Structural and mechanistic dynamics of Rift Valley Fever Virus replication
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| Year of publication | 2025 |
| Type | Conference abstract |
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| Description | 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. |
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