ArticleJournal of virology2005
Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assay.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 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
68 citing papers in PubMed, 88 citations in OpenAlex.
- The role of HIV-1 Gag and genomic RNA interactions in virion assembly.Frontiers in microbiology · 2025Article
- Neutral sphingomyelinase 2 is required for HIV-1 maturation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Review
- Immature HIV-1 assembles from Gag dimers leaving partial hexamers at lattice edges as potential substrates for proteolytic maturation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Inhibition of retroviral Gag assembly by non-silencing miRNAs promotes autophagic viral degradation.Protein & cell · 2018Article
- Formation of RNA Granule-Derived Capsid Assembly Intermediates Appears To Be Conserved between Human Immunodeficiency Virus Type 1 and the Nonprimate Lentivirus Feline Immunodeficiency Virus.Journal of virology · 2018Article
- Identifying the assembly intermediate in which Gag first associates with unspliced HIV-1 RNA suggests a novel model for HIV-1 RNA packaging.PLoS pathogens · 2018Article
- Unraveling the role of membrane microdomains during microbial infections.Cell biology and toxicology · 2017Review
- Molecular mechanisms by which HERV-K Gag interferes with HIV-1 Gag assembly and particle infectivity.Retrovirology · 2017Article
- Analysis of HIV-1 Gag-RNA Interactions in Cells and Virions by CLIP-seq.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and Dependent on the Spacer Peptide Assembly Domain.Journal of virology · 2015Article
- How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Virus research · 2014Review
- Article
- A temporospatial map that defines specific steps at which critical surfaces in the Gag MA and CA domains act during immature HIV-1 capsid assembly in cells.Journal of virology · 2014Article
- Lipid domains in HIV-1 assembly.Frontiers in microbiology · 2014Review
- Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.Biophysical journal · 2013Article
- HIV-1 Gag associates with specific uropod-directed microdomains in a manner dependent on its MA highly basic region.Journal of virology · 2013Article
- Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells.Journal of virology · 2013Article
8 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
4 authors at 2 institutions in 1 country.
Funding
Abstract
Human immunodeficiency virus type 1 (HIV-1) particle production, a process driven by the Gag polyprotein precursor, occurs on the plasma membrane in most cell types. The plasma membrane contains cholesterol-enriched microdomains termed lipid rafts, which can be isolated as detergent-resistant membrane (DRM). Previously, we and others demonstrated that HIV-1 Gag is associated with DRM and that disruption of Gag-raft interactions impairs HIV-1 particle production. However, the determinants of Gag-raft association remain undefined. In this study, we developed a novel epitope-based Gag multimerization assay to examine whether Gag assembly is essential for its association with lipid rafts. We observed that membrane-associated, full-length Gag is poorly detected by immunoprecipitation relative to non-membrane-bound Gag. This poor detection is due to assembly-driven masking of Gag epitopes, as denaturation greatly improves immunoprecipitation. Gag mutants lacking the Gag-Gag interaction domain located in the N terminus of the nucleocapsid (NC) were efficiently immunoprecipitated without denaturation, indicating that the epitope masking is caused by higher-order Gag multimerization. We used this assay to examine the relationship between Gag assembly and Gag binding to total cellular membrane and DRM. Importantly, a multimerization-defective NC mutant displayed wild-type levels of membrane binding and DRM association, indicating that NC-mediated Gag multimerization is dispensable for association of Gag with membrane or DRM. We also demonstrate that different properties of sucrose and iodixanol membrane flotation gradients may explain some discrepancies regarding Gag-raft interactions. This report offers new insights into the association of HIV-1 Gag with membrane and with lipid rafts.
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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.