Inhibition of coronaviral exoribonuclease activity by TRIM-mediated SUMOylation - PubMed
4 hours ago
- #TRIM proteins
- #coronavirus
- #SUMOylation
- TRIM E3 ligase family members play a role in host defense against viruses, but their specific actions against coronaviruses are not fully understood.
- An RNAi screen identified several TRIM proteins with antiviral or proviral effects against SARS-CoV-2.
- TRIM32 restricts SARS-CoV-2 replication in a RING E3 ligase-dependent, interferon-independent manner.
- TRIM32 binds and SUMOylates the Nsp14 exoribonuclease (ExoN), inhibiting its RNA binding and Nsp10 cofactor recruitment, thereby suppressing ExoN activity.
- Nsp14 SUMOylation by TRIM32 is conserved across coronaviruses, suggesting a broad antiviral mechanism.
- This study highlights Nsp14 as a potential therapeutic target for inhibiting coronavirus infections.