Structural highlights
Function
PHOSP_BDVV Essential component of the RNA polymerase transcription and replication complex. Acts as a scaffold which brings L in close proximity to the N-RNA complex. Plays a role in the segregation of the viral genome in host daughter cells during mitosis by interacting with host HMGB1, a host chromatin-remodeling DNA architectural protein, thereby stabilizing RNP on chromosomes. Interacts with host TBK1 and thus interferes with activation of cellular antiviral state. Inhibits cellular histone acetyltransferase activities.[UniProtKB:P0C798][1] [2] [3]
References
- ↑ Schneider U, Blechschmidt K, Schwemmle M, Staeheli P. Overlap of interaction domains indicates a central role of the P protein in assembly and regulation of the Borna disease virus polymerase complex. J Biol Chem. 2004 Dec 31;279(53):55290-6. PMID:15509569 doi:10.1074/jbc.M408913200
- ↑ Matsumoto Y, Hayashi Y, Omori H, Honda T, Daito T, Horie M, Ikuta K, Fujino K, Nakamura S, Schneider U, Chase G, Yoshimori T, Schwemmle M, Tomonaga K. Bornavirus closely associates and segregates with host chromosomes to ensure persistent intranuclear infection. Cell Host Microbe. 2012 May 17;11(5):492-503. PMID:22607802 doi:10.1016/j.chom.2012.04.009
- ↑ Bonnaud EM, Szelechowski M, Bétourné A, Foret C, Thouard A, Gonzalez-Dunia D, Malnou CE. Borna disease virus phosphoprotein modulates epigenetic signaling in neurons to control viral replication. J Virol. 2015 Jun;89(11):5996-6008. PMID:25810554 doi:10.1128/JVI.00454-15
