ArticleJournal of virology2002
Nucleic acid-independent retrovirus assembly can be driven by dimerization.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 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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Who cites it
69 citing papers in PubMed, 105 citations in OpenAlex.
- Molecular physiology of Arc/Arg3.1: The oligomeric state hypothesis of synaptic plasticity.Acta physiologica (Oxford, England) · 2022Review
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- Integrase-RNA interactions underscore the critical role of integrase in HIV-1 virion morphogenesis.eLife · 2020Article
- Removing the Polyanionic Cargo Requirement for Assembly of Alphavirus Core-Like Particles to Make an Empty Alphavirus Core.Viruses · 2020Article
- 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
- Length of encapsidated cargo impacts stability and structure of in vitro assembled alphavirus core-like particles.Journal of physics. Condensed matter : an Institute of Physics journal · 2017Article
- Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor.PloS one · 2017Article
- Dimerization of the SP1 Region of HIV-1 Gag Induces a Helical Conformation and Association into Helical Bundles: Implications for Particle Assembly.Journal of virology · 2016Article
- Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and Dependent on the Spacer Peptide Assembly Domain.Journal of virology · 2015Article
- RNA and Nucleocapsid Are Dispensable for Mature HIV-1 Capsid Assembly.Journal of virology · 2015Article
- A retrovirus packages nascent host noncoding RNAs from a novel surveillance pathway.Genes & development · 2015Article
- Simulations show that virus assembly and budding are facilitated by membrane microdomains.Biophysical journal · 2015Article
- The HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranes.Journal of virology · 2015Article
- How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Virus research · 2014Review
- A murine retrovirus co-Opts YB-1, a translational regulator and stress granule-associated protein, to facilitate virus assembly.Journal of virology · 2014Article
- Effect of multimerization on membrane association of Rous sarcoma virus and HIV-1 matrix domain proteins.Journal of virology · 2013Article
- Alterations in the MA and NC domains modulate phosphoinositide-dependent plasma membrane localization of the Rous sarcoma virus Gag protein.Journal of virology · 2013Article
- Elements in HIV-1 Gag contributing to virus particle assembly.Virus research · 2013Article
- Multiple Gag domains contribute to selective recruitment of murine leukemia virus (MLV) Env to MLV virions.Journal of virology · 2013Article
9 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 1 institution in 1 country.
Funding
Abstract
The Gag protein of retroviruses alone can polymerize into regular virus-like particles (VLPs) both in vitro and in vivo. In most circumstances the capsid (CA) and nucleocapsid (NC) domains of Gag as well as some form of nucleic acid are required for this process. The mechanism by which NC-nucleic acid interaction promotes assembly has remained obscure. We show here that while deletion of the NC domain of Rous sarcoma virus Gag abolishes formation and budding of VLPs at the plasma membranes of baculovirus-infected insect cells, replacement of NC with a dimer-forming leucine zipper domain restores budding of spherical particles morphologically similar to wild-type VLPs. The positioning of the dimerization domain appears to be critical for proper assembly, as the insertion of a 5-amino-acid flexible linker upstream of the zipper domain leads to budding of tubular rather than spherical particles. Similar tubular particles are formed when the same linker is inserted upstream of NC. The tubes are morphologically distinct from tubes formed when the p10 domain upstream of CA is deleted. The fact that a foreign dimerization domain can functionally mimic NC suggests that the role of nucleic acid in retroviral assembly is not to serve as a scaffold but rather to promote the formation of Gag dimers, which are critical intermediates in the polymerization of the Gag shell.
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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.