ArticleeLife2016
Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
What it found
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Who cites it
75 citing papers in PubMed.
- Article
- Study of retroviral restrictions in a Tadarida bat cell line enlightens specific early blocks and TRIM5 locus multiplication.Journal of virology · 2026Article
- TARDBP as a regulator of HIV-1 assembly and infection: a review of targeting the viral capsid precursor Pr55Gag and limiting viral core entry.Cell communication and signaling : CCS · 2026Review
- Host cyclophilin-mediated maturation of an obligate intracellular bacterial surface virulence factor.bioRxiv : the preprint server for biology · 2025Article
- TRIM37 prevents ectopic spindle pole assembly by peptide motif recognition and substrate-dependent oligomerization.Nature structural & molecular biology · 2025Article
- Mesoscale regulation of microtubule-organizing centers by the E3 ligase TRIM37.Nature structural & molecular biology · 2025Article
- Article
- Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025Review
- Cell-free assays reveal that the HIV-1 capsid protects reverse transcripts from cGAS immune sensing.PLoS pathogens · 2025Article
- HIV capsids: orchestrators of innate immune evasion, pathogenesis and pandemicity.The Journal of general virology · 2025Review
- TRIM5 inhibits the replication of Senecavirus A by promoting the RIG-I-mediated type I interferon antiviral response.Veterinary research · 2024Article
- A Branched SELEX Approach Identifies RNA Aptamers That Bind Distinct HIV-1 Capsid Structural Components.ACS infectious diseases · 2024Article
- TBK1 is ubiquitinated by TRIM5α to assemble mitophagy machinery.Cell reports · 2024Article
- HIV-1 with gag processing defects activates cGAS sensing.Retrovirology · 2024Article
- Capsid-dependent lentiviral restrictions.Journal of virology · 2024Review
- Spatiotemporal binding of cyclophilin A and CPSF6 to capsid regulates HIV-1 nuclear entry and integration.bioRxiv : the preprint server for biology · 2024Article
- HIV-1 Capsid Uncoating Is a Multistep Process That Proceeds through Defect Formation Followed by Disassembly of the Capsid Lattice.ACS nano · 2024Article
- HIV-1 capsid and viral DNA integration.mBio · 2024Review
- Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023Review
- HIV-2 Immature Particle Morphology Provides Insights into Gag Lattice Stability and Virus Maturation.Journal of molecular biology · 2023Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
Abstract
TRIM5 proteins are restriction factors that block retroviral infections by binding viral capsids and preventing reverse transcription. Capsid recognition is mediated by C-terminal domains on TRIM5α (SPRY) or TRIMCyp (cyclophilin A), which interact weakly with capsids. Efficient capsid recognition also requires the conserved N-terminal tripartite motifs (TRIM), which mediate oligomerization and create avidity effects. To characterize how TRIM5 proteins recognize viral capsids, we developed methods for isolating native recombinant TRIM5 proteins and purifying stable HIV-1 capsids. Biochemical and EM analyses revealed that TRIM5 proteins assembled into hexagonal nets, both alone and on capsid surfaces. These nets comprised open hexameric rings, with the SPRY domains centered on the edges and the B-box and RING domains at the vertices. Thus, the principles of hexagonal TRIM5 assembly and capsid pattern recognition are conserved across primates, allowing TRIM5 assemblies to maintain the conformational plasticity necessary to recognize divergent and pleomorphic retroviral capsids.
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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.