ArticleThe Journal of cell biology2008
Visualization of a proteasome-independent intermediate during restriction of HIV-1 by rhesus TRIM5alpha.
Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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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
111 citing papers in PubMed, 155 citations in OpenAlex.
- Primate TRIM34 is a broadly-acting, TRIM5-dependent lentiviral restriction factor.bioRxiv : the preprint server for biology · 2023Article
- Article
- Genetic Code Expansion and Bio-Orthogonal Labeling Reveal Intact HIV-1 Capsids inside the Nucleus.mBio · 2022Article
- Localization and functions of native and eGFP-tagged capsid proteins in HIV-1 particles.PLoS pathogens · 2022Article
- Article
- Teaching old dogmas new tricks: recent insights into the nuclear import of HIV-1.Current opinion in virology · 2022Review
- HIV-1 subverts the complement system in semen to enhance viral transmission.Mucosal immunology · 2021Article
- Editing of the TRIM5 Gene Decreases the Permissiveness of Human T Lymphocytic Cells to HIV-1.Viruses · 2020Article
- Correlated cryogenic fluorescence microscopy and electron cryo-tomography shows that exogenous TRIM5α can form hexagonal lattices or autophagy aggregates in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Restrictome of Flaviviruses.Virologica Sinica · 2020Review
- Duplication and divergence of the retrovirus restriction gene Fv1 in Mus caroli allows protection from multiple retroviruses.PLoS genetics · 2020Article
- Capsid-Labelled HIV To Investigate the Role of Capsid during Nuclear Import and Integration.Journal of virology · 2020Article
- TRIM5α self-assembly and compartmentalization of the HIV-1 viral capsid.Nature communications · 2020Article
- HIV-1 uncoats in the nucleus near sites of integration.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Ubiquitination and SUMOylation in HIV Infection: Friends and Foes.Current issues in molecular biology · 2020Review
- Hierarchical assembly governs TRIM5α recognition of HIV-1 and retroviral capsids.Science advances · 2019Article
- Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019Review
- K63-Linked Ubiquitin Is Required for Restriction of HIV-1 Reverse Transcription and Capsid Destabilization by Rhesus TRIM5α.Journal of virology · 2019Article
- Fluorescence Microscopy Assay to Measure HIV-1 Capsid Uncoating KineticsBio-protocol · 2019Article
- Defects in assembly explain reduced antiviral activity of the G249D polymorphism in human TRIM5α.PloS one · 2019Article
51 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
TRIM5 proteins constitute a class of restriction factors that prevent host cell infection by retroviruses from different species. TRIM5alpha restricts retroviral infection early after viral entry, before the generation of viral reverse transcription products. However, the underlying restriction mechanism remains unclear. In this study, we show that during rhesus macaque TRIM5alpha (rhTRIM5alpha)-mediated restriction of HIV-1 infection, cytoplasmic HIV-1 viral complexes can associate with concentrations of TRIM5alpha protein termed cytoplasmic bodies. We observe a dynamic interaction between rhTRIM5alpha and cytoplasmic HIV-1 viral complexes, including the de novo formation of rhTRIM5alpha cytoplasmic body-like structures around viral complexes. We observe that proteasome inhibition allows HIV-1 to remain stably sequestered into large rhTRIM5alpha cytoplasmic bodies, preventing the clearance of HIV-1 viral complexes from the cytoplasm and revealing an intermediate in the restriction process. Furthermore, we can measure no loss of capsid protein from viral complexes arrested at this intermediate step in restriction, suggesting that any rhTRIM5alpha-mediated loss of capsid protein requires proteasome activity.
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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.