ArticleSignal transduction and targeted therapy2024
Natural evidence of coronaviral 2'-O-methyltransferase activity affecting viral pathogenesis via improved substrate RNA binding.
Article in Signal transduction and targeted therapy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- NSUN2-mediated m5C modification of HIV-1 RNA enables evasion of RIG‑I‑dependent innate immunity.PLoS pathogens · 2026Article
- Evolutionary Origins and Functional Diversification of 2'-O-Methyltransferases: Insights from Phylogenetic and Structural Analysis.International journal of molecular sciences · 2025Article
- SARS-CoV-2 specific adaptations in N protein inhibit NF-κB activation and alter pathogenesis.The Journal of cell biology · 2025Article
- Leveraging plant-derived nanovesicles for advanced nucleic acid-based gene therapy.Theranostics · 2025Review
- Immuno-epigenetic paradigms in coronavirus infection.Frontiers in immunology · 2025Review
- Role of the epitranscriptome in viral infections: beneficial or detrimental?Memorias do Instituto Oswaldo Cruz · 2025Review
- Structural and functional insights into the 2'-O-methyltransferase of SARS-CoV-2.Virologica Sinica · 2024Article
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Authors and funding
15 authors.
Funding
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Abstract
Previous studies through targeted mutagenesis of K-D-K-E motif have demonstrated that 2'-O-MTase activity is essential for efficient viral replication and immune evasion. However, the K-D-K-E catalytic motif of 2'-O-MTase is highly conserved across numerous viruses, including flaviviruses, vaccinia viruses, coronaviruses, and extends even to mammals. Here, we observed a stronger 2'-O-MTase activity in SARS-CoV-2 compared to SARS-CoV, despite the presence of a consistently active catalytic center. We further identified critical residues (Leu-36, Asn-138 and Ile-153) which served as determinants of discrepancy in 2'-O-MTase activity between SARS-CoV-2 and SARS-CoV. These residues significantly enhanced the RNA binding affinity of 2'-O-MTase and boosted its versatility toward RNA substrates. Of interest, a triple substitution (Leu
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