Journal
NUCLEIC ACIDS RESEARCH
Volume 50, Issue 2, Pages 635-650Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkab1279
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Funding
- Czech Science Foundation [21-25280S]
- Ministry of Health of the Czech Republic [NU20-05-00472]
- European Regional Development Fund
- OP RDE
- Project: 'Chemical biology for drugging undruggable targets (ChemBioDrug)' [CZ.02.1.01/0.0/0.0/16 019/0000729]
- Academy of Sciences of the Czech Republic [RVO: 61388963]
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This article critically summarizes the tremendous advancements in the field of coronaviral MTases since the beginning of the COVID-19 pandemic, including structural elucidation and the discovery of inhibitors.
Coronaviral methyltransferases (MTases), nsp10/16 and nsp14, catalyze the last two steps of viral RNA-cap creation that takes place in cytoplasm. This cap is essential for the stability of viral RNA and, most importantly, for the evasion of innate immune system. Non-capped RNA is recognized by innate immunity which leads to its degradation and the activation of antiviral immunity. As a result, both coronaviral MTases are in the center of scientific scrutiny. Recently, X-ray and cryo-EM structures of both enzymes were solved even in complex with other parts of the viral replication complex. High-throughput screening as well as structure-guided inhibitor design have led to the discovery of their potent inhibitors. Here, we critically summarize the tremendous advancement of the coronaviral MTase field since the beginning of COVID pandemic.
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