Substrate Specificity of SARS-CoV-2 Nsp10-Nsp16 Methyltransferase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00545559" target="_blank" >RIV/61388963:_____/21:00545559 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.3390/v13091722" target="_blank" >https://doi.org/10.3390/v13091722</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/v13091722" target="_blank" >10.3390/v13091722</a>
Alternative languages
Result language
angličtina
Original language name
Substrate Specificity of SARS-CoV-2 Nsp10-Nsp16 Methyltransferase
Original language description
The ongoing COVID-19 pandemic exemplifies the general need to better understand viral infections. The positive single-strand RNA genome of its causative agent, the SARS coronavirus 2 (SARS-CoV-2), encodes all viral enzymes. In this work, we focused on one particular methyltransferase (MTase), nsp16, which, in complex with nsp10, is capable of methylating the first nucleotide of a capped RNA strand at the 2′-O position. This process is part of a viral capping system and is crucial for viral evasion of the innate immune reaction. In light of recently discovered non-canonical RNA caps, we tested various dinucleoside polyphosphate-capped RNAs as substrates for nsp10-nsp16 MTase. We developed an LC-MS-based method and discovered four types of capped RNA (m7Gp3A(G)- and Gp3A(G)-RNA) that are substrates of the nsp10-nsp16 MTase. Our technique is an alternative to the classical isotope labelling approach for the measurement of 2′-O-MTase activity. Further, we determined the IC50 value of sinefungin to illustrate the use of our approach for inhibitor screening. In the future, this approach may be an alternative technique to the radioactive labelling method for screening inhibitors of any type of 2′-O-MTase.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Viruses
ISSN
1999-4915
e-ISSN
1999-4915
Volume of the periodical
13
Issue of the periodical within the volume
9
Country of publishing house
CH - SWITZERLAND
Number of pages
12
Pages from-to
1722
UT code for WoS article
000702076700001
EID of the result in the Scopus database
2-s2.0-85114370612