ArticleNucleic acids research2005
A hepatitis C virus (HCV) internal ribosome entry site (IRES) domain III-IV-targeted aptamer inhibits translation by binding to an apical loop of domain IIId.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- A sensitive and scalable fluorescence anisotropy single stranded RNA targeting approach for monitoring riboswitch conformational states.Nucleic acids research · 2024Article
- Aptamers for Anti-Viral Therapeutics and Diagnostics.International journal of molecular sciences · 2021Review
- An innovative protein expression system using RNA polymerase I for large-scale screening of high-nucleic-acid content Saccharomyces cerevisiae strains.Microbial biotechnology · 2020Article
- Oligonucleotide aptamers: promising and powerful diagnostic and therapeutic tools for infectious diseases.The Journal of infection · 2018Review
- Advancing viral RNA structure prediction: measuring the thermodynamics of pyrimidine-rich internal loops.RNA (New York, N.Y.) · 2017Article
- Oligonucleotide aptamers: potential novel molecules against viral hepatitis.Research in pharmaceutical sciences · 2017Review
- Use of Aptamers as Diagnostics Tools and Antiviral Agents for Human Viruses.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Pharmacokinetics of a Cholesterol-conjugated Aptamer Against the Hepatitis C Virus (HCV) NS5B Protein.Molecular therapy. Nucleic acids · 2015Article
- Trans-splicing group I intron targeting hepatitis C virus IRES mediates cell death upon viral infection in Huh7.5 cells.Virology · 2015Article
- Aptamers as a novel tool for diagnostics and therapy.Investigational new drugs · 2015Review
- Review
- Translation initiation of the HIV-1 mRNA.Translation (Austin, Tex.) · 2014Review
- Article
- Hepatitis C virus translation inhibitors targeting the internal ribosomal entry site.Journal of medicinal chemistry · 2014Review
- Article
- Prospects for nucleic acid-based therapeutics against hepatitis C virus.World journal of gastroenterology · 2013Review
- Aptamer-based therapeutics: new approaches to combat human viral diseases.Pharmaceuticals (Basel, Switzerland) · 2013Article
- Unmasking the information encoded as structural motifs of viral RNA genomes: a potential antiviral target.Reviews in medical virology · 2013Review
- Hepatitis C virus RNA: molecular switches mediated by long-range RNA-RNA interactions?Nucleic acids research · 2013Article
- Article
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6 authors.
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Abstract
The hepatitis C virus (HCV) has a positive single-stranded RNA genome, and translation starts within the internal ribosome entry site (IRES) in a cap-independent manner. The IRES is well conserved among HCV subtypes and has a unique structure consisting of four domains. We used an in vitro selection procedure to isolate RNA aptamers capable of binding to the IRES domains III-IV. The aptamers that were obtained shared the consensus sequence ACCCA, which is complementary to the apical loop of domain IIId that is known to be a critical region of IRES-dependent translation. This convergence suggests that domain IIId is preferentially selected in an RNA-RNA interaction. Mutation analysis showed that the aptamer binding was sequence and structure dependent. One of the aptamers inhibited translation both in vitro and in vivo. Our results indicate that domain IIId is a suitable target site for HCV blockage and that rationally designed RNA aptamers have great potential as anti-HCV drugs.
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