AustralieFrV1, PascalFrancis, Corpus, bibRecord, 000395

Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease

Identifieur interne : 000395 ( PascalFrancis/Corpus ); précédent : 000394; suivant : 000396

Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease

Auteurs : Linda Wiltzer ; Kazuma Okada ; Satoko Yamaoka ; Florence Larrous ; Henna Veera Kuusisto ; Makoto Sugiyama ; Danielle Blondel ; Hervé Bourhy ; David Andrew Jans ; Naoto Ito ; Gregory William Moseley

Source :

The Journal of infectious diseases [ 0022-1899 ] ; 2014.

RBID : Pascal:14-0154059

Descripteurs français

Pascal (Inist)
- Virus rage, Glycine dehydrogenase (decarboxylating), Protéine, Infection, Rage.

English descriptors

KwdEn :
- Glycine dehydrogenase (decarboxylating), Infection, Protein, Rabies, Rabies virus.

Abstract

Background. Rabies virus (RABV) causes rabies disease resulting in >55000 human deaths/year. The multifunctional RABV P-protein has essential roles in genome replication, and forms interactions with cellular STAT proteins that are thought to underlie viral antagonism of interferon-dependent immunity. However, the molecular details of P-protein-STAT interaction, and its importance to disease are unresolved. Methods. Studies were performed using sequence/structure analysis, mutagenesis, immunoprecipitation, luciferase and qRT-PCR-based signaling assays, confocal microscopy and reverse genetics/in vivo infection. Results. We identified a hydrophobic pocket of the P-protein C-terminal domain as critical to STAT-binding/ antagonism. This interface was found to be functionally and spatially independent of the region responsible for N-protein interaction, which is critical to genome replication. Based on these findings, we generated the first mutant RABV lacking STAT-association. Growth of the virus in vitro was unimpaired, but it lacked STAT-antagonist function and was highly sensitive to interferon. Importantly, growth of the virus was strongly attenuated in brains of infected mice, producing no major neurological symptoms, compared with the invariably lethal wild-type virus. Conclusions. These data represent direct evidence that P-protein-STAT interaction is critical to rabies, and provide novel insights into the mechanism by which RABV coordinates distinct functions in interferon antagonism and replication.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A11	`02`	`1`		`@1 OKADA (Kazuma)`
A11	`03`	`1`		`@1 YAMAOKA (Satoko)`
A11	`04`	`1`		`@1 LARROUS (Florence)`
A11	`05`	`1`		`@1 KUUSISTO (Henna Veera)`
A11	`06`	`1`		`@1 SUGIYAMA (Makoto)`
A11	`07`	`1`		`@1 BLONDEL (Danielle)`
A11	`08`	`1`		`@1 BOURHY (Hervé)`
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A14	`02`			`@1 Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University @2 Victoria 3800 @3 AUS @Z 1 aut. @Z 5 aut. @Z 9 aut.`
A14	`03`			`@1 The United Graduate School of Veterinary Sciences, Gifu University @2 Gifu 501-1193 @3 JPN @Z 2 aut. @Z 3 aut.`
A14	`04`			`@1 Institut Pasteur, Unit Lyssavirus Dynamics and Host Adaptation, Cellule Pasteur @2 Paris @3 FRA @Z 4 aut. @Z 8 aut.`
A14	`05`			`@1 Université Paris Diderot, Sorbonne Paris Cité, Cellule Pasteur @2 Paris @3 FRA @Z 4 aut.`
A14	`06`			`@1 Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University @2 Gifu 501-1193 @3 JPN @Z 6 aut. @Z 10 aut.`
A14	`07`			`@1 Laboratoire de Virologie Moléculaire et Structurale, CNRS, UMR2472 @3 FRA @Z 7 aut.`
A14	`08`			`@1 Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne @2 Parkville, Victoria @3 AUS @Z 11 aut.`
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C01	`01`		`ENG`	@0 Background. Rabies virus (RABV) causes rabies disease resulting in >55000 human deaths/year. The multifunctional RABV P-protein has essential roles in genome replication, and forms interactions with cellular STAT proteins that are thought to underlie viral antagonism of interferon-dependent immunity. However, the molecular details of P-protein-STAT interaction, and its importance to disease are unresolved. Methods. Studies were performed using sequence/structure analysis, mutagenesis, immunoprecipitation, luciferase and qRT-PCR-based signaling assays, confocal microscopy and reverse genetics/in vivo infection. Results. We identified a hydrophobic pocket of the P-protein C-terminal domain as critical to STAT-binding/ antagonism. This interface was found to be functionally and spatially independent of the region responsible for N-protein interaction, which is critical to genome replication. Based on these findings, we generated the first mutant RABV lacking STAT-association. Growth of the virus in vitro was unimpaired, but it lacked STAT-antagonist function and was highly sensitive to interferon. Importantly, growth of the virus was strongly attenuated in brains of infected mice, producing no major neurological symptoms, compared with the invariably lethal wild-type virus. Conclusions. These data represent direct evidence that P-protein-STAT interaction is critical to rabies, and provide novel insights into the mechanism by which RABV coordinates distinct functions in interferon antagonism and replication.
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Format Inist (serveur)

