ArticleJournal of virology2004
Calcium-dependent calpain proteases are implicated in processing of the hepatitis C virus NS5A protein.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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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
17 citing papers in PubMed.
- Article
- Calpain-2 protein influencesFrontiers in microbiology · 2023Article
- The Hepatitis C virus NS5A and core proteins exert antagonistic effects on HAMP gene expression: the hidden interplay with the MTF-1/MRE pathway.FEBS open bio · 2021Article
- Article
- Virus Control of Cell Metabolism for Replication and Evasion of Host Immune Responses.Frontiers in cellular and infection microbiology · 2019Review
- CD163Frontiers in microbiology · 2019Article
- Activities of Thrombin and Factor Xa Are Essential for Replication of Hepatitis E Virus and Are Possibly Implicated in ORF1 Polyprotein Processing.Journal of virology · 2018Article
- Cross-inhibition of pathogenic agents and the host proteins they exploit.Scientific reports · 2016Article
- Understanding the interaction determinants of CAPN1 inhibition by CAST4 from bovines using molecular modeling techniques.Molecules (Basel, Switzerland) · 2014Article
- Permeability changes of integrin-containing multivesicular structures triggered by picornavirus entry.PloS one · 2014Article
- Modulation of hepatitis C virus genome encapsidation by nonstructural protein 4B.Journal of virology · 2013Article
- Regulation of hepatitis C virus replication by nuclear translocation of nonstructural 5A protein and transcriptional activation of host genes.Journal of virology · 2013Article
- Viruses as modulators of mitochondrial functions.Advances in virology · 2013Review
- Caspase cleavage of viral proteins, another way for viruses to make the best of apoptosis.Cell death & disease · 2012Review
- HCV peptide (C5A), an amphipathic α-helical peptide of hepatitis virus C, is an activator of N-formyl peptide receptor in human phagocytes.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- Release of intracellular calcium stores facilitates coxsackievirus entry into polarized endothelial cells.PLoS pathogens · 2010Article
- Calpain 1 and 2 are required for RNA replication of echovirus 1.Journal of virology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nonstructural 5A (NS5A) protein of the hepatitis C virus (HCV) is a multifunctional phosphoprotein that is implicated in viral replication and HCV-mediated pathogenesis. We report here that the NS5A protein from the HCV genotype 1a is processed into shorter distinct forms when expressed in mammalian cells (Vero, HepG2, HuH-7, and WRL68) infected with an NS5A-expressing HSV-1-based amplicon vector or when transiently transfected with NS5A-expressing plasmids in the absence of exogenous apoptotic stimuli. Inhibitor studies combined with cell-free cleavage assays suggest that calcium-dependent calpain proteases, in addition to caspase-like proteases, are involved in NS5A processing. Interestingly, His-tagging experiments indicated that all the detectable NS5A-cleaved products are N-terminal forms of the protein. Additionally, immunofluorescence studies showed that, despite proteolytic cleavage, the NS5A protein exhibits a cytoplasm-perinuclear localization similar to that of the full-length protein. Thus, our results are consistent with recent data that demonstrated that NS5A is capable of perturbing intracellular calcium homeostasis and suggest that NS5A is both an inducer and a substrate of the calcium-dependent calpain protease(s). This may imply that cleavage of NS5A by calpain(s) could play a role in the modulation of NS5A function.
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