ArticleProceedings of the National Academy of Sciences of the United States of America1999
A mimic of HIV-1 nucleocapsid protein impairs reverse transcription and displays antiviral activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 41 citations in OpenAlex.
- Identification of Novel Nucleocapsid Chimeric Proteins Inhibiting HIV-1 Replication.International journal of molecular sciences · 2022Article
- Current Peptide and Protein Candidates Challenging HIV Therapy beyond the Vaccine Era.Viruses · 2017Review
- HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Current topics in medicinal chemistry · 2016Review
- Nucleocapsid Annealing-Mediated Electrophoresis (NAME) assay allows the rapid identification of HIV-1 nucleocapsid inhibitors.Journal of visualized experiments : JoVE · 2015Article
- Advances in targeting nucleocapsid-nucleic acid interactions in HIV-1 therapy.Virus research · 2014Review
- Retrospective on the all-in-one retroviral nucleocapsid protein.Virus research · 2014Review
- Article
- Identification of HIV-1 inhibitors targeting the nucleocapsid protein.Journal of medicinal chemistry · 2012Article
- The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication.Journal of virology · 2012Article
- Nucleocapsid protein annealing of a primer-template enhances (+)-strand DNA synthesis and fidelity by HIV-1 reverse transcriptase.Journal of molecular biology · 2012Article
- Phages and HIV-1: from display to interplay.International journal of molecular sciences · 2012Review
- Beyond plasma membrane targeting: role of the MA domain of Gag in retroviral genome encapsidation.Journal of molecular biology · 2011Review
- Nucleocapsid protein function in early infection processes.Virus research · 2008Review
- New pandemics: HIV and AIDS, HCV and chronic hepatitis, influenza virus and flu.Retrovirology · 2007Article
- Structure of the zinc finger domain encompassing residues 13-51 of the nucleocapsid protein from simian immunodeficiency virus.The Biochemical journal · 2006Article
- Inhibitory effects of archetypical nucleic acid ligands on the interactions of HIV-1 nucleocapsid protein with elements of Psi-RNA.Nucleic acids research · 2006Article
- Equine infectious anemia virus Gag p9 function in early steps of virus infection and provirus production.Journal of virology · 2005Article
- Molecular mechanisms of HIV-1 associated neurodegeneration.Journal of biosciences · 2005Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Combined inhibition of HIV-1 reverse transcriptase and protease has significantly improved the treatment of AIDS. Nevertheless, resistance to these drugs occurs rapidly because of viral mutations, emphasizing the importance of identifying novel retroviral targets to develop new drug combinations. The critical role played by the nucleocapsid protein NCp7 of HIV-1 at different steps of the retrovirus life cycle makes it an attractive target for the development of new antiviral agents. NCp7 contains two highly conserved zinc fingers and is characterized by a three-dimensional structure that cannot be modified without a complete loss of infectivity of mutated viruses. Based on these structural data, we report that RB 2121, a cyclic peptide designed to mimic several essential biological determinants of NCp7, displays antiviral activity by inhibiting HIV-1 replication in CEM-4 cells infected by HIV-1. In vitro, RB 2121 does not interfere with HIV-1 cell entry and viral enzymes but is able to inhibit the annealing activities of NCp7 by recognizing nucleic acids. Analysis of proviral DNA synthesis by means of PCR has shown that RB 2121 acts at an early step of the retrovirus life cycle by inducing a dose-dependent reduction in transcribed DNA levels through inhibition of NCp7-reverse transcriptase interaction. Because of its original mechanism of action, RB 2121 provides an interesting lead for the rational development of new anti-HIV-1 agents that could be associated advantageously with enzyme inhibitors to counteract rapid virus mutations and resistance problems observed in tritherapies.
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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.