ArticleJournal of virology2012
Functional redundancy in HIV-1 viral particle assembly.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
24 citing papers in PubMed, 29 citations in OpenAlex.
- Initiation of HIV-1 Gag lattice assembly is required for recognition of the viral genome packaging signal.eLife · 2023Article
- Review
- Across the Hall from Pioneers.Viruses · 2021Article
- Review
- Article
- Critical Role of the Human T-Cell Leukemia Virus Type 1 Capsid N-Terminal Domain for Gag-Gag Interactions and Virus Particle Assembly.Journal of virology · 2018Article
- Perturbation of Human T-Cell Leukemia Virus Type 1 Particle Morphology by Differential Gag Co-Packaging.Viruses · 2017Article
- Disparate Contributions of Human Retrovirus Capsid Subdomains to Gag-Gag Oligomerization, Virus Morphology, and Particle Biogenesis.Journal of virology · 2017Article
- Functional Equivalence of Retroviral MA Domains in Facilitating Psi RNA Binding Specificity by Gag.Viruses · 2016Article
- Coadministration of a Plasmid Encoding HIV-1 Gag Enhances the Efficacy of Cancer DNA Vaccines.Molecular therapy : the journal of the American Society of Gene Therapy · 2016Article
- The Host RNAs in Retroviral Particles.Viruses · 2016Review
- Analysis of the human immunodeficiency virus-1 RNA packageome.RNA (New York, N.Y.) · 2016Article
- Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation.Journal of virology · 2016Article
- Review
- 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
- Molecular determinants of the ratio of inert to infectious virus particles.Progress in molecular biology and translational science · 2015Review
- Distinct nucleic acid interaction properties of HIV-1 nucleocapsid protein precursor NCp15 explain reduced viral infectivity.Nucleic acids research · 2014Article
- An immature retroviral RNA genome resembles a kinetically trapped intermediate state.Journal of virology · 2014Article
- HIV virions as nanoscopic test tubes for probing oligomerization of the integrase enzyme.ACS nano · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Expression of a retroviral Gag protein in mammalian cells leads to the assembly of virus particles. In vitro, recombinant Gag proteins are soluble but assemble into virus-like particles (VLPs) upon addition of nucleic acid. We have proposed that Gag undergoes a conformational change when it is at a high local concentration and that this change is an essential prerequisite for particle assembly; perhaps one way that this condition can be fulfilled is by the cooperative binding of Gag molecules to nucleic acid. We have now characterized the assembly in human cells of HIV-1 Gag molecules with a variety of defects, including (i) inability to bind to the plasma membrane, (ii) near-total inability of their capsid domains to engage in dimeric interaction, and (iii) drastically compromised ability to bind RNA. We find that Gag molecules with any one of these defects still retain some ability to assemble into roughly spherical objects with roughly correct radius of curvature. However, combination of any two of the defects completely destroys this capability. The results suggest that these three functions are somewhat redundant with respect to their contribution to particle assembly. We suggest that they are alternative mechanisms for the initial concentration of Gag molecules; under our experimental conditions, any two of the three is sufficient to lead to some semblance of correct assembly.
Indexed as
Identifiers
What OpenQuestion holds
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.