An evolutionarily unique viral RdRP suggests a common dual-function feature of the priming element.

Authors

Hengxia Jia, Shunli Liu, Guibo Rao, Qiaojie Liu, Jiqin Wu, Sheng Cao, Peng Gong

Published in

Science advances. Volume 11. Issue 16. Pages eadv9640. Apr 18, 2025. Epub Apr 18, 2025.

Abstract

Many RNA-dependent RNA polymerases (RdRPs) encoded by RNA viruses use de novo initiation strategy to start RNA synthesis, and they usually contain a priming element (PE) to interact with template RNA and priming nucleoside triphosphate to facilitate initiation. Upon transition to elongation in dengue virus 2 (DENV2) RdRP, PE refolds and contributes to elongation complex stability by interacting with the upstream RNA duplex. However, whether this PE dual-function feature commonly exists in viral RdRPs remains elusive, as PE is highly diverse among the entire RNA virus group. Here, a more complexed PE refolding is observed in RdRP crystal structures of Aspergillus fumigatus polymycovirus-1 (AfuPmV-1), a polymycovirus evolutionarily connecting positive-strand and double-stranded RNA viruses. Although structural details and enzymology features are very different in transition from initiation to elongation in DENV2 and AfuPmV-1 RdRPs, what is in common is the PE dual-function feature that demonstrates functional conservation beyond sequence and structure.

PMID:
40249801
Bibliographic data and abstract were imported from PubMed on 19 Apr 2025.

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