ArticleJournal of virology2008
Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
57 citing papers in PubMed, 101 citations in OpenAlex.
- Hepatitis C virus p7 regulates Core protein processing via signal peptide peptidase to promote virion assembly.Journal of virology · 2026Article
- Signal peptide peptidase- and SPP-like 3-dependent shedding of α1,6-fucosyltransferase differentially affects core fucosylation.The Journal of biological chemistry · 2026Article
- Structural insights into human signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Article
- Signal peptide peptidase: a potential therapeutic target for parasitic and viral infections.Expert opinion on therapeutic targets · 2022Review
- The Nuclear Translocation of Heme Oxygenase-1 in Human Diseases.Frontiers in cell and developmental biology · 2022Review
- Ganglioside GD2 Enhances the Malignant Phenotypes of Melanoma Cells by Cooperating with Integrins.International journal of molecular sciences · 2021Article
- Hepatitis C virus modulates signal peptide peptidase to alter host protein processing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Physiological functions of SPP/SPPL intramembrane proteases.Cellular and molecular life sciences : CMLS · 2020Review
- Bioinformatics Analysis of Domain 1 of HCV-Core Protein: Iran.International journal of peptide research and therapeutics · 2020Article
- USP15 Participates in Hepatitis C Virus Propagation through Regulation of Viral RNA Translation and Lipid Droplet Formation.Journal of virology · 2019Article
- Characterization of SPP inhibitors suppressing propagation of HCV and protozoa.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Polymorphisms in the hepatitis C virus core and its association with development of hepatocellular carcinoma.Journal of biosciences · 2017Review
- HCV core inhibits hepatocellular carcinoma cell replicative senescence through downregulating microRNA-138 expression.Journal of molecular medicine (Berlin, Germany) · 2017Article
- Insights into the mechanism of isoenzyme-specific signal peptide peptidase-mediated translocation of heme oxygenase.PloS one · 2017Article
- Role of cleavage at the core-E1 junction of hepatitis C virus polyprotein in viral morphogenesis.PloS one · 2017Article
- TRC8-dependent degradation of hepatitis C virus immature core protein regulates viral propagation and pathogenesis.Nature communications · 2016Article
- Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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 Ala(191) 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 Phe(177) by mass spectrometry. Mutations introduced into two residues (Ile(176) and Phe(177)) 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.