TRIM family proteins: retroviral restriction and antiviral defence
Abstract
Members of the tripartite motif (TRIM) protein family are involved in various cellular processes, including cell proliferation, differentiation, development, oncogenesis and apoptosis. Some TRIM proteins display antiviral properties, targeting retroviruses in particular. The potential activity of TRIM19, better known as promyelocytic leukaemia protein, against several viruses has been well documented and, recently, TRIM5alpha has been identified as the factor responsible for the previously described Lv1 and Ref1 antiretroviral activities. There is also evidence indicating that other TRIM proteins can influence viral replication. These findings are reviewed here, and the possibility that TRIMs represent a new and widespread class of antiviral proteins involved in innate immunity is also considered.
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Incoming retroviruses are targeted by TRIM5α, which leads to capsid disassembly.
“Incoming retroviruses are targeted by TRIM5α, which leads to capsid disassembly 58.”
From Are human endogenous retroviruses pathogenic? An approach to testing the hypothesis (2013) · cites this paper as [58]
Recognition of polymeric capsid proteins by TRIM5α is thought to occur shortly after virion entry and uncoating.
“and recognition of polymeric capsid proteins by TRIM5α is thought to occur shortly after virion entry and uncoating 58.”
From Are human endogenous retroviruses pathogenic? An approach to testing the hypothesis (2013) · cites this paper as [58]
TRIM5α shows high selectivity for retroviral capsids, and the human isoform binds HIV-1 capsids only weakly.
“TRIM5α shows high selectivity for retroviral capsids and the human isoform binds HIV-1 capsids only weakly 58.”
From Are human endogenous retroviruses pathogenic? An approach to testing the hypothesis (2013) · cites this paper as [58]
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- Authors
- Nisole, S., Stoye, J. P., & Saïb, A.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- National Institute for Medical Research (GB)
- Corresponding author
- Nisole, Sébastien
- Venue
- Nature Reviews Microbiology
- Published
- 2005-09-09
- Volume
- 3
- Issue
- 10
- Pages
- 799-808
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W2002039213
- Cited by
- 761
- References
- 7
- Citations by year
- 2026: 8 · 2025: 18 · 2024: 29 · 2023: 29 · 2022: 21 · 2021: 37 · 2020: 39 · 2019: 40 · 2018: 28 · 2017: 32 · 2016: 24 · 2015: 37 · 2014: 44 · 2013: 47 · 2012: 43
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Styrelsen för Internationellt Utvecklingssamarbete
- Research Councils UK
- Fondation pour la Recherche Médicale
- Medical Research Council
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- TRIM proteins, retroviral restriction, antiviral defense, innate immunity, TRIM5α, antiretroviral activity, viral replication, carcinogenesis, apoptosis
- MeSH terms
- Tripartite Motif Proteins, Promyelocytic Leukemia Protein, Animals, Humans, Neoplasm Proteins, Nuclear Proteins, Proteins, Repressor Proteins, Retroviridae, Transcription Factors, Virus Replication, Minor Histocompatibility Antigens, Alternative Splicing, Protein Structure, Tertiary, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases
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