NO :	PASCAL 14-0154059 INIST
ET :	Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease
AU :	WILTZER (Linda); OKADA (Kazuma); YAMAOKA (Satoko); LARROUS (Florence); KUUSISTO (Henna Veera); SUGIYAMA (Makoto); BLONDEL (Danielle); BOURHY (Hervé); JANS (David Andrew); ITO (Naoto); MOSELEY (Gregory William)
AF :	Viral Pathogenesis Laboratory, Monash University/Victoria 3800/Australie (1 aut., 11 aut.); Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University/Victoria 3800/Australie (1 aut., 5 aut., 9 aut.); The United Graduate School of Veterinary Sciences, Gifu University/Gifu 501-1193/Japon (2 aut., 3 aut.); Institut Pasteur, Unit Lyssavirus Dynamics and Host Adaptation, Cellule Pasteur/Paris/France (4 aut., 8 aut.); Université Paris Diderot, Sorbonne Paris Cité, Cellule Pasteur/Paris/France (4 aut.); Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University/Gifu 501-1193/Japon (6 aut., 10 aut.); Laboratoire de Virologie Moléculaire et Structurale, CNRS, UMR2472/France (7 aut.); Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne/Parkville, Victoria/Australie (11 aut.)
DT :	Publication en série; Niveau analytique
SO :	The Journal of infectious diseases; ISSN 0022-1899; Coden JIDIAQ; Royaume-Uni; Da. 2014; Vol. 209; No. 11; Pp. 1744-1753; Bibl. 44 ref.
LA :	Anglais
EA :	Background. Rabies virus (RABV) causes rabies disease resulting in >55000 human deaths/year. The multifunctional RABV P-protein has essential roles in genome replication, and forms interactions with cellular STAT proteins that are thought to underlie viral antagonism of interferon-dependent immunity. However, the molecular details of P-protein-STAT interaction, and its importance to disease are unresolved. Methods. Studies were performed using sequence/structure analysis, mutagenesis, immunoprecipitation, luciferase and qRT-PCR-based signaling assays, confocal microscopy and reverse genetics/in vivo infection. Results. We identified a hydrophobic pocket of the P-protein C-terminal domain as critical to STAT-binding/ antagonism. This interface was found to be functionally and spatially independent of the region responsible for N-protein interaction, which is critical to genome replication. Based on these findings, we generated the first mutant RABV lacking STAT-association. Growth of the virus in vitro was unimpaired, but it lacked STAT-antagonist function and was highly sensitive to interferon. Importantly, growth of the virus was strongly attenuated in brains of infected mice, producing no major neurological symptoms, compared with the invariably lethal wild-type virus. Conclusions. These data represent direct evidence that P-protein-STAT interaction is critical to rabies, and provide novel insights into the mechanism by which RABV coordinates distinct functions in interferon antagonism and replication.
CC :	002A05C10; 002B05
FD :	Virus rage; Glycine dehydrogenase (decarboxylating); Protéine; Infection; Rage
FG :	Lyssavirus; Rhabdoviridae; Mononegavirales; Virus; Oxidoreductases; Enzyme; Pathologie du système nerveux; Virose
ED :	Rabies virus; Glycine dehydrogenase (decarboxylating); Protein; Infection; Rabies
EG :	Lyssavirus; Rhabdoviridae; Mononegavirales; Virus; Oxidoreductases; Enzyme; Nervous system diseases; Viral disease
SD :	Rabies virus; Glycine dehydrogenase (decarboxylating); Proteína; Infección; Rabia
LO :	INIST-2052.354000502740270110
ID :	14-0154059

