SrasV1, PascalFrancis, Corpus, bibRecord, 000072

Ultrastructural Characterization of Arterivirus Replication Structures: Reshaping the Endoplasmic Reticulum To Accommodate Viral RNA Synthesis

Identifieur interne : 000072 ( PascalFrancis/Corpus ); précédent : 000071; suivant : 000073

Ultrastructural Characterization of Arterivirus Replication Structures: Reshaping the Endoplasmic Reticulum To Accommodate Viral RNA Synthesis

Auteurs : Kèvin Knoops ; Montserrat Barcena ; Ronald W. A. L. Limpens ; Abraham J. Koster ; A. Mieke Mommaas ; Eric J. Snijder

Source :

Journal of virology [ 0022-538X ] ; 2012.

RBID : Pascal:12-0114301

Descripteurs français

Pascal (Inist)
- Arterivirus, Réplication, Réticulum endoplasmique.

English descriptors

KwdEn :
- Arterivirus, Endoplasmic reticulum, Replication.

Abstract

Virus-induced membrane structures support the assembly and function of positive-strand RNA virus replication complexes. The replicase proteins of arteriviruses are associated with double-membrane vesicles (DMVs), which were previously proposed to derive from the endoplasmic reticulum (ER). Using electron tomography, we performed an in-depth ultrastructural analysis of cells infected with the prototypic arterivirus equine arteritis virus (EAV). We established that the outer membranes of EAV-induced DMVs are interconnected with each other and with the ER, thus forming a reticulovesicular network (RVN) resembling that previously described for the distantly related severe acute respiratory syndrome (SARS) coronavirus. Despite significant morphological differences, a striking parallel between the two virus groups, and possibly all members of the order Nidovirales, is the accumulation in the DMV interior of double-stranded RNA, the presumed intermediate of viral RNA synthesis. In our electron tomograms, connections between the DMV interior and cytosol could not be unambiguously identified, suggesting that the double-stranded RNA is compartmentalized by the DMV membranes. As a novel approach to visualize and quantify the RNA content of viral replication structures, we explored electron spectroscopic imaging of DMVs, which revealed the presence of phosphorus in amounts equaling on average a few dozen copies of the EAV RNA genome. Finally, our electron tomograms revealed a network of nucleocapsid protein-containing protein tubules that appears to be intertwined with the RVN. This potential intermediate in nucleocapsid formation, which was not observed in coronavirus-infected cells, suggests that arterivirus RNA synthesis and assembly are coordinated in intracellular space.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A03		`1`		`@0 J. virol.`
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A11	`01`	`1`		`@1 KNOOPS (Kèvin)`
A11	`02`	`1`		`@1 BARCENA (Montserrat)`
A11	`03`	`1`		`@1 LIMPENS (Ronald W. A. L.)`
A11	`04`	`1`		`@1 KOSTER (Abraham J.)`
A11	`05`	`1`		`@1 MIEKE MOMMAAS (A.)`
A11	`06`	`1`		`@1 SNIJDER (Eric J.)`
A14	`01`			`@1 Electron Microscopy Section, Department of Molecular Cell Biology, Leiden University Medical Center @2 Leiden @3 NLD @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut.`
A14	`02`			`@1 Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center @2 Leiden @3 NLD @Z 1 aut. @Z 6 aut.`
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A21				`@1 2012`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 13592 @5 354000506798780080`
A44				`@0 0000 @1 © 2012 INIST-CNRS. All rights reserved.`
A45				`@0 67 ref.`
A47	`01`	`1`		`@0 12-0114301`
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A61				`@0 A`
A64	`01`	`1`		`@0 Journal of virology`
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C01	`01`		`ENG`	@0 Virus-induced membrane structures support the assembly and function of positive-strand RNA virus replication complexes. The replicase proteins of arteriviruses are associated with double-membrane vesicles (DMVs), which were previously proposed to derive from the endoplasmic reticulum (ER). Using electron tomography, we performed an in-depth ultrastructural analysis of cells infected with the prototypic arterivirus equine arteritis virus (EAV). We established that the outer membranes of EAV-induced DMVs are interconnected with each other and with the ER, thus forming a reticulovesicular network (RVN) resembling that previously described for the distantly related severe acute respiratory syndrome (SARS) coronavirus. Despite significant morphological differences, a striking parallel between the two virus groups, and possibly all members of the order Nidovirales, is the accumulation