ArticleJournal of virology2013
Retrovirus restriction by TRIM5 proteins requires recognition of only a small fraction of viral capsid subunits.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Localization and functions of native and eGFP-tagged capsid proteins in HIV-1 particles.PLoS pathogens · 2022Article
- Review
- A lysine ring in HIV capsid pores coordinates IP6 to drive mature capsid assembly.PLoS pathogens · 2021Article
- Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019Review
- Do Human Endogenous Retroviruses Contribute to Multiple Sclerosis, and if So, How?Molecular neurobiology · 2019Review
- Article
- Allosteric HIV-1 Integrase Inhibitors Lead to Premature Degradation of the Viral RNA Genome and Integrase in Target Cells.Journal of virology · 2017Article
- Quantitative computational models of molecular self-assembly in systems biology.Physical biology · 2017Review
- Cyclophilin A potentiates TRIM5α inhibition of HIV-1 nuclear import without promoting TRIM5α binding to the viral capsid.PloS one · 2017Article
- HIV-1 capsid uncoating initiates after the first strand transfer of reverse transcription.Retrovirology · 2016Article
- Article
- HIV-1 capsid is involved in post-nuclear entry steps.Retrovirology · 2016Article
- Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.Nature communications · 2016Article
- Potent restriction of HIV-1 and SIVmac239 replication by African green monkey TRIM5α.Retrovirology · 2015Article
- Identification of capsid mutations that alter the rate of HIV-1 uncoating in infected cells.Journal of virology · 2015Article
- Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The host restriction factors TRIM5α and TRIMCyp potently inhibit retrovirus infection by binding to the incoming retrovirus capsid. TRIM5 proteins are dimeric, and their association with the viral capsid appears to be enhanced by avidity effects owing to formation of higher-order oligomeric complexes. We examined the stoichiometric requirement for TRIM5 functional recognition by quantifying the efficiencies of restriction of HIV-1 and murine leukemia virus (MLV) particles containing various proportions of restriction-sensitive and -insensitive CA subunits. Both TRIMCyp and TRIM5α inhibited infection of retrovirus particles containing as little as 25% of the restriction-sensitive CA protein. Accordingly, we also observed efficient binding of TRIMCyp in vitro to capsid assemblies containing as little as one-fourth wild-type CA protein. Paradoxically, the ability of HIV-1 particles to abrogate TRIMCyp restriction in trans was more strongly dependent on the fraction of wild-type CA than was restriction of infection. Collectively, our results indicate that TRIM5 restriction factors bind to retroviral capsids in a highly cooperative manner and suggest that TRIM5 can engage a capsid lattice containing a minimum of three or fewer recognizable subunits per hexamer. Our study supports a model in which localized binding of TRIM5 to the viral capsid nucleates rapid polymerization of a TRIM5 lattice on the capsid surface.
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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.