ArticleProceedings of the National Academy of Sciences of the United States of America2026
Inhibition of coronaviral exoribonuclease activity by TRIM-mediated SUMOylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Effect of inhaled interferon-β1a on SARS-CoV-2 diversity and evolution.Microbiology spectrum · 2026Trial
- Ubiquitin E3 ligase activity in TRIpartite Motif (TRIM) family proteins.Biochemical Society transactions · 2026Review
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8 authors.
Funding
Abstract
Members of the TRIM E3 ligase family are effectors of the host innate or intrinsic defense against various viruses; however, how specific TRIM proteins antagonize coronavirus infection is still largely elusive. Through an RNAi screen targeting 71 human TRIM genes, we identified multiple TRIM proteins with antiviral or proviral activity against SARS-CoV-2. TRIM32 potently restricted SARS-CoV-2 replication in a RING E3 ligase-dependent but interferon-independent manner. Mechanistically, TRIM32 binds to and SUMOylates the 3'-to-5' exoribonuclease (ExoN) of Nsp14, an enzyme essential for SARS-CoV-2 replication. TRIM32-mediated Nsp14 SUMOylation at K9 and K200 inhibits RNA binding and Nsp10 cofactor recruitment, respectively, ultimately suppressing ExoN activity. Our study further revealed that Nsp14 SUMOylation by TRIM32 and its antiviral activity are broadly conserved for coronaviruses. These results identify the coronaviral Nsp14 protein as a direct target of host restriction via SUMOylation, which may uncover ways to therapeutically inhibit coronavirus infections in humans.
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