Review: Coronaviral RNA-methyltransferases: function, structure and inhibition
There are 7 coronaviruses known to infect humans, one of them causing a global pandemic last two years affecting billions of people around the world. No wonder, the field of coronavirus research is rapidly developing.
Among the main research targets are coronaviral methyltransferases (MTases), nsp10/16 and nsp14, which 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 as the non-capped RNA is recognized by innate immunity which leads to its degradation and the activation of antiviral immunity.
Recently, X-ray and cryo-EM structures of both enzymes were solved even in complex with other parts of the viral replication complex. And high-throughput screening as well as structure-guided inhibitor design have led to the discovery of their potent inhibitors.
These tremendous advancements of the coronaviral MTase field since the beginning of COVID pandemic are now summarized in recent Nucleic Acids Research review from Radim Nencka and Evžen Bouřa Groups from IOCB Prague.
Read here:
- Nencka, R.; Silhan, J.; Klima, M.; Otava, T.; Kocek, H.; Krafcikova, P.; Boura, E. Coronaviral RNA-methyltransferases: function, structure and inhibition. Nucleic Acids Research 2022, 50, 635-650. https://doi.org/10.1093/nar/gkab1279
