SrasV1, PascalFrancis, Corpus, bibRecord, 000327

Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication

Identifieur interne : 000327 ( PascalFrancis/Corpus ); précédent : 000326; suivant : 000328

Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication

Auteurs : M. Oostra ; E. G. Te Lintelo ; M. Deijs ; M. H. Verheije ; P. J. M. Rottier ; C. A. M. De Haan

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : Pascal:07-0517267

Descripteurs français

Pascal (Inist)
- Coronavirus, Localisation, Protéine membranaire, Réplication, Virologie.

English descriptors

KwdEn :
- Coronavirus, Localization, Membrane protein, Replication, Virology.

Abstract

The coronavirus nonstructural proteins (nsp's) derived from the replicase polyproteins collectively constitute the viral replication complexes, which are anchored to double-membrane vesicles. Little is known about the biogenesis of these complexes, the membrane anchoring of which is probably mediated by nsp3, nsp4, and nsp6, as they contain several putative transmembrane domains. As a first step to getting more insight into the formation of the coronavirus replication complex, the membrane topology, processing, and subcellular localization of nsp4 of the mouse hepatitis virus (MHV) and severe acute respiratory syndrome-associated coronavirus (SARS-CoV) were elucidated in this study. Both nsp4 proteins became N glycosylated, while their amino and carboxy termini were localized to the cytoplasm. These observations imply nsp4 to assemble in the membrane as a tetraspanning transmembrane protein with a Nendo/Cendo topology. The amino terminus of SARS-CoV nsp4, but not that of MHV nsp4, was shown to be (partially) processed by signal peptidase. nsp4 localized to the endoplasmic reticulum (ER) when expressed alone but was recruited to the replication complexes in infected cells, nsp4 present in these complexes did not colocalize with markers of the ER or Golgi apparatus, while the susceptibility of its sugars to endoglycosidase H indicated that the protein had also not traveled trough the latter compartment. The important role of the early secretory pathway in formation of the replication complexes was also demonstrated by the inhibition of coronaviral replication when the ER export machinery was blocked by use of the kinase inhibitor H89 or by expression of a mutant, Sarl[H79G].

