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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Published inViruses 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
LanguageEnglish
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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Abstract 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 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 α-helical structure split into two parts by an original β-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.
AbstractList 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 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 α-helical structure split into two parts by an original β-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.
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 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 α-helical structure split into two parts by an original β-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.
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.
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 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 α-helical structure split into two parts by an original β-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.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 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 α-helical structure split into two parts by an original β-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.
Audience Academic
Author Gonzalez-Dunia, Daniel
Crépin, Thibaut
Freslon, Lily L.
Ruigrok, Rob W. H.
Coyaud, Etienne
Tomonaga, Keizo
Kawasaki, Junna
Bachiri, Kamel
Laurent, Estelle M. N.
Horie, Masayuki
Suberbielle, Elsa
Bourhis, Jean-Marie
Tarbouriech, Nicolas
Chenavier, Florian
Legrand, Pierre
AuthorAffiliation 5 Synchrotron SOLEIL, L’Orme des Merisiers, 91192 Gif-sur-Yvette, France
6 Institut Toulousain des Maladies Infectieuses et Inflammatoires (Infinity), Université de Toulouse, Inserm, CNRS, UPS, 31024 Toulouse, France
1 Institut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 38058 Grenoble, France
3 Laboratory of RNA Viruses, Department of Mammalian Regulatory Network, Graduate School of Biostudies, Kyoto University, Kyoto 606-8507, Japan
9 Osaka International Research Center for Infectious Diseases, Osaka Metropolitan University, Izumisano 598-8531, Japan
2 Laboratory of RNA Viruses, Department of Virus Research, Institute for Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japan
7 Department of Molecular Virology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan
8 Laboratory of Veterinary Microbiology, Graduate School of Veterinary Science, Osaka Metropolitan University, Izumisano 598-8531, Japan
4 Department of Biology, Univ. Lille, Inse
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/36366462$$D View this record in MEDLINE/PubMed
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CitedBy_id crossref_primary_10_1016_j_colsurfb_2024_114385
crossref_primary_10_1007_s15010_023_02048_1
crossref_primary_10_1107_S2053230X23000717
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– notice: 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
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Issue 11
Keywords phosphoprotein
interactomics
Bornaviridae
structure
Language English
License https://creativecommons.org/licenses/by/4.0
Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
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PMCID: PMC9692295
These authors contributed equally to this work.
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Snippet Determining the structural organisation of viral replication complexes and unravelling the impact of infection on cellular homeostasis represent important...
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SubjectTerms 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
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Title Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing
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Volume 14
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