scholarly journals Hepatitis C Virus Core Protein: Carboxy-Terminal Boundaries of Two Processed Species Suggest Cleavage by a Signal Peptide Peptidase

Virology ◽  
1996 ◽  
Vol 224 (1) ◽  
pp. 93-104 ◽  
Author(s):  
Peter Hüssy ◽  
Hanno Langen ◽  
Jan Mous ◽  
Helmut Jacobsen
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Core Protein ◽  
Signal Peptide Peptidase ◽  
Virus Core ◽  
Carboxy Terminal

scholarly journals Signal Peptide Peptidase-catalyzed Cleavage of Hepatitis C Virus Core Protein Is Dispensable for Virus Budding but Destabilizes the Viral Capsid

2006 ◽  
Vol 281 (38) ◽  
pp. 27679-27692 ◽  
Author(s):  
Christelle Vauloup-Fellous ◽  
Véronique Pène ◽  
Julie Garaud-Aunis ◽  
Francis Harper ◽  
Sabine Bardin ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Core Protein ◽  
Viral Capsid ◽  
Virus Budding ◽  
Signal Peptide Peptidase ◽  
Virus Core

scholarly journals Maturation of Hepatitis C Virus Core Protein by Signal Peptide Peptidase Is Required for Virus Production

2008 ◽  
Vol 283 (24) ◽  
pp. 16850-16859 ◽  
Author(s):  
Paul Targett-Adams ◽  
Graham Hope ◽  
Steeve Boulant ◽  
John McLauchlan
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Core Protein ◽  
Virus Production ◽  
Signal Peptide Peptidase ◽  
Virus Core

Abstract 812: Processing of core protein by signal peptide peptidase participates in propagation and pathogenesis of hepatitis C virus

2015 ◽  
Author(s):  
Toru Okamoto ◽  
Sayaka Aizawa ◽  
Takahisa Kouwaki ◽  
Tatsuya Suzuki ◽  
Takasuke Fukuhara ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Core Protein ◽  
Signal Peptide Peptidase

scholarly journals Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and E1 proteins of hepatitis C virus strain J1

2006 ◽  
Vol 87 (3) ◽  
pp. 623-627 ◽  
Author(s):  
R. Graham Hope ◽  
Marion J. McElwee ◽  
John McLauchlan
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Core Protein ◽  
Signal Peptidase ◽  
Wild Type ◽  
Signal Peptide Peptidase ◽  
Standard Buffer ◽  
Hcv Core Protein ◽  
Mutant Forms

Maturation of hepatitis C virus (HCV) core protein requires cleavage by signal peptidase (SP) and signal peptide peptidase (SPP) at a signal peptide between core and the E1 glycoprotein. For HCV strain Glasgow, amino acids Ala180, Ser183 and Cys184 within the signal peptide have previously been shown to be essential for efficient SPP cleavage. By contrast, these residues apparently did not contribute to core maturation in HCV strain J1. In the present study, the source of this discrepancy has been analysed and it is concluded that interpretation of the strain J1 data was incorrect, due to the inability to separate wild-type and mutant forms of core on gels by using standard buffer systems.

scholarly journals Intramembrane Processing by Signal Peptide Peptidase Regulates the Membrane Localization of Hepatitis C Virus Core Protein and Viral Propagation

2008 ◽  
Vol 82 (17) ◽  
pp. 8349-8361 ◽  
Author(s):  
Kiyoko Okamoto ◽  
Yoshio Mori ◽  
Yasumasa Komoda ◽  
Toru Okamoto ◽  
Masayasu Okochi ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Core Protein ◽  
Biological Significance ◽  
Signal Peptidase ◽  
Signal Peptide Peptidase ◽  
Viral Propagation ◽  
The Core ◽  
Hcv Core Protein

ABSTRACT Hepatitis C virus (HCV) core protein has shown to be localized in the detergent-resistant membrane (DRM), which is distinct from the classical raft fraction including caveolin, although the biological significance of the DRM localization of the core protein has not been determined. The HCV core protein is cleaved off from a precursor polyprotein at the lumen side of Ala191 by signal peptidase and is then further processed by signal peptide peptidase (SPP) within the transmembrane region. In this study, we examined the role of SPP in the localization of the HCV core protein in the DRM and in viral propagation. The C terminus of the HCV core protein cleaved by SPP in 293T cells was identified as Phe177 by mass spectrometry. Mutations introduced into two residues (Ile176 and Phe177) upstream of the cleavage site of the core protein abrogated processing by SPP and localization in the DRM fraction. Expression of a dominant-negative SPP or treatment with an SPP inhibitor, L685,458, resulted in reductions in the levels of processed core protein localized in the DRM fraction. The production of HCV RNA in cells persistently infected with strain JFH-1 was impaired by treatment with the SPP inhibitor. Furthermore, mutant JFH-1 viruses bearing SPP-resistant mutations in the core protein failed to propagate in a permissive cell line. These results suggest that intramembrane processing of HCV core protein by SPP is required for the localization of the HCV core protein in the DRM and for viral propagation.

scholarly journals Core protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly

2006 ◽  
Vol 87 (4) ◽  
pp. 855-860 ◽  
Author(s):  
Malika Ait-Goughoulte ◽  
Christophe Hourioux ◽  
Romuald Patient ◽  
Sylvie Trassard ◽  
Denys Brand ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Signal Peptide ◽  
Semliki Forest Virus ◽  
Core Protein ◽  
Protein Cleavage ◽  
Particle Assembly ◽  
Signal Peptide Peptidase ◽  
Hcv Core Protein ◽  
Er Membrane

Hepatitis C virus (HCV) core protein, expressed with a Semliki Forest virus replicon, self-assembles into HCV-like particles (HCV-LP) at the endoplasmic reticulum (ER) membrane, providing an opportunity to study HCV assembly and morphogenesis by electron microscopy. This model was used to investigate whether the processing of the HCV core protein by the signal peptide peptidase (SPP) is required for the HCV-LP assembly. Several mutants were designed as there are conflicting reports concerning the cleavage of mutant proteins by SPP. Production of the only core mutant protein that escaped SPP processing led to the formation of multiple layers of electron-dense ER membrane, with no evidence of HCV-LP assembly. These data shed light on the HCV core residues involved in SPP cleavage and suggest that this cleavage is essential for HCV assembly.

Biosynthesis and biochemical properties of the hepatitis C virus core protein.

1994 ◽  
Vol 68 (6) ◽  
pp. 3631-3641 ◽  
Author(s):  
E Santolini ◽  
G Migliaccio ◽  
N La Monica
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Core Protein ◽  
Biochemical Properties ◽  
Virus Core
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