Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein

Journal article

Bornaviruses are RNA viruses with a mammalian, reptilian, and avian host range. The viruses infect neuronal cells and in rare cases cause a lethal encephalitis. The family Bornaviridae are part of the Mononegavirales order of viruses, which contain a nonsegmented viral genome. Mononegavirales encode a viral phosphoprotein (P) that binds both the viral polymerase (L) and the viral nucleoprotein (N). The P protein acts as a molecular chaperone and is required for the formation of a functional replication/transcription complex. In this study, the structure of the oligomerization domain of the phosphoprotein determined by X-ray crystallography is reported. The structural results are complemented with biophysical characterization using circular dichroism, differential scanning calorimetry and small-angle X-ray scattering. The data reveal the phosphoprotein to assemble into a stable tetramer, with the regions outside the oligomerization domain remaining highly flexible. A helix-breaking motif is observed between the α-helices at the midpoint of the oligomerization domain that appears to be conserved across the Bornaviridae. These data provide information on an important component of the bornavirus replication complex.

Authors: Whitehead, JD; Grimes, JM; Keown, JR

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: International Union of Crystallography
• Journal: Acta Crystallographica Section F: Structural Biology Communications
• Volume: 79
• Issue: 3
• Pages: 51-60
• Publication date: 2023-02-08
• Acceptance date: 2023-01-26
• DOI: 10.1107/s2053230x23000717
• EISSN: 2053-230X
• ISSN: 2053-230X
• Language: English
• Keywords: Paramyxoviridae; Viral disease; Phosphorylation; Peptide sequence; Gene; Virology; Cell biology; Phosphoprotein; Heptad repeat; Viral replication; Biology; Virus; Nucleoprotein; Genetics; Mononegavirales