in the DMV interior of double-stranded RNA, the presumed intermediate of viral RNA synthesis. In our electron tomograms, connections between the DMV interior and cytosol could not be unambiguously identified, suggesting that the double-stranded RNA is compartmentalized by the DMV membranes. As a novel approach to visualize and quantify the RNA content of viral replication structures, we explored electron spectroscopic imaging of DMVs, which revealed the presence of phosphorus in amounts equaling on average a few dozen copies of the EAV RNA genome. Finally, our electron tomograms revealed a network of nucleocapsid protein-containing protein tubules that appears to be intertwined with the RVN. This potential intermediate in nucleocapsid formation, which was not observed in coronavirus-infected cells, suggests that arterivirus RNA synthesis and assembly are coordinated in intracellular space.
C02	`01`	`X`		`@0 002A05C10`
C03	`01`	`X`	`FRE`	`@0 Arterivirus @2 NW @5 01`
C03	`01`	`X`	`ENG`	`@0 Arterivirus @2 NW @5 01`
C03	`01`	`X`	`SPA`	`@0 Arterivirus @2 NW @5 01`
C03	`02`	`X`	`FRE`	`@0 Réplication @5 05`
C03	`02`	`X`	`ENG`	`@0 Replication @5 05`
C03	`02`	`X`	`SPA`	`@0 Replicación @5 05`
C03	`03`	`X`	`FRE`	`@0 Réticulum endoplasmique @5 06`
C03	`03`	`X`	`ENG`	`@0 Endoplasmic reticulum @5 06`
C03	`03`	`X`	`SPA`	`@0 Retículo endoplásmico @5 06`
C07	`01`	`X`	`FRE`	`@0 Arteriviridae @2 NW`
C07	`01`	`X`	`ENG`	`@0 Arteriviridae @2 NW`
C07	`01`	`X`	`SPA`	`@0 Arteriviridae @2 NW`
C07	`02`	`X`	`FRE`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`ENG`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`SPA`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`03`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`03`	`X`	`SPA`	`@0 Virus @2 NW`
N21				`@1 086`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 12-0114301 INIST
ET :	Ultrastructural Characterization of Arterivirus Replication Structures: Reshaping the Endoplasmic Reticulum To Accommodate Viral RNA Synthesis
AU :	KNOOPS (Kèvin); BARCENA (Montserrat); LIMPENS (Ronald W. A. L.); KOSTER (Abraham J.); MIEKE MOMMAAS (A.); SNIJDER (Eric J.)
AF :	Electron Microscopy Section, Department of Molecular Cell Biology, Leiden University Medical Center/Leiden/Pays-Bas (1 aut., 2 aut., 3 aut., 4 aut., 5 aut.); Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center/Leiden/Pays-Bas (1 aut., 6 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2012; Vol. 86; No. 5; Pp. 2474-2487; Bibl. 67 ref.
LA :	Anglais
EA :	Virus-induced membrane structures support the assembly and function of positive-strand RNA virus replication complexes. The replicase proteins of arteriviruses are associated with double-membrane vesicles (DMVs), which were previously proposed to derive from the endoplasmic reticulum (ER). Using electron tomography, we performed an in-depth ultrastructural analysis of cells infected with the prototypic arterivirus equine arteritis virus (EAV). We established that the outer membranes of EAV-induced DMVs are interconnected with each other and with the ER, thus forming a reticulovesicular network (RVN) resembling that previously described for the distantly related severe acute respiratory syndrome (SARS) coronavirus. Despite significant morphological differences, a striking parallel between the two virus groups, and possibly all members of the order Nidovirales, is the accumulation in the DMV interior of double-stranded RNA, the presumed intermediate of viral RNA synthesis. In our electron tomograms, connections between the DMV interior and cytosol could not be unambiguously identified, suggesting that the double-stranded RNA is compartmentalized by the DMV membranes. As a novel approach to visualize and quantify the RNA content of viral replication structures, we explored electron spectroscopic imaging of DMVs, which revealed the presence of phosphorus in amounts equaling on average a few dozen copies of the EAV RNA genome. Finally, our electron tomograms revealed a network of nucleocapsid protein-containing protein tubules that appears to be intertwined with the RVN. This potential intermediate in nucleocapsid formation, which was not observed in coronavirus-infected cells, suggests that arterivirus RNA synthesis and assembly are coordinated in intracellular space.
CC :	002A05C10
FD :	Arterivirus; Réplication; Réticulum endoplasmique
FG :	Arteriviridae; Nidovirales; Virus
ED :	Arterivirus; Replication; Endoplasmic reticulum
EG :	Arteriviridae; Nidovirales; Virus
SD :	Arterivirus; Replicación; Retículo endoplásmico
LO :	INIST-13592.354000506798780080
ID :	12-0114301

