Core ◽  
Virus Core ◽  
Lysine Residues ◽  
Dependent Mechanism

ABSTRACT We have previously reported on the ubiquitylation and degradation of hepatitis C virus core protein. Here we demonstrate that proteasomal degradation of the core protein is mediated by two distinct mechanisms. One leads to polyubiquitylation, in which lysine residues in the N-terminal region are preferential ubiquitylation sites. The other is independent of the presence of ubiquitin. Gain- and loss-of-function analyses using lysineless mutants substantiate the hypothesis that the proteasome activator PA28γ, a binding partner of the core, is involved in the ubiquitin-independent degradation of the core protein. Our results suggest that turnover of this multifunctional viral protein can be tightly controlled via dual ubiquitin-dependent and -independent proteasomal pathways.

scholarly journals A Disulfide-Bonded Dimer of the Core Protein of Hepatitis C Virus Is Important for Virus-Like Particle Production

2010 ◽  
Vol 84 (18) ◽  
pp. 9118-9127 ◽  
Author(s):  
Yukihiro Kushima ◽  
Takaji Wakita ◽  
Makoto Hijikata
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Particle Production ◽  
Rna Binding ◽  
Core Protein ◽  
Dominant Negative ◽  
Proteinase K ◽  
Dominant Negative Effect ◽  
The Core ◽  
Virus Like Particle

ABSTRACT Hepatitis C virus (HCV) core protein forms the nucleocapsid of the HCV particle. Although many functions of core protein have been reported, how the HCV particle is assembled is not well understood. Here we show that the nucleocapsid-like particle of HCV is composed of a disulfide-bonded core protein complex (dbc-complex). We also found that the disulfide-bonded dimer of the core protein (dbd-core) is formed at the endoplasmic reticulum (ER), where the core protein is initially produced and processed. Mutational analysis revealed that the cysteine residue at amino acid position 128 (Cys128) of the core protein, a highly conserved residue among almost all reported isolates, is responsible for dbd-core formation and virus-like particle production but has no effect on the replication of the HCV RNA genome or the several known functions of the core protein, including RNA binding ability and localization to the lipid droplet. The Cys128 mutant core protein showed a dominant negative effect in terms of HCV-like particle production. These results suggest that this disulfide bond is critical for the HCV virion. We also obtained the results that the dbc-complex in the nucleocapsid-like structure was sensitive to proteinase K but not trypsin digestion, suggesting that the capsid is built up of a tightly packed structure of the core protein, with its amino (N)-terminal arginine-rich region being concealed inside.

scholarly journals Polymorphisms of the core, NS3, and NS5A proteins of hepatitis C virus genotype 1b associate With development of hepatocellular carcinoma

Hepatology ◽  
2013 ◽  
Vol 58 (2) ◽  
pp. 555-563 ◽  
Author(s):  
Ahmed El-Shamy ◽  
Michiko Shindo ◽  
Ikuo Shoji ◽  
Lin Deng ◽  
Tadao Okuno ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Virus Genotype ◽  
The Core ◽  
Genotype 1B

scholarly journals Hepatitis C virus core protein induces hepatic steatosis in transgenic mice.

1997 ◽  
Vol 78 (7) ◽  
pp. 1527-1531 ◽  
Author(s):  
K Moriya ◽  
Y Matsuura ◽  
T Miyamura ◽  
K Koike ◽  
Y Shintani ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transgenic Mice ◽  
Hepatic Steatosis ◽  
Core Protein ◽  
Virus Core
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