Folding, Assembly and Subcellular Localization of Hepatitis C Virus Glycoproteins

2000 ◽  
pp. 135-148 ◽  
Author(s):  
J. Dubuisson
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization

scholarly journals The N-terminal helix α0 of hepatitis C virus NS3 protein dictates the subcellular localization and stability of NS3/NS4A complex

Virology ◽  
2012 ◽  
Vol 422 (2) ◽  
pp. 214-223 ◽  
Author(s):  
Ying He ◽  
Leiyun Weng ◽  
Rui Li ◽  
Li Li ◽  
Tetsuya Toyoda ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Ns3 Protein

scholarly journals NS3 protein of Hepatitis C virus associates with the tumour suppressor p53 and inhibits its function in an NS3 sequence-dependent manner

2006 ◽  
Vol 87 (6) ◽  
pp. 1703-1713 ◽  
Author(s):  
Lin Deng ◽  
Motoko Nagano-Fujii ◽  
Motofumi Tanaka ◽  
Yuki Nomura-Takigawa ◽  
Masanori Ikeda ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Serine Protease ◽  
Protease Activity ◽  
Hcv Rna ◽  
Dependent Manner ◽  
Diffuse Type ◽  
Serine Protease Activity ◽  
Tumour Suppressor P53

The N-terminal 198 residues of NS3 (NS3-N) of Hepatitis C virus (HCV) subtype 1b obtained from 29 patients, as well as full-length NS3 (NS3-Full), were analysed for their subcellular localization, interaction with the tumour suppressor p53 and serine protease activity in the presence and absence of the viral cofactor NS4A. Based on the subcellular-localization patterns in the absence of NS4A, NS3-N sequences were classified into three groups, with each group exhibiting either dot-like, diffuse or a mixed type of localization. Chimeric NS3-Full sequences, each consisting of an individual NS3-N and a shared C-terminal sequence, showed the same localization patterns as those of the respective NS3-N. Site-directed mutagenesis experiments revealed that a single or a few amino acid substitutions at a particular position(s) of NS3-N altered the localization pattern. Interestingly, NS3 of the dot-like type, either NS3-N or NS3-Full, interacted with p53 more strongly than that of the diffuse type, in both the presence and the absence of NS4A. Moreover, NS3-N of the dot-like type suppressed trans-activating activity of p53 more strongly than that of the diffuse type. Serine protease activity did not differ significantly between the two types of NS3. In HCV RNA replicon-harbouring cells, physical interaction between NS3 and p53 was observed consistently and p53-mediated transcriptional activation was suppressed significantly compared with HCV RNA-negative control cells. Our results collectively suggest the possibility that NS3 plays an important role in the hepatocarcinogenesis of HCV by interacting differentially with p53 in an NS3 sequence-dependent manner.

scholarly journals The hepatitis C virus NS5A inhibitor (BMS-790052) alters the subcellular localization of the NS5A non-structural viral protein

Virology ◽  
2011 ◽  
Vol 414 (1) ◽  
pp. 10-18 ◽  
Author(s):  
Choongho Lee ◽  
Han Ma ◽  
Julie Qi Hang ◽  
Vincent Leveque ◽  
Ella H. Sklan ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Viral Protein ◽  
Ns5a Inhibitor

scholarly journals Subcellular Localization and Topology of the p7 Polypeptide of Hepatitis C Virus

2002 ◽  
Vol 76 (8) ◽  
pp. 3720-3730 ◽  
Author(s):  
Séverine Carrère-Kremer ◽  
Claire Montpellier-Pala ◽  
Laurence Cocquerel ◽  
Czeslaw Wychowski ◽  
François Penin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Secretory Pathway ◽  
Transmembrane Domain ◽  
Signal Sequence ◽  
C Terminus ◽  
Membrane Spanning ◽  
Polytopic Membrane Protein