Links to Exploration step

Pascal:12-0114301

Le document en format XML

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<front><div type="abstract" xml:lang="en">Virus-induced membrane structures support the assembly and function of positive-strand RNA virus replication complexes. The replicase proteins of arteriviruses are associated with double-membrane vesicles (DMVs), which were previously proposed to derive from the endoplasmic reticulum (ER). Using electron tomography, we performed an in-depth ultrastructural analysis of cells infected with the prototypic arterivirus equine arteritis virus (EAV). We established that the outer membranes of EAV-induced DMVs are interconnected with each other and with the ER, thus forming a reticulovesicular network (RVN) resembling that previously described for the distantly related severe acute respiratory syndrome (SARS) coronavirus. Despite significant morphological differences, a striking parallel between the two virus groups, and possibly all members of the order Nidovirales, is the accumulation in the DMV interior of double-stranded RNA, the presumed intermediate of viral RNA synthesis. In our electron tomograms, connections between the DMV interior and cytosol could not be unambiguously identified, suggesting that the double-stranded RNA is compartmentalized by the DMV membranes. As a novel approach to visualize and quantify the RNA content of viral replication structures, we explored electron spectroscopic imaging of DMVs, which revealed the presence of phosphorus in amounts equaling on average a few dozen copies of the EAV RNA genome. Finally, our electron tomograms revealed a network of nucleocapsid protein-containing protein tubules that appears to be intertwined with the RVN. This potential intermediate in nucleocapsid formation, which was not observed in coronavirus-infected cells, suggests that arterivirus RNA synthesis and assembly are coordinated in intracellular space.</div>
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<fC01 i1="01" l="ENG"><s0>Virus-induced membrane structures support the assembly and function of positive-strand RNA virus replication complexes. The replicase proteins of arteriviruses are associated with double-membrane vesicles (DMVs), which were previously proposed to derive from the endoplasmic reticulum (ER). Using electron tomography, we performed an in-depth ultrastructural analysis of cells infected with the prototypic arterivirus equine arteritis virus (EAV). We established that the outer membranes of EAV-induced DMVs are interconnected with each other and with the ER, thus forming a reticulovesicular network (RVN) resembling that previously described for the distantly related severe acute respiratory syndrome (SARS) coronavirus. Despite significant morphological differences, a striking parallel between the two virus groups, and possibly all members of the order Nidovirales, is the accumulation in the DMV interior of double-stranded RNA, the presumed intermediate of viral RNA synthesis. In our electron tomograms, connections between the DMV interior and cytosol could not be unambiguously identified, suggesting that the double-stranded RNA is compartmentalized by the DMV membranes. As a novel approach to visualize and quantify the RNA content of viral replication structures, we explored electron spectroscopic imaging of DMVs, which revealed the presence of phosphorus in amounts equaling on average a few dozen copies of the EAV RNA genome. Finally, our electron tomograms revealed a network of nucleocapsid protein-containing protein tubules that appears to be intertwined with the RVN. This potential intermediate in nucleocapsid formation, which was not observed in coronavirus-infected cells, suggests that arterivirus RNA synthesis and assembly are coordinated in intracellular space.</s0>
