ArticleRNA biology2015
Local RNA flexibility perturbation of the IRES element induced by a novel ligand inhibits viral RNA translation.
Article in RNA biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Decoding the Structural Complexity of Viral RNAs with SHAPE to Guide Antiviral Therapeutics.Viruses · 2026Review
- Article
- Ins and outs of IRES elements: function and significance.Biochemical Society transactions · 2025Review
- Small Molecules Targeting Viral RNA.International journal of molecular sciences · 2023Review
- Pharmacophore-Based Discovery of Viral RNA Conformational Modulators.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Picornavirus translation strategies.FEBS open bio · 2022Review
- Conserved RNA secondary structure in Cherry virus A 5'-UTR associated with translation regulation.Virology journal · 2022Article
- Translation of Plant RNA Viruses.Viruses · 2021Review
- Amilorides inhibit SARS-CoV-2 replication in vitro by targeting RNA structures.Science advances · 2021Article
- Amilorides inhibit SARS-CoV-2 replication in vitro by targeting RNA structures.bioRxiv : the preprint server for biology · 2020Article
- IRES-targeting small molecule inhibits enterovirus 71 replication via allosteric stabilization of a ternary complex.Nature communications · 2020Article
- RNA-protein coevolution study of Gemin5 uncovers the role of the PXSS motif of RBS1 domain for RNA binding.RNA biology · 2020Article
- A unique internal ribosome entry site representing a dynamic equilibrium state of RNA tertiary structure in the 5'-UTR of Wheat yellow mosaic virus RNA1.Nucleic acids research · 2020Article
- Understanding the Contributions of Conformational Changes, Thermodynamics, and Kinetics of RNA-Small Molecule Interactions.ACS chemical biology · 2019Review
- Deconstructing internal ribosome entry site elements: an update of structural motifs and functional divergences.Open biology · 2018Review
- In-cell SHAPE uncovers dynamic interactions between the untranslated regions of the foot-and-mouth disease virus RNA.Nucleic acids research · 2017Article
- Insights into Structural and Mechanistic Features of Viral IRES Elements.Frontiers in microbiology · 2017Review
- RNAiFold2T: Constraint Programming design of thermo-IRES switches.Bioinformatics (Oxford, England) · 2016Article
- Designing synthetic RNAs to determine the relevance of structural motifs in picornavirus IRES elements.Scientific reports · 2016Article
- Fingerprinting the junctions of RNA structure by an open-paddlewheel diruthenium compound.RNA (New York, N.Y.) · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The internal ribosome entry site (IRES) element located at the 5'untranslated genomic region of various RNA viruses mediates cap-independent initiation of translation. Picornavirus IRES activity is highly dependent on both its structural organization and its interaction with host factors. Small molecules able to interfere with RNA function are valuable candidates for antiviral agents. Here we show that a small molecule based on benzimidazole (IRAB) inhibited foot-and-mouth disease virus (FMDV) IRES-dependent protein synthesis in cells transfected with infectious RNA leading to a decrease of the virus titer, which was higher than that induced by a structurally related benzimidazole derivative. Interestingly, IRAB preferentially inhibited IRES-dependent translation in cell free systems in a dose-dependent manner. RNA structural analysis by SHAPE demonstrated an increased local flexibility of the IRES structure upon incubation with IRAB, which affected 3 stem-loops (SL) of domain 3. Fluorescence binding assays conducted with individual aminopurine-labeled oligoribonucleotides indicated that the SL3A binds IRAB (EC50 18 μM). Taken together, the results derived from SHAPE reactivity and fluorescence binding assays suggested that the target site of IRAB within the FMDV IRES might be a folded RNA structure that involves the entire apical region of domain 3. Our data suggest that the conformational changes induced by this compound on a specific region of the IRES structure which is essential for its activity is, at least in part, responsible for the reduced IRES efficiency observed in cell free lysates and, particularly, in RNA-transfected cells.
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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.