ABSTRACT Although biological and biochemical data have been accumulated on most hepatitis C virus proteins, the structure and function of the 63-amino-acid p7 polypeptide of this virus have never been investigated. In this work, sequence analyses predicted that p7 contains two transmembrane passages connected by a short hydrophilic segment. The C-terminal transmembrane domain of p7 was predicted to function as a signal sequence, which was confirmed experimentally by analyzing the translocation of a reporter glycoprotein fused at its C terminus. The p7 polypeptide was tagged either with the ectodomain of CD4 or with a Myc epitope to study its membrane integration, its subcellular localization, and its topology. Alkaline extraction studies confirmed that p7 is an integral membrane polypeptide. The CD4-p7 chimera was detected by immunofluorescence on the surface of nonpermeabilized cells, indicating that it is exported to the plasma membrane. However, pulse-chase analyses showed that only approximately 20% of endoglycosidase H-resistant CD4-p7 was detected after long chase times, suggesting that a large proportion of p7 stays in an early compartment of the secretory pathway. Finally, by inserting a Myc epitope in several positions of p7 and analyzing the accessibility of this epitope on the plasma membrane of HepG2 cells, we showed that p7 has a double membrane-spanning topology, with both its N and C termini oriented toward the extracellular environment. Altogether, these data indicate that p7 is a polytopic membrane protein that could have a functional role in several compartments of the secretory pathway.

scholarly journals Analysis of the subcellular localization of hepatitis C virus E2 glycoprotein in live cells using EGFP fusion proteins

2003 ◽  
Vol 84 (3) ◽  
pp. 561-566 ◽  
Author(s):  
François Kien ◽  
Jean-Daniel Abraham ◽  
Catherine Schuster ◽  
Marie Paule Kieny
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Fusion Protein ◽  
Subcellular Localization ◽  
Fluorescent Protein ◽  
Live Cells ◽  
Target Cells ◽  
E2 Glycoprotein ◽  
Covalently Linked ◽  
Green Fluorescent

Hepatitis C virus (HCV) E1 and E2 glycoproteins assemble intracellularly to form a non-covalently linked heterodimer, which is retained in the endoplasmic reticulum (ER). To study the subcellular localization of E2 in live cells, the enhanced green fluorescent protein (EGFP) was fused to the N terminus of E2. Using fluorescence and confocal microscopy, we have confirmed that E2 is located in the ER, where budding of HCV virions is thought to occur. Immunoprecipitation experiments using a conformation-sensitive antibody and a GST pull-down assay showed that fusion of EGFP to E2 interferes neither with its heterodimeric assembly with E1, nor with proper folding of the ectodomain, nor with the capacity of E2 to interact with human CD81, indicating that the EGFP–E2 fusion protein is functional. As a tool to study binding of E2 to target cells, we also described the expression of an EGFP–E2 fusion protein at the cell surface.

scholarly journals SUBCELLULAR LOCALIZATION OF HEPATITIS C VIRUS STRUCTURAL PROTEINS IN THE LIVER OF TRANSGENIC MICE

1997 ◽  
Vol 50 (4-5) ◽  
pp. 169-177 ◽  
Author(s):  
Kyoji MORIYA ◽  
Hajime FUJIE ◽  
Hiroshi YOTSUYANAGI ◽  
Yoshizumi SHINTANI ◽  
Takeya TSUTSUMI ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transgenic Mice ◽  
Subcellular Localization ◽  
Structural Proteins

scholarly journals Regulated processing of hepatitis C virus core protein is linked to subcellular localization.

1997 ◽  
Vol 71 (1) ◽  
pp. 657-662 ◽  
Author(s):  
Q Liu ◽  
C Tackney ◽  
R A Bhat ◽  
A M Prince ◽  
P Zhang
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Core Protein ◽  
Virus Core

scholarly journals Differential Subcellular Localization of Hepatitis C Virus Core Gene Products

Virology ◽  
1995 ◽  
Vol 213 (2) ◽  
pp. 455-461 ◽  
Author(s):  
SHIH-YEN LO ◽  
FRANK MASIARZ ◽  
SOON B. HWANG ◽  
MICHAEL M.C. LAI ◽  
JING-HSIUNG OU
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Core Gene ◽  
Gene Products ◽  
Virus Core
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