ArticleRetrovirology2016
HIV-1 capsid is involved in post-nuclear entry steps.
Article in Retrovirology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
45 citing papers in PubMed, 65 citations in OpenAlex.
- Capsid stabilization reprograms the nuclear fate of the HIV genome.Science advances · 2026Article
- Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with nuclear speckles.eLife · 2026Article
- Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with the nuclear speckle.bioRxiv : the preprint server for biology · 2025Article
- Understanding the HIV-CA protein and the ligands that bind at the N-terminal domain (NTD) - C-terminal domain (CTD) interface.RSC medicinal chemistry · 2025Review
- RNA-binding protein PTENα blocks RIG-I activation to prevent viral inflammation.Nature chemical biology · 2024Article
- The capsid revolution.Journal of molecular cell biology · 2024Review
- HIV-1 capsid and viral DNA integration.mBio · 2024Review
- Design, synthesis, and mechanistic study of 2-piperazineone-bearing peptidomimetics as novel HIV capsid modulators.RSC medicinal chemistry · 2023Article
- Design, Synthesis and Structure-Activity Relationships of Phenylalanine-Containing Peptidomimetics as Novel HIV-1 Capsid Binders Based on Ugi Four-Component Reaction.Molecules (Basel, Switzerland) · 2022Article
- Three-dimensional insights into human enveloped viruses in vitro and in situ.Biochemical Society transactions · 2022Review
- Structure and function of retroviral integrase.Nature reviews. Microbiology · 2022Review
- Rotten to the core: antivirals targeting the HIV-1 capsid core.Retrovirology · 2021Review
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- Dynactin 1 negatively regulates HIV-1 infection by sequestering the host cofactor CLIP170.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Design, synthesis, and antiviral activity of phenylalanine derivatives as HIV-1 capsid inhibitors.Bioorganic & medicinal chemistry · 2021Article
- HIV-1 capsid exploitation of the host microtubule cytoskeleton during early infection.Retrovirology · 2021Review
- Review
- The Role of Capsid in the Early Steps of HIV-1 Infection: New Insights into the Core of the Matter.Viruses · 2021Review
- HIV-1 uncoating by release of viral cDNA from capsid-like structures in the nucleus of infected cells.eLife · 2021Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
Abstract
backgroundHIV-1 capsid influences viral uncoating and nuclear import. Some capsid is detected in the nucleus but it is unclear if it has any function. We reported that the antibiotic Coumermycin-A1 (C-A1) inhibits HIV-1 integration and that a capsid mutation confers resistance to C-A1, suggesting that capsid might affect post-nuclear entry steps.
resultsHere we report that C-A1 inhibits HIV-1 integration in a capsid-dependent way. Using molecular docking, we identify an extended binding pocket delimited by two adjacent capsid monomers where C-A1 is predicted to bind. Isothermal titration calorimetry confirmed that C-A1 binds to hexameric capsid. Cyclosporine washout assays in Jurkat CD4+ T cells expressing engineered human TRIMCyp showed that C-A1 causes faster and greater escape from TRIMCyp restriction. Sub-cellular fractionation showed that small amounts of capsid accumulated in the nuclei of infected cells and C-A1 reduced the nuclear capsid. A105S and N74D capsid mutant viruses did not accumulate capsid in the nucleus, irrespective of C-A1 treatment. Depletion of Nup153, a nucleoporin located at the nuclear side of the nuclear pore that binds to HIV-1 capsid, made the virus less susceptible to TRIMCyp restriction, suggesting that Nup153 may help maintain some integrity of the viral core in the nucleus. Furthermore C-A1 increased binding of CPSF6, a nuclear protein, to capsid.
conclusionsOur results indicate that capsid is involved in post-nuclear entry steps preceding integration.
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What OpenQuestion holds
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.