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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A08	`01`	`1`	`ENG`	`@1 Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication`
A11	`01`	`1`		`@1 OOSTRA (M.)`
A11	`02`	`1`		`@1 TE LINTELO (E. G.)`
A11	`03`	`1`		`@1 DEIJS (M.)`
A11	`04`	`1`		`@1 VERHEIJE (M. H.)`
A11	`05`	`1`		`@1 ROTTIER (P. J. M.)`
A11	`06`	`1`		`@1 DE HAAN (C. A. M.)`
A14	`01`			`@1 Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1 @2 3584 CL Utrecht @3 NLD @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut. @Z 6 aut.`
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A21				`@1 2007`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 13592 @5 354000173476840230`
A44				`@0 0000 @1 © 2007 INIST-CNRS. All rights reserved.`
A45				`@0 74 ref.`
A47	`01`	`1`		`@0 07-0517267`
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A64	`01`	`1`		`@0 Journal of virology`
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C01	`01`		`ENG`	@0 The coronavirus nonstructural proteins (nsp's) derived from the replicase polyproteins collectively constitute the viral replication complexes, which are anchored to double-membrane vesicles. Little is known about the biogenesis of these complexes, the membrane anchoring of which is probably mediated by nsp3, nsp4, and nsp6, as they contain several putative transmembrane domains. As a first step to getting more insight into the formation of the coronavirus replication complex, the membrane topology, processing, and subcellular localization of nsp4 of the mouse hepatitis virus (MHV) and severe acute respiratory syndrome-associated coronavirus (SARS-CoV) were elucidated in this study. Both nsp4 proteins became N glycosylated, while their amino and carboxy termini were localized to the cytoplasm. These observations imply nsp4 to assemble in the membrane as a tetraspanning transmembrane protein with a Nendo/Cendo topology. The amino terminus of SARS-CoV nsp4, but not that of MHV nsp4, was shown to be (partially) processed by signal peptidase. nsp4 localized to the endoplasmic reticulum (ER) when expressed alone but was recruited to the replication complexes in infected cells, nsp4 present in these complexes did not colocalize with markers of the ER or Golgi apparatus, while the susceptibility of its sugars to endoglycosidase H indicated that the protein had also not traveled trough the latter compartment. The important role of the early secretory pathway in formation of the replication complexes was also demonstrated by the inhibition of coronaviral replication when the ER export machinery was blocked by use of the kinase inhibitor H89 or by expression of a mutant, Sarl[H79G].
C02	`01`	`X`		`@0 002A05C10`
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C03	`01`	`X`	`ENG`	`@0 Coronavirus @2 NW @5 01`
C03	`01`	`X`	`SPA`	`@0 Coronavirus @2 NW @5 01`
C03	`02`	`X`	`FRE`	`@0 Localisation @5 05`
C03	`02`	`X`	`ENG`	`@0 Localization @5 05`
C03	`02`	`X`	`SPA`	`@0 Localización @5 05`
C03	`03`	`X`	`FRE`	`@0 Protéine membranaire @5 06`
C03	`03`	`X`	`ENG`	`@0 Membrane protein @5 06`
C03	`03`	`X`	`SPA`	`@0 Proteína membranar @5 06`
C03	`04`	`X`	`FRE`	`@0 Réplication @5 07`
C03	`04`	`X`	`ENG`	`@0 Replication @5 07`
C03	`04`	`X`	`SPA`	`@0 Replicación @5 07`
C03	`05`	`X`	`FRE`	`@0 Virologie @5 08`
C03	`05`	`X`	`ENG`	`@0 Virology @5 08`
C03	`05`	`X`	`SPA`	`@0 Virología @5 08`
C07	`01`	`X`	`FRE`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`SPA`	`@0 Coronaviridae @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				`@1 337`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 07-0517267 INIST
ET :	Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication
AU :	OOSTRA (M.); TE LINTELO (E. G.); DEIJS (M.); VERHEIJE (M. H.); ROTTIER (P. J. M.); DE HAAN (C. A. M.)
AF :	Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1/3584 CL Utrecht/Pays-Bas (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 6 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 22; Pp. 12323-12336; Bibl. 74 ref.
LA :	Anglais
EA :	The coronavirus nonstructural proteins (nsp's) derived from the replicase polyproteins collectively constitute the viral replication complexes, which are anchored to double-membrane vesicles. Little is known about the biogenesis of these complexes, the membrane anchoring of which is probably mediated by nsp3, nsp4, and nsp6, as they contain several putative transmembrane domains. As a first step to getting more insight into the formation of the coronavirus replication complex, the membrane topology, processing, and subcellular localization of nsp4 of the mouse hepatitis virus (MHV) and severe acute respiratory syndrome-associated coronavirus (SARS-CoV) were elucidated in this study. Both nsp4 proteins became N glycosylated, while their amino and carboxy termini were localized to the cytoplasm. These observations imply nsp4 to assemble in the membrane as a tetraspanning transmembrane protein with a Nendo/Cendo topology. The amino terminus of SARS-CoV nsp4, but not that of MHV nsp4, was shown to be (partially) processed by signal peptidase. nsp4 localized to the endoplasmic reticulum (ER) when expressed alone but was recruited to the replication complexes in infected cells, nsp4 present in these complexes did not colocalize with markers of the ER or Golgi apparatus, while the susceptibility of its sugars to endoglycosidase H indicated that the protein had also not traveled trough the latter compartment. The important role of the early secretory pathway in formation of the replication complexes was also demonstrated by the inhibition of coronaviral replication when the ER export machinery was blocked by use of the kinase inhibitor H89 or by expression of a mutant, Sarl[H79G].
CC :	002A05C10
FD :	Coronavirus; Localisation; Protéine membranaire; Réplication; Virologie
FG :	Coronaviridae; Nidovirales; Virus
ED :	Coronavirus; Localization; Membrane protein; Replication; Virology
EG :	Coronaviridae; Nidovirales; Virus
SD :	Coronavirus; Localización; Proteína membranar; Replicación; Virología
LO :	INIST-13592.354000173476840230
ID :	07-0517267

