ArticlePLoS pathogens2009
Dynamics of HIV-1 assembly and release.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 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.
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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
131 citing papers in PubMed, 207 citations in OpenAlex.
- Real-Time Imaging of HIV-1 Protease Activation and Substrate Cleavage in Single Virions Assembling on the Plasma Membrane.Viruses · 2026Article
- Smart event-triggered MINFLUX microscopy to catch and follow rare events.Nature communications · 2026Article
- The biased adenosine-rich content of the HIV-1 genome serves as a molecular signature that facilitates efficient packaging.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Lenacapavir prevents production of infectious HIV-1 by abrogating immature virus assembly.bioRxiv : the preprint server for biology · 2026Article
- Evolution of split-protein technologies in virology: From mechanistic discovery and diagnostics to therapeutic promise.Journal of virus eradication · 2025Review
- 3D localization of retrovirus assembly in the presence of structured background with deep learning.Biophysical journal · 2025Article
- Integrated Antigenic and Nucleic Acid Detection in Single Virions and Extracellular Vesicles with Viral Content.Advanced healthcare materials · 2025Article
- Article
- Probing Gag-Env dynamics at HIV-1 assembly sites using live-cell microscopy.Journal of virology · 2024Article
- Studying Retroviral Life Cycles Using Visible Viruses and Live Cell Imaging.Annual review of virology · 2024Review
- Roles of RNA scaffolding in nanoscale Gag multimerization and selective protein sorting at HIV membranes.Science advances · 2024Article
- Visualizing HIV-1 Assembly at the T-Cell Plasma Membrane Using Single-Molecule Localization Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Virus tracking technologies and their applications in viral life cycle: research advances and future perspectives.Frontiers in immunology · 2023Review
- Analysis of individual HIV-1 budding event using fast AFM reveals a multiplexed role for VPS4.Biophysical journal · 2022Article
- Viro-fluidics: Real-time analysis of virus production kinetics at the single-cell level.Biophysical reports · 2022Article
- Specific Interaction of DARPin with HIV-1 CAViruses · 2022Article
- Review
- Review
- Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking.Viruses · 2022Article
71 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly and release of human immunodeficiency virus (HIV) occur at the plasma membrane of infected cells and are driven by the Gag polyprotein. Previous studies analyzed viral morphogenesis using biochemical methods and static images, while dynamic and kinetic information has been lacking until very recently. Using a combination of wide-field and total internal reflection fluorescence microscopy, we have investigated the assembly and release of fluorescently labeled HIV-1 at the plasma membrane of living cells with high time resolution. Gag assembled into discrete clusters corresponding to single virions. Formation of multiple particles from the same site was rarely observed. Using a photoconvertible fluorescent protein fused to Gag, we determined that assembly was nucleated preferentially by Gag molecules that had recently attached to the plasma membrane or arrived directly from the cytosol. Both membrane-bound and cytosol derived Gag polyproteins contributed to the growing bud. After their initial appearance, assembly sites accumulated at the plasma membrane of individual cells over 1-2 hours. Assembly kinetics were rapid: the number of Gag molecules at a budding site increased, following a saturating exponential with a rate constant of approximately 5 x 10(-3) s(-1), corresponding to 8-9 min for 90% completion of assembly for a single virion. Release of extracellular particles was observed at approximately 1,500+/-700 s after the onset of assembly. The ability of the virus to recruit components of the cellular ESCRT machinery or to undergo proteolytic maturation, or the absence of Vpu did not significantly alter the assembly kinetics.
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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.