ArticlePLoS pathogens2020
TRIM34 restricts HIV-1 and SIV capsids in a TRIM5α-dependent manner.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 54 citations in OpenAlex.
- Oncogenic viral infection triggers LAMP2A SUMOylation and chaperone-mediated autophagy to promote tumorigenesis.Nature microbiology · 2026Article
- Ubiquitin E3 ligase activity in TRIpartite Motif (TRIM) family proteins.Biochemical Society transactions · 2026Review
- CypA is a molecular barrier to HIV emergence from Eastern chimpanzees.bioRxiv : the preprint server for biology · 2026Article
- Systematic Reanalysis of Whole-Exome Sequencing in Genetically Unsolved Pediatric Primary Ciliary Dyskinesia.Pediatric pulmonology · 2026Article
- TRIM5 integrates hypoglycemic stress and influenza infection.Nature communications · 2026Article
- Tripartite motif-containing 34 (TRIM34) protein interacts with the nucleocytoplasmic transport machinery and negatively modulates antiviral responses.PLoS pathogens · 2026Article
- Updates on the role of TRIM proteins in AIDS: molecular mechanisms and potential for interventions.Frontiers in immunology · 2026Review
- DNA methylation signatures of severe RSV infection in infants: evidence from non-invasive saliva samples.Epigenetics & chromatin · 2025Article
- Subtype AD Recombinant HIV-1 Transmitted/Founder Viruses Are Less Sensitive to Type I Interferons than Subtype D.Viruses · 2025Article
- Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM.Cell reports · 2025Article
- Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025Review
- Interleukin-27-polarized HIV-resistant M2 macrophages are a novel subtype of macrophages that express distinct antiviral gene profiles in individual cells: implication for the antiviral effect via different mechanisms in the individual cell-dependent manner.Frontiers in immunology · 2025Article
- Mapping of susceptibility loci for Ebola virus pathogenesis in mice.Cell reports · 2024Article
- Replication competent HIV-guided CRISPR screen identifies antiviral factors including targets of the accessory protein Nef.Nature communications · 2024Article
- Capsid-dependent lentiviral restrictions.Journal of virology · 2024Review
- Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.PLoS pathogens · 2024Article
- Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023Review
- Primate TRIM34 is a broadly-acting, TRIM5-dependent lentiviral restriction factor.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The HIV-1 capsid protein makes up the core of the virion and plays a critical role in early steps of HIV replication. Due to its exposure in the cytoplasm after entry, HIV capsid is a target for host cell factors that act directly to block infection such as TRIM5α and MxB. Several host proteins also play a role in facilitating infection, including in the protection of HIV-1 capsid from recognition by host cell restriction factors. Through an unbiased screening approach, called HIV-CRISPR, we show that the CPSF6-binding deficient, N74D HIV-1 capsid mutant is sensitive to restriction mediated by human TRIM34, a close paralog of the well-characterized HIV restriction factor TRIM5α. This restriction occurs at the step of reverse transcription, is independent of interferon stimulation, and limits HIV-1 infection in key target cells of HIV infection including CD4+ T cells and monocyte-derived dendritic cells. TRIM34 can also restrict some SIV capsids. TRIM34 restriction requires TRIM5α as knockout or knockdown of TRIM5α results in a loss of antiviral activity. Through immunofluorescence studies, we show that TRIM34 and TRIM5α colocalize to cytoplasmic bodies and are more frequently observed to be associated with infecting N74D capsids than with WT HIV-1 capsids. Our results identify TRIM34 as an HIV-1 CA-targeting restriction factor and highlight the potential role for heteromultimeric TRIM interactions in contributing to restriction of HIV-1 infection in human cells.
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