ArticleBiophysical journal2013
Identification of pauses during formation of HIV-1 virus like particles.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
- Lenacapavir prevents production of infectious HIV-1 by abrogating immature virus assembly.bioRxiv : the preprint server for biology · 2026Article
- 3D localization of retrovirus assembly in the presence of structured background with deep learning.Biophysical journal · 2025Article
- Article
- Review
- Tsg101/ESCRT-I recruitment regulated by the dual binding modes of K63-linked diubiquitin.Structure (London, England : 1993) · 2022Article
- Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53.eLife · 2021Article
- Application of Advanced Light Microscopy to the Study of HIV and Its Interactions with the Host.Viruses · 2021Review
- Article
- Rapid formation of human immunodeficiency virus-like particles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- High-speed imaging of ESCRT recruitment and dynamics during HIV virus like particle budding.PloS one · 2020Article
- Calibrating Evanescent-Wave Penetration Depths for Biological TIRF Microscopy.Biophysical journal · 2019Review
- VLPs Derived from the CCMV Plant Virus Can Directly Transfect and Deliver Heterologous Genes for Translation into Mammalian Cells.BioMed research international · 2019Article
- Correlative iPALM and SEM resolves virus cavity and Gag lattice defects in HIV virions.European biophysics journal : EBJ · 2019Article
- Single molecule localisation microscopy reveals how HIV-1 Gag proteins sense membrane virus assembly sites in living host CD4 T cells.Scientific reports · 2018Article
- Article
- Immature HIV-1 lattice assembly dynamics are regulated by scaffolding from nucleic acid and the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Subcellular Localization of HIV-1Journal of virology · 2017Article
- Imaging HIV-1 RNA dimerization in cells by multicolor super-resolution and fluctuation microscopies.Nucleic acids research · 2016Article
- Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.Journal of biomolecular NMR · 2016Article
- HIV-1 RNA genome dimerizes on the plasma membrane in the presence of Gag protein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HIV Gag polymerizes on the plasma membrane to form virus like particles (VLPs) that have similar diameters to wild-type viruses. We use multicolor, dual-penetration depth, total internal reflection fluorescence microscopy, which corrects for azimuthal movement, to image the assembly of individual VLPs from the time of nucleation to the recruitment of VPS4 (a component of the endosomal sorting complexes required for transport, and which marks the final stage of VLP assembly). Using a mathematical model for assembly and maximum-likelihood comparison of fits both with and without pauses, we detect pauses during Gag polymerization in 60% of VLPs. Pauses range from 2 to 20 min, with an exponentially distributed duration that is independent of cytosolic Gag concentration. VLPs assembled with late domain mutants of Gag (which do not recruit the key endosomal sorting complexes required for transport proteins Alix or TSG101) exhibit similar pause distributions. These pauses indicate that a single rate-limiting event is required for continuation of assembly. We suggest that pauses are either related to incorporation of defects in the hexagonal Gag lattice during VLP assembly or are caused by shortcomings in interactions of Gag with essential and still undefined cellular components during formation of curvature on the plasma membrane.
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