ArticleJournal of virology2001
Hepatitis C virus 3'X region interacts with human ribosomal proteins.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 75 citations in OpenAlex.
- Decoding the Structural Complexity of Viral RNAs with SHAPE to Guide Antiviral Therapeutics.Viruses · 2026Review
- Hepatitis C Virus 5'UTR Sequences That Bind eIF3 and Ribosomal 40S Subunits Confer Stimulation of Minus-Strand RNA Synthesis.International journal of molecular sciences · 2026Article
- Article
- Selective regulation in ribosome biogenesis and protein production for efficient viral translation.Archives of microbiology · 2021Review
- The Role of the RNA-RNA Interactome in the Hepatitis C Virus Life Cycle.International journal of molecular sciences · 2020Review
- Hallmarks of ribosomopathies.Nucleic acids research · 2020Review
- Ribosomal Protein L13 Promotes IRES-Driven Translation of Foot-and-Mouth Disease Virus in a Helicase DDX3-Dependent Manner.Journal of virology · 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
- RNA binding protein 24 regulates the translation and replication of hepatitis C virus.Protein & cell · 2018Article
- Form confers function: Case of the 3'X region of the hepatitis C virus genome.World journal of gastroenterology · 2018Review
- Making Bunyaviruses Talk: Interrogation Tactics to Identify Host Factors Required for Infection.Viruses · 2016Review
- Rpl22 is required for IME1 mRNA translation and meiotic induction in S. cerevisiae.Cell division · 2016Article
- Ribosomal proteins: functions beyond the ribosome.Journal of molecular cell biology · 2015Review
- Regulatory Roles of Rpl22 in Hematopoiesis: An Old Dog with New Tricks.Critical reviews in immunology · 2015Review
- Review
- Unmasking the information encoded as structural motifs of viral RNA genomes: a potential antiviral target.Reviews in medical virology · 2013Review
- Hepatitis C virus 3'UTR regulates viral translation through direct interactions with the host translation machinery.Nucleic acids research · 2013Article
- Systematic analysis of enhancer and critical cis-acting RNA elements in the protein-encoding region of the hepatitis C virus genome.Journal of virology · 2013Article
- Article
- Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteins.Nature communications · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To identify proteins that can bind the 3' untranslated region (UTR) of hepatitis C virus (HCV) we screened human cDNA libraries using the Saccharomyces cerevisiae three-hybrid system. Screening with an RNA sequence derived from the 3'-terminal 98 nucleotides (3'X region) of an infectious clone of HCV (H77c) yielded clones of human ribosomal proteins L22, L3, S3, and mL3, a mitochondrial homologue of L3. We performed preliminary characterization of the binding between the 3'X region and these proteins by a three-hybrid mating assay using mutant 3'X sequences. We have further characterized the interaction between 3'X and L22, since this protein is known to be associated with two small Epstein-Barr virus (EBV)-encoded RNA species (EBERs) which are abundantly produced in cells latently infected with EBV. The EBERs, which have similar predicted secondary structure to the HCV 3'X, assemble into ribonucleoprotein particles that include L22 and La protein. To confirm that L22 binds HCV 3'X we performed in vitro binding assays using recombinant L22 (expressed as a glutathione S-transferase [GST] fusion protein) together with a 3'X riboprobe. The 3'X region binds to the GST-L22 fusion protein (but not to GST alone), and this interaction is subject to competition with unlabeled 3'X RNA. To establish the functional role played by L22 in internal ribosome entry site (IRES)-mediated translation of HCV sequences we performed translational analysis in HuH-7 cells using monocistronic and bicistronic reporter constructs. The relative amount of core-chloramphenicol acetyltransferase reporter protein translated under the control of the HCV IRES was stimulated in the presence of L22 and La when these proteins were supplied in trans.
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