ArticlePLoS biology2020
Permeability of the HIV-1 capsid to metabolites modulates viral DNA synthesis.
Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 68 citations in OpenAlex.
- The Central Pore of HIV-1 Capsomers Promotes Sustained Stability of the Viral Capsid.Journal of molecular biology · 2026Article
- Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026Review
- Atomic resolution structure of human papillomavirus bound to heparin.Nature communications · 2026Article
- Atomistic characterization of the maturation mechanisms in the HIV-1 capsid domain.Nature communications · 2026Article
- Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure.bioRxiv : the preprint server for biology · 2026Article
- Role of viral protein ratio in the structure and separation of empty and full adeno-associated virus capsids: A molecular dynamics study.Molecular therapy. Advances · 2026Article
- Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1The journal of physical chemistry. B · 2026Article
- Lenacapavir-induced capsid damage uncovers HIV-1 genomes emanating from nuclear speckles.The EMBO journal · 2026Article
- Structural Basis for HIV-1 Maturation Inhibition by PF-46396 Determined by MAS NMR.Journal of the American Chemical Society · 2025Article
- Exploring the Structural Divergence of HIV and SRLV Lentiviral Capsids.Journal of the American Chemical Society · 2025Article
- Considerations for capsid-targeting antiretrovirals in pre-exposure prophylaxis.Trends in molecular medicine · 2025Review
- Structural basis for HIV-1 capsid adaption to a deficiency in IP6 packaging.Nature communications · 2025Article
- A novel aptamer-based dNTP assay reveals that intact HIV virions are highly stable and do not contain enough dNTPs to support DNA synthesis.Journal of virology · 2025Article
- Kinetic implications of IPScience advances · 2025Article
- Article
- IP6, PF74 affect HIV-1 capsid stability through modulation of hexamer-hexamer tilt angle preference.Biophysical journal · 2025Article
- HIV capsids: orchestrators of innate immune evasion, pathogenesis and pandemicity.The Journal of general virology · 2025Review
- HIV-1 adapts to lost IP6 coordination through second-site mutations that restore conical capsid assembly.Nature communications · 2024Article
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Spatiotemporal binding of cyclophilin A and CPSF6 to capsid regulates HIV-1 nuclear entry and integration.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
Reverse transcription, an essential event in the HIV-1 life cycle, requires deoxynucleotide triphosphates (dNTPs) to fuel DNA synthesis, thus requiring penetration of dNTPs into the viral capsid. The central cavity of the capsid protein (CA) hexamer reveals itself as a plausible channel that allows the passage of dNTPs into assembled capsids. Nevertheless, the molecular mechanism of nucleotide import into the capsid remains unknown. Employing all-atom molecular dynamics (MD) simulations, we established that cooperative binding between nucleotides inside a CA hexamer cavity results in energetically favorable conditions for passive translocation of dNTPs into the HIV-1 capsid. Furthermore, binding of the host cell metabolite inositol hexakisphosphate (IP6) enhances dNTP import, while binding of synthesized molecules like benzenehexacarboxylic acid (BHC) inhibits it. The enhancing effect on reverse transcription by IP6 and the consequences of interactions between CA and nucleotides were corroborated using atomic force microscopy, transmission electron microscopy, and virological assays. Collectively, our results provide an atomistic description of the permeability of the HIV-1 capsid to small molecules and reveal a novel mechanism for the involvement of metabolites in HIV-1 capsid stabilization, nucleotide import, and reverse transcription.
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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.