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</fC03>
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<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Endoplasmic reticulum</s0>
<s5>06</s5>
</fC03>
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<s5>06</s5>
</fC03>
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<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Arteriviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Arteriviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fN21><s1>086</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
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<server><NO>PASCAL 12-0114301 INIST</NO>
<ET>Ultrastructural Characterization of Arterivirus Replication Structures: Reshaping the Endoplasmic Reticulum To Accommodate Viral RNA Synthesis</ET>
<AU>KNOOPS (Kèvin); BARCENA (Montserrat); LIMPENS (Ronald W. A. L.); KOSTER (Abraham J.); MIEKE MOMMAAS (A.); SNIJDER (Eric J.)</AU>
<AF>Electron Microscopy Section, Department of Molecular Cell Biology, Leiden University Medical Center/Leiden/Pays-Bas (1 aut., 2 aut., 3 aut., 4 aut., 5 aut.); Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center/Leiden/Pays-Bas (1 aut., 6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2012; Vol. 86; No. 5; Pp. 2474-2487; Bibl. 67 ref.</SO>
<LA>Anglais</LA>
<EA>Virus-induced membrane structures support the assembly and function of positive-strand RNA virus replication complexes. The replicase proteins of arteriviruses are associated with double-membrane vesicles (DMVs), which were previously proposed to derive from the endoplasmic reticulum (ER). Using electron tomography, we performed an in-depth ultrastructural analysis of cells infected with the prototypic arterivirus equine arteritis virus (EAV). We established that the outer membranes of EAV-induced DMVs are interconnected with each other and with the ER, thus forming a reticulovesicular network (RVN) resembling that previously described for the distantly related severe acute respiratory syndrome (SARS) coronavirus. Despite significant morphological differences, a striking parallel between the two virus groups, and possibly all members of the order Nidovirales, is the accumulation in the DMV interior of double-stranded RNA, the presumed intermediate of viral RNA synthesis. In our electron tomograms, connections between the DMV interior and cytosol could not be unambiguously identified, suggesting that the double-stranded RNA is compartmentalized by the DMV membranes. As a novel approach to visualize and quantify the RNA content of viral replication structures, we explored electron spectroscopic imaging of DMVs, which revealed the presence of phosphorus in amounts equaling on average a few dozen copies of the EAV RNA genome. Finally, our electron tomograms revealed a network of nucleocapsid protein-containing protein tubules that appears to be intertwined with the RVN. This potential intermediate in nucleocapsid formation, which was not observed in coronavirus-infected cells, suggests that arterivirus RNA synthesis and assembly are coordinated in intracellular space.</EA>
<CC>002A05C10</CC>
<FD>Arterivirus; Réplication; Réticulum endoplasmique</FD>
<FG>Arteriviridae; Nidovirales; Virus</FG>
<ED>Arterivirus; Replication; Endoplasmic reticulum</ED>
<EG>Arteriviridae; Nidovirales; Virus</EG>
<SD>Arterivirus; Replicación; Retículo endoplásmico</SD>
<LO>INIST-13592.354000506798780080</LO>
<ID>12-0114301</ID>
</server>
</inist>
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Ultrastructural Characterization of Arterivirus Replication Structures: Reshaping the Endoplasmic Reticulum To Accommodate Viral RNA Synthesis

Ultrastructural Characterization of Arterivirus Replication Structures: Reshaping the Endoplasmic Reticulum To Accommodate Viral RNA Synthesis

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