ArticleJournal of virology2013
Virus-specific effects of TRIM5α(rh) RING domain functions on restriction of retroviruses.
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 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Study of retroviral restrictions in a Tadarida bat cell line enlightens specific early blocks and TRIM5 locus multiplication.Journal of virology · 2026Article
- TRIM62 From Chicken as a Negative Regulator of Reticuloendotheliosis Virus Replication.Frontiers in veterinary science · 2020Article
- An E3 ubiquitin ligase from Nicotiana benthamiana targets the replicase of Bamboo mosaic virus and restricts its replication.Molecular plant pathology · 2019Article
- Prospects in Innate Immune Responses as Potential Control Strategies against Non-Primate Lentiviruses.Viruses · 2018Review
- Article
- 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
- Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction.Virology · 2014Article
- Ring finger protein 39 genetic variants associate with HIV-1 plasma viral loads and its replication in cell culture.Cell & bioscience · 2014Article
- Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The tripartite motif protein TRIM5α restricts particular retrovirus infections by binding to the incoming capsid and inhibiting the early stage of virus infection. The TRIM5α RING domain exhibits E3 ubiquitin ligase activity and assists the higher-order association of TRIM5α dimers, which promotes capsid binding. We characterized a panel of RING domain mutants of the rhesus monkey TRIM5α (TRIM5α(rh)) protein. The RING domain function that significantly contributed to retroviral restriction depended upon the restricted virus. The E3 ubiquitin ligase activity of the RING domain contributes to the potency of HIV-1 restriction. Nonetheless, TRIM5α(rh) mutants without detectable E3 ubiquitin ligase activity still blocked reverse transcription and inhibited HIV-1 infection at a moderate level. When TRIM5α(rh) capsid binding was weakened by substitution with a less efficient B30.2/SPRY domain, the promotion of higher-order association by the RING domain was more important to HIV-1 restriction than its E3 ubiquitin ligase activity. For the restriction of N-tropic murine leukemia virus (N-MLV) and equine infectious anemia virus (EIAV) infection, promotion of higher-order association represented the major contribution of the RING domain. Thus, both identity of the target virus and the B30.2/SPRY domain-mediated affinity for the viral capsid determine the relative contribution of the two known RING domain functions to TRIM5α restriction of retrovirus infection.
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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.