ArticleJournal of biomedical science2006
Hepatitis C virus NS4A inhibits cap-dependent and the viral IRES-mediated translation through interacting with eukaryotic elongation factor 1A.
Article in Journal of biomedical science, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- The SARS-CoV-2 targeted human RNA binding proteins network biology to investigate COVID-19 associated manifestations.International journal of biological macromolecules · 2022Article
- Non-canonical initiation factors modulate repeat-associated non-AUG translation.Human molecular genetics · 2022Article
- Chicken eEF1α is a Critical Factor for the Polymerase Complex Activity of Very Virulent Infectious Bursal Disease Virus.Viruses · 2020Article
- Structures and Functions of the 3' Untranslated Regions of Positive-Sense Single-Stranded RNA Viruses Infecting Humans and Animals.Frontiers in cellular and infection microbiology · 2020Review
- Hepatitis C Virus NS3 Protein Plays a Dual Role in WRN-Mediated Repair of Nonhomologous End Joining.Journal of virology · 2019Article
- G-Quadruplex in the NRF2 mRNA 5' Untranslated Region Regulates De Novo NRF2 Protein Translation under Oxidative Stress.Molecular and cellular biology · 2017Article
- eEF1A Interacts with the NS5A Protein and Inhibits the Growth of Classical Swine Fever Virus.Viruses · 2015Article
- Host proteins associated with Hepatitis C virus encoded NS4A.Virusdisease · 2014Article
- Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain.Journal of virology · 2014Article
- The eukaryotic elongation factor 1A is critical for genome replication of the paramyxovirus respiratory syncytial virus.PloS one · 2014Article
- ACH-806, an NS4A antagonist, inhibits hepatitis C virus replication by altering the composition of viral replication complexes.Antimicrobial agents and chemotherapy · 2013Article
- Identification of cis-acting nucleotides and a structural feature in West Nile virus 3'-terminus RNA that facilitate viral minus strand RNA synthesis.Journal of virology · 2013Article
- The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis.Microbiology and molecular biology reviews : MMBR · 2013Review
- Phylogenetic and structural analysis of HCV nonstructural protein 4A from Pakistani patients.Virus genes · 2012Article
- Mass spectrometry based proteomic studies on viruses and hosts--a review.Analytica chimica acta · 2011Review
- The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly.Journal of virology · 2011Article
- Translation elongation factor 1A facilitates the assembly of the tombusvirus replicase and stimulates minus-strand synthesis.PLoS pathogens · 2010Article
- Global genomics and proteomics approaches to identify host factors as targets to induce resistance against Tomato bushy stunt virus.Advances in virus research · 2010Review
- Refractoriness of hepatitis C virus internal ribosome entry site to processing by Dicer in vivo.Journal of negative results in biomedicine · 2009Article
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Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genomic RNA of hepatitis C virus (HCV) encodes the viral polyprotein precursor that undergoes proteolytic cleavage into structural and nonstructural proteins by cellular and the viral NS3 and NS2-3 proteases. Nonstructural protein 4A (NS4A) is a cofactor of the NS3 serine protease and has been demonstrated to inhibit protein synthesis. In this study, GST pull-down assay was performed to examine potential cellular factors that interact with the NS4A protein and are involved in the pathogenesis of HCV. A trypsin digestion followed by LC-MS/MS analysis revealed that one of the GST-NS4A-interacting proteins to be eukaryotic elongation factor 1A (eEF1A). Both the N-terminal domain of NS4A from amino acid residues 1-20, and the central domain from residues 21-34 interacted with eEF1A, but the central domain was the key player involved in the NS4A-mediated translation inhibition. NS4A(21-34) diminished both cap-dependent and HCV IRES-mediated translation in a dose-dependent manner. The translation inhibitory effect of NS4A(21-34) was relieved by the addition of purified recombinant eEF1A in an in vitro translation system. Taken together, NS4A inhibits host and viral translation through interacting with eEF1A, implying a possible mechanism by which NS4A is involved in the pathogenesis and chronic infection of HCV.
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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.