9H1G

Structure of the borna disease virus 1 replication complex

Summary for 9H1G

• Entry DOI: 10.2210/pdb9h1g/pdb
• EMDB information: 51765
• Descriptor: RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total)
• Functional Keywords: polymerase, phosphoprotein, bornavirus, rdrp, viral protein
• Biological source: Borna disease virus 1; More
• Total number of polymer chains: 5
• Total formula weight: 295545.62

Authors

Keown, J.R.,Carrique, L.,Grimes, J.M. (deposition date: 2024-10-09, release date: 2025-08-20, Last modification date: 2026-03-04)

Primary citation

Carrique, L.,Gunl, F.,Deng, A.,Grimes, J.M.,Keown, J.R.
The structure of the mammalian bornavirus polymerase complex.
Nat Commun, 16:7508-7508, 2025

PubMed 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.

PubMed: 40804239
DOI: 10.1038/s41467-025-62906-4

Experimental method

ELECTRON MICROSCOPY (3.07 Å)