Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing

Determining 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 appe...

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Bibliographic Details
Published in:	Viruses Vol. 14; no. 11; p. 2358
Main Authors:	Tarbouriech, Nicolas, Chenavier, Florian, Kawasaki, Junna, Bachiri, Kamel, Bourhis, Jean-Marie, Legrand, Pierre, Freslon, Lily L, Laurent, Estelle M N, Suberbielle, Elsa, Ruigrok, Rob W H, Tomonaga, Keizo, Gonzalez-Dunia, Daniel, Horie, Masayuki, Coyaud, Etienne, Crépin, Thibaut
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 26-10-2022 MDPI
Subjects:	Animals Biochemistry, Molecular Biology Borna disease Borna disease virus - genetics Bornaviridae Bornaviridae - genetics Chromatography Datasets Development and progression Disease DNA DNA damage DNA Repair Double-strand break repair Epigenetics Experiments Gene expression Genetic aspects Genomes Homeostasis Humans interactomics Life Sciences Mammals Messenger RNA Microbiology and Parasitology mRNA mRNA processing phosphoprotein Phosphoproteins Phosphoproteins - genetics Physiological aspects Polyethylene glycol Proteins Replication RNA polymerase RNA processing RNA virus infections RNA, Messenger - genetics Sensors Structural Biology Structure Structure-function relationships Viral proteins Virology Virus research Viruses Japan France phosphoprotein interactomics Bornaviridae structure
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Summary:	Determining 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 , bornaviruses (family ) 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 α-helical structure split into two parts by an original β-strand twist motif, which is highly conserved across the members of whole 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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 PMCID: PMC9692295 These authors contributed equally to this work.
ISSN:	1999-4915 1999-4915
DOI:	10.3390/v14112358