The structure of the mammalian bornavirus polymerase complex

Loïc Carrique, Franziska Günl, Adrian Deng, Jonathan M. Grimes and Jeremy R. Keown ()
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Loïc Carrique: University of Oxford
Franziska Günl: University of Oxford
Adrian Deng: University of Warwick
Jonathan M. Grimes: University of Oxford
Jeremy R. Keown: University of Oxford

Nature Communications, 2025, vol. 16, issue 1, 1-11

Abstract: Abstract Borna disease virus 1 (BoDV-1) is a non-segmented RNA virus with one of the smallest known RNA virus genomes. BoDV-1 replicates in the nucleus of infected cells using a virally encoded polymerase complex composed of the large protein and phosphoprotein. Here, we present the BoDV-1 polymerase complex at resolutions up to 2.8 Å, describing the fully ordered large polymerase protein bound to tetrameric phosphoprotein. The complex is maintained through the ordered C-terminal region of one copy of the phosphoprotein. Analysis of the model reveals a conserved methyltransferase domain, though key S-adenosyl methionine binding residues are missing. While no RNA is observed in our models, analysis of a sample under reaction conditions induces an opening and closing of the template entry and exit channels, respectively. Higher-order polymerase assemblies suggest oligomerisation as a conserved feature of negative strand RNA virus polymerases. We provide a molecular framework to investigate bornavirus replication and transcription.

Date: 2025
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DOI: 10.1038/s41467-025-62906-4

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