Cited by 648HIV Research and Treatmentinterferon and immune responsesImmune Response and Inflammation

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TRIM5 is an innate immune sensor for the retrovirus capsid lattice

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Pertel, Thomas, Hausmann, Stéphane, Morger, Damien, Züger, Sara, Guerra, Jessica, Lascano, Josefina, Reinhard, Christian, Santoni, Federico A., Uchil, Pradeep D., Chatel, Laurence, Bisiaux, Aurélie, Albert, Matthew L., Strambio-De-Castillia, Caterina, Mothes, Walther, Pizzato, Massimo, Grütter, Markus G., Luban, Jeremy·2011·Nature

DOI 10.1038/nature09976PMC PMC3081621

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Abstract

TRIM5 is a RING domain-E3 ubiquitin ligase that restricts infection by human immunodeficiency virus (HIV)-1 and other retroviruses immediately following virus invasion of the target cell cytoplasm. Antiviral potency correlates with TRIM5 avidity for the retrovirion capsid lattice and several reports indicate that TRIM5 has a role in signal transduction, but the precise mechanism of restriction is unknown. Here we demonstrate that TRIM5 promotes innate immune signalling and that this activity is amplified by retroviral infection and interaction with the capsid lattice. Acting with the heterodimeric, ubiquitin-conjugating enzyme UBC13-UEV1A (also known as UBE2N-UBE2V1), TRIM5 catalyses the synthesis of unattached K63-linked ubiquitin chains that activate the TAK1 (also known as MAP3K7) kinase complex and stimulate AP-1 and NFκB signalling. Interaction with the HIV-1 capsid lattice greatly enhances the UBC13-UEV1A-dependent E3 activity of TRIM5 and challenge with retroviruses induces the transcription of AP-1 and NF-κB-dependent factors with a magnitude that tracks with TRIM5 avidity for the invading capsid. Finally, TAK1 and UBC13-UEV1A contribute to capsid-specific restriction by TRIM5. Thus, the retroviral restriction factor TRIM5 has two additional activities that are linked to restriction: it constitutively promotes innate immune signalling and it acts as a pattern recognition receptor specific for the retrovirus capsid lattice.

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Authors: Pertel, T., Hausmann, S., Morger, D., Züger, S., Guerra, J., Lascano, J., Reinhard, C., Santoni, F. A., Uchil, P. D., Chatel, L., Bisiaux, A., Albert, M. L., Strambio-De-Castillia, C., Mothes, W., Pizzato, M., Grütter, M. G., & Luban, J.
Affiliations: University of Geneva (CH)
University of Zurich (CH)
Yale University (US)
Light Chain Bioscience (Switzerland) (CH)
Inserm (FR)
Corresponding author: Luban, Jeremy
ORCID: Pertel, Thomas
Hausmann, Stéphane
Guerra, Jessica
Lascano, Josefina
Santoni, Federico A.
Uchil, Pradeep D.
Chatel, Laurence
Bisiaux, Aurélie
Albert, Matthew L.
Mothes, Walther
Pizzato, Massimo
Luban, Jeremy
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2011-04
Volume: 472
Issue: 7343
Pages: 361-365
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature09976
PMC: PMC3081621
OpenAlex: W2057040546
Cited by: 645
References: 27
Citations by year: 2026: 14 · 2025: 20 · 2024: 35 · 2023: 27 · 2022: 19 · 2021: 34 · 2020: 39 · 2019: 50 · 2018: 43 · 2017: 41 · 2016: 39 · 2015: 48 · 2014: 56 · 2013: 70 · 2012: 72
FWCI: 29.88
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Archive ouverte UNIGE (University of Geneva) (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
SERVAL (Université de Lausanne) (acceptedVersion, other-oa)
IRIS (submittedVersion)
HAL (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Iris (University of Trento) (submittedVersion)
Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
Funders: National Science Foundation
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (59159, 128655, 122342, 3100A0)
National Institutes of Health (3100A0-128655)
National Institute of Allergy and Infectious Diseases (R01 AI59159, R01AI059159, R21AI087467)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: TRIM5, antiretroviral restriction factors, E3 ubiquitin ligase, pattern recognition receptors, innate immune signaling, K63-linked ubiquitin, TAK1, NF-κB signaling, retroviral infection
MeSH terms: Tripartite Motif Proteins, Antiviral Restriction Factors, MAP Kinase Kinase Kinase 7, Capsid, Carrier Proteins, Cell Line, Enzyme Activation, Humans, Immunity, Innate, Lipopolysaccharides, Protein Binding, Retroviridae, Transcription Factors, Signal Transduction, HIV-1, NF-kappa B, Transcription Factor AP-1, MAP Kinase Kinase Kinases, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Receptors, Pattern Recognition, HEK293 Cells

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TRIM5 is an innate immune sensor for the retrovirus capsid lattice

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