TRIM7 inhibits coxsackievirus and norovirus infection Norovirus coxsackievirus TRIM7 MRC_LMB Cambridge_Uni TheCrick
TRIM7 is a protein that accelerates substrate ubiquitination and has antiviral properties; however, the mechanism of viral inhibition is not well-characterized i.e., whether TRIM7 directly binds to and degrades viral proteins or has indirect antiviral effects by activating immunological pathways is not known.
Isothermal titration calorimetry binding experiments were performed using recombinant proteins to probe TRIM7-PRYSPRY interactions with rabbit glycogenin-1 , a TRIM7 ligand. Peptides corresponding to glycogenin helices were synthesized. GYG epitope bound to TRIM7 was identified , following which the team searched for an identical sequence in other ligands of TRIM7.
Furthermore, several HA-TRIM7 constructs were overexpressed in 293T cells to assess the activeness of RING in cells and full-length proteins. The team investigated if TRIM7 binding to helix-FQ substrates would lead to cellular degradation, for which cells were co-transfected with plasmids encoding for EGFP-GYG1 constructs and mCherry-Trim7 constructs . Cellular proteins were quantified using immunoblotting and fluorescence microscopy.
Therefore, the helix-FQ motif was a structural necessity to enable TRIM7-mediated inhibition of noroviruses and coxsackie viruses. In addition, TRIM7 would lose its viral inhibition activity if it is not bound to the glutamine motifs created by 3Cpro-mediated protein cleavage. However, TRIM7 could not restrict SARS-CoV-2.
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