8b8a
Multimerization domain of borna disease virus 1 phosphoprotein
Structural highlights
FunctionPHOSP_BDV1 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:P0C799] Publication Abstract from PubMedDetermining the structural organisation of viral replication complexes and unravelling the impact of infection on cellular homeostasis represent important challenges in virology. This may prove particularly useful when confronted with viruses that pose a significant threat to human health, that appear unique within their family, or for which knowledge is scarce. Among Mononegavirales, bornaviruses (family Bornaviridae) stand out due to their compact genomes and their nuclear localisation for replication. The recent recognition of the zoonotic potential of several orthobornaviruses has sparked a surge of interest in improving our knowledge on this viral family. In this work, we provide a complete analysis of the structural organisation of Borna disease virus 1 (BoDV-1) phosphoprotein (P), an important cofactor for polymerase activity. Using X-ray diffusion and diffraction experiments, we revealed that BoDV-1 P adopts a long coiled-coil alpha-helical structure split into two parts by an original beta-strand twist motif, which is highly conserved across the members of whole Orthobornavirus genus and may regulate viral replication. In parallel, we used BioID to determine the proximal interactome of P in living cells. We confirmed previously known interactors and identified novel proteins linked to several biological processes such as DNA repair or mRNA metabolism. Altogether, our study provides important structure/function cues, which may improve our understanding of BoDV-1 pathogenesis. Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing.,Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crepin T Viruses. 2022 Oct 26;14(11):2358. doi: 10.3390/v14112358. PMID:36366462[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
