Structural basis for RNA-cap recognition and methylation by the mpox methyltransferase VP39

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00574061" target="_blank" >RIV/61388963:_____/23:00574061 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1016/j.antiviral.2023.105663" target="_blank" >https://doi.org/10.1016/j.antiviral.2023.105663</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.antiviral.2023.105663" target="_blank" >10.1016/j.antiviral.2023.105663</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural basis for RNA-cap recognition and methylation by the mpox methyltransferase VP39

Popis výsledku v původním jazyce

Mpox is a zoonotic disease caused by the mpox virus (MPXV), which has gained attention due to its rapid and widespread transmission, with reports from more than 100 countries. The virus belongs to the Orthopoxvirus genus, which also includes variola virus and vaccinia virus. In poxviruses, the RNA cap is crucial for the translation and stability of viral mRNAs and also for immune evasion. This study presents the crystal structure of the mpox 2′-O-methyltransfarase VP39 in complex with a short cap-0 RNA. The RNA substrate binds to the protein without causing any significant changes to its overall fold and is held in place by a combination of electrostatic interactions, π-π stacking and hydrogen bonding. The structure also explains the mpox VP39 preference for a guanine base at the first position, it reveals that guanine forms a hydrogen bond that an adenine would not be able to form.

Název v anglickém jazyce

Structural basis for RNA-cap recognition and methylation by the mpox methyltransferase VP39

Popis výsledku anglicky

Mpox is a zoonotic disease caused by the mpox virus (MPXV), which has gained attention due to its rapid and widespread transmission, with reports from more than 100 countries. The virus belongs to the Orthopoxvirus genus, which also includes variola virus and vaccinia virus. In poxviruses, the RNA cap is crucial for the translation and stability of viral mRNAs and also for immune evasion. This study presents the crystal structure of the mpox 2′-O-methyltransfarase VP39 in complex with a short cap-0 RNA. The RNA substrate binds to the protein without causing any significant changes to its overall fold and is held in place by a combination of electrostatic interactions, π-π stacking and hydrogen bonding. The structure also explains the mpox VP39 preference for a guanine base at the first position, it reveals that guanine forms a hydrogen bond that an adenine would not be able to form.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10607 - Virology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Antiviral Research

ISSN

0166-3542

e-ISSN

1872-9096

Svazek periodika

216

Číslo periodika v rámci svazku

August

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

4

Strana od-do

105663

Kód UT WoS článku

001045871600001

EID výsledku v databázi Scopus

2-s2.0-85165411106