Links to Exploration step

Pascal:14-0154059

Le document en format XML

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<author><name sortKey="Ito, Naoto" sort="Ito, Naoto" uniqKey="Ito N" first="Naoto" last="Ito">Naoto Ito</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease</title>
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<author><name sortKey="Okada, Kazuma" sort="Okada, Kazuma" uniqKey="Okada K" first="Kazuma" last="Okada">Kazuma Okada</name>
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<author><name sortKey="Yamaoka, Satoko" sort="Yamaoka, Satoko" uniqKey="Yamaoka S" first="Satoko" last="Yamaoka">Satoko Yamaoka</name>
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<author><name sortKey="Larrous, Florence" sort="Larrous, Florence" uniqKey="Larrous F" first="Florence" last="Larrous">Florence Larrous</name>
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<s2>Paris</s2>
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<affiliation><inist:fA14 i1="05"><s1>Université Paris Diderot, Sorbonne Paris Cité, Cellule Pasteur</s1>
<s2>Paris</s2>
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<sZ>4 aut.</sZ>
</inist:fA14>
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<author><name sortKey="Kuusisto, Henna Veera" sort="Kuusisto, Henna Veera" uniqKey="Kuusisto H" first="Henna Veera" last="Kuusisto">Henna Veera Kuusisto</name>
<affiliation><inist:fA14 i1="02"><s1>Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University</s1>
<s2>Victoria 3800</s2>
<s3>AUS</s3>
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<author><name sortKey="Sugiyama, Makoto" sort="Sugiyama, Makoto" uniqKey="Sugiyama M" first="Makoto" last="Sugiyama">Makoto Sugiyama</name>
<affiliation><inist:fA14 i1="06"><s1>Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University</s1>
<s2>Gifu 501-1193</s2>
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<author><name sortKey="Blondel, Danielle" sort="Blondel, Danielle" uniqKey="Blondel D" first="Danielle" last="Blondel">Danielle Blondel</name>
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<s3>FRA</s3>
<sZ>7 aut.</sZ>
</inist:fA14>
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<author><name sortKey="Bourhy, Herve" sort="Bourhy, Herve" uniqKey="Bourhy H" first="Hervé" last="Bourhy">Hervé Bourhy</name>
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<s2>Paris</s2>
<s3>FRA</s3>
<sZ>4 aut.</sZ>
<sZ>8 aut.</sZ>
</inist:fA14>
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</author>
<author><name sortKey="Jans, David Andrew" sort="Jans, David Andrew" uniqKey="Jans D" first="David Andrew" last="Jans">David Andrew Jans</name>
<affiliation><inist:fA14 i1="02"><s1>Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University</s1>
<s2>Victoria 3800</s2>
<s3>AUS</s3>
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<author><name sortKey="Ito, Naoto" sort="Ito, Naoto" uniqKey="Ito N" first="Naoto" last="Ito">Naoto Ito</name>
<affiliation><inist:fA14 i1="06"><s1>Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University</s1>
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<s3>JPN</s3>
<sZ>6 aut.</sZ>
<sZ>10 aut.</sZ>
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</affiliation>
</author>
<author><name sortKey="Moseley, Gregory William" sort="Moseley, Gregory William" uniqKey="Moseley G" first="Gregory William" last="Moseley">Gregory William Moseley</name>
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<s2>Victoria 3800</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>11 aut.</sZ>
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<affiliation><inist:fA14 i1="08"><s1>Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne</s1>
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<s3>AUS</s3>
<sZ>11 aut.</sZ>
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<series><title level="j" type="main">The Journal of infectious diseases</title>
<title level="j" type="abbreviated">J. infect. dis.</title>
