Structural and mechanistic dynamics of Rift Valley Fever Virus replication

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00141468" target="_blank" >RIV/00216224:14740/25:00141468 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structural and mechanistic dynamics of Rift Valley Fever Virus replication

Popis výsledku v původním jazyce

Rift Valley fever virus (RVFV) is a zoonotic, segmented RNA virus responsible for severe outbreaks in both humans and livestock. In newborn livestock, RVFV can cause mortality rates of up to 100%, while human fatalities from severe hemorrhagic disease can reach as high as 50%. The virus encodes an RNA-dependent RNA polymerase, known as the L-protein, which is essential for both replication and transcription. The L-protein employs a distinctive prime-and-realign mechanism for internal replication, which is directed by regulatory sequences known as promoters, found at the 5′ and 3′ ends of the single-stranded viral RNAs. However, the mechanistic details of the replication process involving the L-protein of RVFV remain elusive. In this study, we used cryo-electron microscopy (cryo-EM) single-particle analysis to examine the L-protein during replication with various promoter sets. By visualizing the structural intermediates, our findings uncover several conformational changes driven by differential promoter binding. Overall, this study offers valuable insights into the structural and mechanistic dynamics of RVFV replication, enhancing our understanding of how promoter-induced conformational stabilization influences viral RNA synthesis.

Název v anglickém jazyce

Structural and mechanistic dynamics of Rift Valley Fever Virus replication

Popis výsledku anglicky

Rift Valley fever virus (RVFV) is a zoonotic, segmented RNA virus responsible for severe outbreaks in both humans and livestock. In newborn livestock, RVFV can cause mortality rates of up to 100%, while human fatalities from severe hemorrhagic disease can reach as high as 50%. The virus encodes an RNA-dependent RNA polymerase, known as the L-protein, which is essential for both replication and transcription. The L-protein employs a distinctive prime-and-realign mechanism for internal replication, which is directed by regulatory sequences known as promoters, found at the 5′ and 3′ ends of the single-stranded viral RNAs. However, the mechanistic details of the replication process involving the L-protein of RVFV remain elusive. In this study, we used cryo-electron microscopy (cryo-EM) single-particle analysis to examine the L-protein during replication with various promoter sets. By visualizing the structural intermediates, our findings uncover several conformational changes driven by differential promoter binding. Overall, this study offers valuable insights into the structural and mechanistic dynamics of RVFV replication, enhancing our understanding of how promoter-induced conformational stabilization influences viral RNA synthesis.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LL2008" target="_blank" >LL2008: Komunikace mezi transkripcí a translací</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2025

Kód důvěrnosti údajů

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