Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein

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.

Source: Acta Crystallographica Section F - February 23, 2023 Category: Biochemistry Authors: Whitehead, J.D. Grimes, J.M. Keown, J.R. Tags: bornavirus phosphoproteins X-ray crystallography negative-strand RNA viruses replication research communications Source Type: research