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 : 000328Localization 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 HaanSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
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.
pA |
|
---|
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:07-0517267Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en" level="a">Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication</title>
<author><name sortKey="Oostra, M" sort="Oostra, M" uniqKey="Oostra M" first="M." last="Oostra">M. Oostra</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Te Lintelo, E G" sort="Te Lintelo, E G" uniqKey="Te Lintelo E" first="E. G." last="Te Lintelo">E. G. Te Lintelo</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Deijs, M" sort="Deijs, M" uniqKey="Deijs M" first="M." last="Deijs">M. Deijs</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Verheije, M H" sort="Verheije, M H" uniqKey="Verheije M" first="M. H." last="Verheije">M. H. Verheije</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Rottier, P J M" sort="Rottier, P J M" uniqKey="Rottier P" first="P. J. M." last="Rottier">P. J. M. Rottier</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="De Haan, C A M" sort="De Haan, C A M" uniqKey="De Haan C" first="C. A. M." last="De Haan">C. A. M. De Haan</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">INIST</idno>
<idno type="inist">07-0517267</idno>
<date when="2007">2007</date>
<idno type="stanalyst">PASCAL 07-0517267 INIST</idno>
<idno type="RBID">Pascal:07-0517267</idno>
<idno type="wicri:Area/PascalFrancis/Corpus">000327</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication</title>
<author><name sortKey="Oostra, M" sort="Oostra, M" uniqKey="Oostra M" first="M." last="Oostra">M. Oostra</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Te Lintelo, E G" sort="Te Lintelo, E G" uniqKey="Te Lintelo E" first="E. G." last="Te Lintelo">E. G. Te Lintelo</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Deijs, M" sort="Deijs, M" uniqKey="Deijs M" first="M." last="Deijs">M. Deijs</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Verheije, M H" sort="Verheije, M H" uniqKey="Verheije M" first="M. H." last="Verheije">M. H. Verheije</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Rottier, P J M" sort="Rottier, P J M" uniqKey="Rottier P" first="P. J. M." last="Rottier">P. J. M. Rottier</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="De Haan, C A M" sort="De Haan, C A M" uniqKey="De Haan C" first="C. A. M." last="De Haan">C. A. M. De Haan</name>
<affiliation><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date when="2007">2007</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term>
<term>Localization</term>
<term>Membrane protein</term>
<term>Replication</term>
<term>Virology</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term>
<term>Localisation</term>
<term>Protéine membranaire</term>
<term>Réplication</term>
<term>Virologie</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
<inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0022-538X</s0>
</fA01>
<fA03 i2="1"><s0>J. virol.</s0>
</fA03>
<fA05><s2>81</s2>
</fA05>
<fA06><s2>22</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>OOSTRA (M.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>TE LINTELO (E. G.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>DEIJS (M.)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>VERHEIJE (M. H.)</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>ROTTIER (P. J. M.)</s1>
</fA11>
<fA11 i1="06" i2="1"><s1>DE HAAN (C. A. M.)</s1>
</fA11>
<fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</fA14>
<fA20><s1>12323-12336</s1>
</fA20>
<fA21><s1>2007</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>13592</s2>
<s5>354000173476840230</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2007 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>74 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>07-0517267</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Journal of virology</s0>
</fA64>
<fA66 i1="01"><s0>USA</s0>
</fA66>
<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>
</fC01>
<fC02 i1="01" i2="X"><s0>002A05C10</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Localisation</s0>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Localization</s0>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Localización</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Protéine membranaire</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Membrane protein</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Proteína membranar</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Réplication</s0>
<s5>07</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Replication</s0>
<s5>07</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Replicación</s0>
<s5>07</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Virologie</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Virology</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Virología</s0>
<s5>08</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Coronaviridae</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>337</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<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>
</server>
</inist>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PascalFrancis/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000327 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PascalFrancis/Corpus/biblio.hfd -nk 000327 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= PascalFrancis |étape= Corpus |type= RBID |clé= Pascal:07-0517267 |texte= Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication }}
![]() | This area was generated with Dilib version V0.6.33. | ![]() |