ArticleJournal of virology2006
Gag regulates association of human immunodeficiency virus type 1 envelope with detergent-resistant membranes.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Cholesterol in the Viral Membrane is a Molecular Switch Governing HIV-1 Env Clustering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Dual Pathways of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trafficking Modulate the Selective Exclusion of Uncleaved Oligomers from Virions.Journal of virology · 2021Article
- Review
- Quantification of phosphoinositides reveals strong enrichment of PIPScientific reports · 2019Article
- Distinct functions for the membrane-proximal ectodomain region (MPER) of HIV-1 gp41 in cell-free and cell-cell viral transmission and cell-cell fusion.The Journal of biological chemistry · 2018Article
- Localization to detergent-resistant membranes and HIV-1 core entry inhibition correlate with HIV-1 restriction by SERINC5.Virology · 2018Article
- In Vivo Analysis of Infectivity, Fusogenicity, and Incorporation of a Mutagenic Viral Glycoprotein Library Reveals Determinants for Virus Incorporation.Journal of virology · 2016Article
- Lipid rafts both in cellular membrane and viral envelope are critical for PRRSV efficient infection.Virology · 2015Article
- The cytoplasmic tail of retroviral envelope glycoproteins.Progress in molecular biology and translational science · 2015Review
- Interaction of pathogens with host cholesterol metabolism.Current opinion in lipidology · 2014Review
- Counteraction of the multifunctional restriction factor tetherin.Frontiers in microbiology · 2014Review
- The frantic play of the concealed HIV envelope cytoplasmic tail.Retrovirology · 2013Review
- Multiple Gag domains contribute to selective recruitment of murine leukemia virus (MLV) Env to MLV virions.Journal of virology · 2013Article
- Human Ubc9 is involved in intracellular HIV-1 Env stability after trafficking out of the trans-Golgi network in a Gag dependent manner.PloS one · 2013Article
- C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.The Journal of general virology · 2013Review
- Article
- A highly conserved residue in the C-terminal helix of HIV-1 matrix is required for envelope incorporation into virus particles.Journal of virology · 2012Article
- Dynamic Association between HIV-1 Gag and Membrane Domains.Molecular biology international · 2012Article
- Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane.Journal of virology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Assembly of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein on budding virus particles is important for efficient infection of target cells. In infected cells, lipid rafts have been proposed to form platforms for virus assembly and budding. Gag precursors partly associate with detergent-resistant membranes (DRMs) that are believed to represent lipid rafts. The cytoplasmic domain of the envelope gp41 usually carries palmitate groups that were also reported to confer DRM association. Gag precursors confer budding and carry envelope glycoproteins onto virions via specific Gag-envelope interactions. Thus, specific mutations in both the matrix domain of the Gag precursor and gp41 cytoplasmic domain abrogate envelope incorporation onto virions. Here, we show that HIV-1 envelope association with DRMs is directly influenced by its interaction with Gag. Thus, in the absence of Gag, envelope fails to associate with DRMs. A mutation in the p17 matrix (L30E) domain in Gag (Gag L30E) that abrogates envelope incorporation onto virions also eliminated envelope association with DRMs in 293T cells and in the T-cell line, MOLT 4. These observations are consistent with a requirement for an Env-Gag interaction for raft association and subsequent assembly onto virions. In addition to this observation, we found that mutations in the gp41 cytoplasmic domain that abrogated envelope incorporation onto virions and impaired infectivity of cell-free virus also eliminated envelope association with DRMs. On the basis of these observations, we propose that Gag-envelope interaction is essential for efficient envelope association with DRMs, which in turn is essential for envelope budding and assembly onto virus particles.
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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.