ArticleJournal of virology2018
PF74 Reinforces the HIV-1 Capsid To Impair Reverse Transcription-Induced Uncoating.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed.
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- BRCA1-RAD51 homologous DNA repair pathway promotes HIV-1 reverse transcription.Science advances · 2026Article
- Article
- 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
- Super-Resolution Imaging of Nuclear Pore Responses to Mechanical Stress and Energy Depletion.Viruses · 2026Article
- Lenacapavir-induced capsid damage uncovers HIV-1 genomes emanating from nuclear speckles.The EMBO journal · 2026Article
- Structural, biophysical, and virological mechanistic characterization of HIV-1 capsid-targeting antivirals.bioRxiv : the preprint server for biology · 2025Article
- Lenacapavir-induced Lattice Hyperstabilization is Central to HIV-1 Capsid Failure at the Nuclear Pore Complex and in the Cytoplasm.bioRxiv : the preprint server for biology · 2025Article
- Time-Resolved Fluorescence Imaging and Correlative Cryo-Electron Tomography to Study Structural Changes of the HIV-1 Capsid.ACS nano · 2025Article
- Reverse transcription progression and genome length regulate HIV-1 core elasticity and disassembly.PLoS pathogens · 2025Article
- The identification of a novel interaction site for the human immunodeficiency virus capsid on nucleoporin 153.The Journal of general virology · 2025Article
- HIV-1 cell-to-cell infection of macrophages escapes type I interferon and host restriction factors, and is resistant to antiretroviral drugs.PLoS pathogens · 2025Article
- IP6, PF74 affect HIV-1 capsid stability through modulation of hexamer-hexamer tilt angle preference.Biophysical journal · 2025Article
- Quinazolinone-based Subchemotypes for Targeting HIV-1 Capsid Protein: Design and Synthesis.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2024Article
- State of the ART (antiretroviral therapy): Long-acting HIV-1 therapeutics.Global health & medicine · 2024Review
- Elasticity of the HIV-1 core facilitates nuclear entry and infection.PLoS pathogens · 2024Article
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Design and Synthesis of New GS-6207 Subtypes for Targeting HIV-1 Capsid Protein.International journal of molecular sciences · 2024Article
- Article
- HIV-1 Capsid Uncoating Is a Multistep Process That Proceeds through Defect Formation Followed by Disassembly of the Capsid Lattice.ACS nano · 2024Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
The RNA genome of human immunodeficiency virus type 1 (HIV-1) is enclosed in a cone-shaped capsid shell that disassembles following cell entry via a process known as uncoating. During HIV-1 infection, the capsid is important for reverse transcription and entry of the virus into the target cell nucleus. The small molecule PF74 inhibits HIV-1 infection at early stages by binding to the capsid and perturbing uncoating. However, the mechanism by which PF74 alters capsid stability and reduces viral infection is presently unknown. Here, we show, using atomic force microscopy (AFM), that binding of PF74 to recombinant capsid-like assemblies and to HIV-1 isolated cores stabilizes the capsid in a concentration-dependent manner. At a PF74 concentration of 10 μM, the mechanical stability of the core is increased to a level similar to that of the intrinsically hyperstable capsid mutant E45A. PF74 also prevented the complete disassembly of HIV-1 cores normally observed during 24 h of reverse transcription. Specifically, cores treated with PF74 only partially disassembled: the main body of the capsid remained intact and stiff, and a cap-like structure dissociated from the narrow end of the core. Moreover, the internal coiled structure that was observed to form during reverse transcription
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