Links to Exploration step

Pascal:07-0517267

Le document en format XML

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<front><div type="abstract" xml:lang="en">The coronavirus nonstructural proteins (nsp's) derived from the replicase polyproteins collectively constitute the viral replication complexes, which are anchored to double-membrane vesicles. Little is known about the biogenesis of these complexes, the membrane anchoring of which is probably mediated by nsp3, nsp4, and nsp6, as they contain several putative transmembrane domains. As a first step to getting more insight into the formation of the coronavirus replication complex, the membrane topology, processing, and subcellular localization of nsp4 of the mouse hepatitis virus (MHV) and severe acute respiratory syndrome-associated coronavirus (SARS-CoV) were elucidated in this study. Both nsp4 proteins became N glycosylated, while their amino and carboxy termini were localized to the cytoplasm. These observations imply nsp4 to assemble in the membrane as a tetraspanning transmembrane protein with a Nendo/Cendo topology. The amino terminus of SARS-CoV nsp4, but not that of MHV nsp4, was shown to be (partially) processed by signal peptidase. nsp4 localized to the endoplasmic reticulum (ER) when expressed alone but was recruited to the replication complexes in infected cells, nsp4 present in these complexes did not colocalize with markers of the ER or Golgi apparatus, while the susceptibility of its sugars to endoglycosidase H indicated that the protein had also not traveled trough the latter compartment. The important role of the early secretory pathway in formation of the replication complexes was also demonstrated by the inhibition of coronaviral replication when the ER export machinery was blocked by use of the kinase inhibitor H89 or by expression of a mutant, Sarl[H79G].</div>
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<fC01 i1="01" l="ENG"><s0>The coronavirus nonstructural proteins (nsp's) derived from the replicase polyproteins collectively constitute the viral replication complexes, which are anchored to double-membrane vesicles. Little is known about the biogenesis of these complexes, the membrane anchoring of which is probably mediated by nsp3, nsp4, and nsp6, as they contain several putative transmembrane domains. As a first step to getting more insight into the formation of the coronavirus replication complex, the membrane topology, processing, and subcellular localization of nsp4 of the mouse hepatitis virus (MHV) and severe acute respiratory syndrome-associated coronavirus (SARS-CoV) were elucidated in this study. Both nsp4 proteins became N glycosylated, while their amino and carboxy termini were localized to the cytoplasm. These observations imply nsp4 to assemble in the membrane as a tetraspanning transmembrane protein with a Nendo/Cendo topology. The amino terminus of SARS-CoV nsp4, but not that of MHV nsp4, was shown to be (partially) processed by signal peptidase. nsp4 localized to the endoplasmic reticulum (ER) when expressed alone but was recruited to the replication complexes in infected cells, nsp4 present in these complexes did not colocalize with markers of the ER or Golgi apparatus, while the susceptibility of its sugars to endoglycosidase H indicated that the protein had also not traveled trough the latter compartment. The important role of the early secretory pathway in formation of the replication complexes was also demonstrated by the inhibition of coronaviral replication when the ER export machinery was blocked by use of the kinase inhibitor H89 or by expression of a mutant, Sarl[H79G].</s0>
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<server><NO>PASCAL 07-0517267 INIST</NO>
<ET>Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication</ET>
<AU>OOSTRA (M.); TE LINTELO (E. G.); DEIJS (M.); VERHEIJE (M. H.); ROTTIER (P. J. M.); DE HAAN (C. A. M.)</AU>
<AF>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1/3584 CL Utrecht/Pays-Bas (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 22; Pp. 12323-12336; Bibl. 74 ref.</SO>
<LA>Anglais</LA>
<EA>The coronavirus nonstructural proteins (nsp's) derived from the replicase polyproteins collectively constitute the viral replication complexes, which are anchored to double-membrane vesicles. Little is known about the biogenesis of these complexes, the membrane anchoring of which is probably mediated by nsp3, nsp4, and nsp6, as they contain several putative transmembrane domains. As a first step to getting more insight into the formation of the coronavirus replication complex, the membrane topology, processing, and subcellular localization of nsp4 of the mouse hepatitis virus (MHV) and severe acute respiratory syndrome-associated coronavirus (SARS-CoV) were elucidated in this study. Both nsp4 proteins became N glycosylated, while their amino and carboxy termini were localized to the cytoplasm. These observations imply nsp4 to assemble in the membrane as a tetraspanning transmembrane protein with a Nendo/Cendo topology. The amino terminus of SARS-CoV nsp4, but not that of MHV nsp4, was shown to be (partially) processed by signal peptidase. nsp4 localized to the endoplasmic reticulum (ER) when expressed alone but was recruited to the replication complexes in infected cells, nsp4 present in these complexes did not colocalize with markers of the ER or Golgi apparatus, while the susceptibility of its sugars to endoglycosidase H indicated that the protein had also not traveled trough the latter compartment. The important role of the early secretory pathway in formation of the replication complexes was also demonstrated by the inhibition of coronaviral replication when the ER export machinery was blocked by use of the kinase inhibitor H89 or by expression of a mutant, Sarl[H79G].</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Localisation; Protéine membranaire; Réplication; Virologie</FD>
<FG>Coronaviridae; Nidovirales; Virus</FG>
<ED>Coronavirus; Localization; Membrane protein; Replication; Virology</ED>
<EG>Coronaviridae; Nidovirales; Virus</EG>
<SD>Coronavirus; Localización; Proteína membranar; Replicación; Virología</SD>
<LO>INIST-13592.354000173476840230</LO>
<ID>07-0517267</ID>
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Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication

Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication

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