ArticleVirus research2013
Elements in HIV-1 Gag contributing to virus particle assembly.
Article in Virus research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Exploring the Structural Divergence of HIV and SRLV Lentiviral Capsids.Journal of the American Chemical Society · 2025Article
- Influence of HIV-1 Genomic RNA on the Formation of Gag Biomolecular Condensates.Journal of molecular biology · 2023Article
- Remodeling of the Plasma Membrane by Surface-Bound Protein Monomers and Oligomers: The Critical Role of Intrinsically Disordered Regions.The Journal of membrane biology · 2022Review
- NMR Studies of Retroviral Genome Packaging.Viruses · 2020Review
- Article
- Retroviral Gag protein-RNA interactions: Implications for specific genomic RNA packaging and virion assembly.Seminars in cell & developmental biology · 2019Review
- Article
- Perturbation of Human T-Cell Leukemia Virus Type 1 Particle Morphology by Differential Gag Co-Packaging.Viruses · 2017Article
- The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV.PLoS pathogens · 2017Article
- Functional Equivalence of Retroviral MA Domains in Facilitating Psi RNA Binding Specificity by Gag.Viruses · 2016Article
- HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Current topics in medicinal chemistry · 2016Review
- Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and Dependent on the Spacer Peptide Assembly Domain.Journal of virology · 2015Article
- Hydrodynamic and Membrane Binding Properties of Purified Rous Sarcoma Virus Gag Protein.Journal of virology · 2015Article
- Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers.The Journal of cell biology · 2015Article
- Atomic Modeling of an Immature Retroviral Lattice Using Molecular Dynamics and Mutagenesis.Structure (London, England : 1993) · 2015Article
- A novel minimal in vitro system for analyzing HIV-1 Gag-mediated budding.Journal of biological physics · 2015Article
- Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Membrane interaction of retroviral Gag proteins.Frontiers in microbiology · 2014Review
- 3D molecular models of whole HIV-1 virions generated with cellPACK.Faraday discussions · 2014Article
- Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages.Frontiers in microbiology · 2014Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The Gag polyprotein is the building block of retroviral particles and its expression is sufficient for assembly in cells. In HIV-1, nucleic acid (NA) is required for recombinant Gag molecules to assemble in a defined system in vitro. Experiments performed by Barklis and co-workers suggested that NA contributes to assembly by promoting Gag oligomerization. Gag is composed of four main domains: the matrix (MA), capsid (CA), nucleocapsid (NC), and p6 domains. We have recently shown that the SP1 linker, which lies between the CA and NC domains, assumes a helical structure at high, but not low, concentrations. We suggested that Gag oligomerization mediates assembly via an SP1-dependent conformational switch that exposes new interfaces for assembly. Although NA is required for assembly in vitro, deletion of NC, the main RNA-binding domain, does not eliminate particle formation in vivo; these particles lack NA. We hypothesized that alternative pathways that lead to Gag oligomerization or an increase in local Gag concentration, namely Gag-membrane or inter-protein interactions, rescue assembly in the absence of NC-RNA binding. We constructed mutants in which either Gag-membrane binding, the Gag dimer interface, or NC-RNA binding are disrupted. None of these mutants disables assembly. However, combined mutations in any two of these three classes render Gag completely unable to form virus-like particles. Thus, it seems, Gag utilizes at least three types of interactions to form oligomers and any two out of the three are sufficient for assembly.
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Registered trials
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