ArticleBiochemistry2005
Combinatorial selection, inhibition, and antiviral activity of DNA thioaptamers targeting the RNase H domain of HIV-1 reverse transcriptase.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 53 citations in OpenAlex.
- Aptamers as promising nanotheranostic tools in the COVID-19 pandemic era.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022Review
- Aptamers: An Emerging Tool for Diagnosis and Therapeutics in Tuberculosis.Frontiers in cellular and infection microbiology · 2021Review
- Aptamers against Immunoglobulins: Design, Selection and Bioanalytical Applications.International journal of molecular sciences · 2020Review
- Aptamers Chemistry: Chemical Modifications and Conjugation Strategies.Molecules (Basel, Switzerland) · 2019Review
- Selection of 2'-Deoxy-2'-Fluoroarabino Nucleic Acid (FANA) Aptamers That Bind HIV-1 Integrase with Picomolar Affinity.ACS chemical biology · 2019Article
- Molecular Application of Aptamers in the Diagnosis and Treatment of Cancer and Communicable Diseases.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Oligonucleotide aptamers: promising and powerful diagnostic and therapeutic tools for infectious diseases.The Journal of infection · 2018Review
- Development of Phosphorothioate DNA and DNA Thioaptamers.Biomedicines · 2017Review
- Selection of 2'-deoxy-2'-fluoroarabinonucleotide (FANA) aptamers that bind HIV-1 reverse transcriptase with picomolar affinity.Nucleic acids research · 2015Article
- Generation of Aptamers with an Expanded Chemical Repertoire.Molecules (Basel, Switzerland) · 2015Review
- Selection of a novel DNA thioaptamer against HER2 structure.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2015Article
- High-affinity RNA Aptamers Against the HIV-1 Protease Inhibit Both In Vitro Protease Activity and Late Events of Viral Replication.Molecular therapy. Nucleic acids · 2015Article
- Review
- Aptamer-based therapeutics: new approaches to combat human viral diseases.Pharmaceuticals (Basel, Switzerland) · 2013Article
- High-throughput sequence analysis reveals structural diversity and improved potency among RNA inhibitors of HIV reverse transcriptase.Nucleic acids research · 2013Article
- Aptamers and the next generation of diagnostic reagents.Proteomics. Clinical applications · 2012Review
- Article
- Article
- Broad-spectrum aptamer inhibitors of HIV reverse transcriptase closely mimic natural substrates.Nucleic acids research · 2011Article
- Strategies for the discovery of therapeutic aptamers.Expert opinion on drug discovery · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Despite the key role played by the RNase H of human immunodeficiency virus-1 reverse transcriptase (HIV-1 RT) in viral proliferation, only a few inhibitors of RNase H have been reported. Using in vitro combinatorial selection methods and the RNase H domain of the HIV RT, we have selected double-stranded DNA thioaptamers (aptamers with selected thiophosphate backbone substitutions) that inhibit RNase H activity and viral replication. The selected thioaptamer sequences had a very high proportion of G residues. The consensus sequence for the selected thioaptamers showed G clusters separated by single residues at the 5'-end of the sequence. Gel electrophoresis mobility shift assays and nuclear magnetic resonance spectroscopy showed that the selected thioaptamer binds to the isolated RNase H domain, but did not bind to a structurally similar RNase H from Escherichia coli. The lead thioaptamer, R12-2, showed specific binding to HIV-1 RT with a binding constant (K(d)) of 70 nM. The thioaptamer inhibited the RNase H activity of intact HIV-1 RT. In cell culture, transfection of thioaptamer R12-2 (0.5 microg/mL) markedly inhibited viral production and exhibited a dose response of inhibition with R12-2 concentrations ranging from 0.03 to 2.0 microg/mL (IC(50) < 100 nM). Inhibition was also seen across a wide range of virus inoculum, ranging from a multiplicity of infection (moi) of 0.0005 to 0.05, with a reduction of the level of virus production by more than 50% at high moi. Suppression of virus was comparable to that seen with AZT when moi <or= 0.005.
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Registered trials
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.