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<front><div type="abstract" xml:lang="en">Background. Rabies virus (RABV) causes rabies disease resulting in >55000 human deaths/year. The multifunctional RABV P-protein has essential roles in genome replication, and forms interactions with cellular STAT proteins that are thought to underlie viral antagonism of interferon-dependent immunity. However, the molecular details of P-protein-STAT interaction, and its importance to disease are unresolved. Methods. Studies were performed using sequence/structure analysis, mutagenesis, immunoprecipitation, luciferase and qRT-PCR-based signaling assays, confocal microscopy and reverse genetics/in vivo infection. Results. We identified a hydrophobic pocket of the P-protein C-terminal domain as critical to STAT-binding/ antagonism. This interface was found to be functionally and spatially independent of the region responsible for N-protein interaction, which is critical to genome replication. Based on these findings, we generated the first mutant RABV lacking STAT-association. Growth of the virus in vitro was unimpaired, but it lacked STAT-antagonist function and was highly sensitive to interferon. Importantly, growth of the virus was strongly attenuated in brains of infected mice, producing no major neurological symptoms, compared with the invariably lethal wild-type virus. Conclusions. These data represent direct evidence that P-protein-STAT interaction is critical to rabies, and provide novel insights into the mechanism by which RABV coordinates distinct functions in interferon antagonism and replication.</div>
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<sZ>8 aut.</sZ>
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<ET>Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease</ET>
<AU>WILTZER (Linda); OKADA (Kazuma); YAMAOKA (Satoko); LARROUS (Florence); KUUSISTO (Henna Veera); SUGIYAMA (Makoto); BLONDEL (Danielle); BOURHY (Hervé); JANS (David Andrew); ITO (Naoto); MOSELEY (Gregory William)</AU>
<AF>Viral Pathogenesis Laboratory, Monash University/Victoria 3800/Australie (1 aut., 11 aut.); Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University/Victoria 3800/Australie (1 aut., 5 aut., 9 aut.); The United Graduate School of Veterinary Sciences, Gifu University/Gifu 501-1193/Japon (2 aut., 3 aut.); Institut Pasteur, Unit Lyssavirus Dynamics and Host Adaptation, Cellule Pasteur/Paris/France (4 aut., 8 aut.); Université Paris Diderot, Sorbonne Paris Cité, Cellule Pasteur/Paris/France (4 aut.); Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University/Gifu 501-1193/Japon (6 aut., 10 aut.); Laboratoire de Virologie Moléculaire et Structurale, CNRS, UMR2472/France (7 aut.); Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne/Parkville, Victoria/Australie (11 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>The Journal of infectious diseases; ISSN 0022-1899; Coden JIDIAQ; Royaume-Uni; Da. 2014; Vol. 209; No. 11; Pp. 1744-1753; Bibl. 44 ref.</SO>
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<EA>Background. Rabies virus (RABV) causes rabies disease resulting in >55000 human deaths/year. The multifunctional RABV P-protein has essential roles in genome replication, and forms interactions with cellular STAT proteins that are thought to underlie viral antagonism of interferon-dependent immunity. However, the molecular details of P-protein-STAT interaction, and its importance to disease are unresolved. Methods. Studies were performed using sequence/structure analysis, mutagenesis, immunoprecipitation, luciferase and qRT-PCR-based signaling assays, confocal microscopy and reverse genetics/in vivo infection. Results. We identified a hydrophobic pocket of the P-protein C-terminal domain as critical to STAT-binding/ antagonism. This interface was found to be functionally and spatially independent of the region responsible for N-protein interaction, which is critical to genome replication. Based on these findings, we generated the first mutant RABV lacking STAT-association. Growth of the virus in vitro was unimpaired, but it lacked STAT-antagonist function and was highly sensitive to interferon. Importantly, growth of the virus was strongly attenuated in brains of infected mice, producing no major neurological symptoms, compared with the invariably lethal wild-type virus. Conclusions. These data represent direct evidence that P-protein-STAT interaction is critical to rabies, and provide novel insights into the mechanism by which RABV coordinates distinct functions in interferon antagonism and replication.</EA>
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Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease

Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease

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