Elucidation of enzymatic mechanism and structure of Ntaya NS5 enzyme

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F24%3A00599885" target="_blank" >RIV/61388963:_____/24:00599885 - isvavai.cz</a>
Result on the web
<a href="http://www.ccsss.cz/index.php/ccsss/issue/view/48/87" target="_blank" >http://www.ccsss.cz/index.php/ccsss/issue/view/48/87</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Elucidation of enzymatic mechanism and structure of Ntaya NS5 enzyme
Original language description
Flaviviruses are single-stranded positive-sense RNA (+RNA) viruses that cause several (re)emerging diseases, including Yellow fever, Dengue, and West Nile fevers1. The Zika epidemic exemplified their potential danger when arelatively harmless virus known since the 1950s became adeadly pathogen2. The NS5 protein (non-structural protein 5) is essential for viral replication, comprising an N-terminal methyltransferase (MTase) domain and a C-terminal RNAdependent RNA polymerase (RdRp) domain. This protein plays a key role in RNA replication and the installation of the 5' RNA cap3. In our study, we structurally and biochemically analyzed the Ntaya virus MTase and RdRp domains, comparing their properties with those of other flaviviral NS5 proteins. While the enzymatic centers are highly conserved across Flaviviridae family, suggesting the potential for developing broad-spectrum of antiviral drugs targeting all flaviviruses, significant differences were observed in the enzymatic activites of the isolated MTase domains4.
Czech name
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Czech description
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Project
<a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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