SrasV1, PascalFrancis, Corpus, bibRecord, 000548

Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry

Identifieur interne : 000548 ( PascalFrancis/Corpus ); précédent : 000547; suivant : 000549

Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry

Auteurs : Rene Broer ; Bertrand Boson ; Willy Spaan ; Francois-Loïc Cosset ; Jeroen Corver

Source :

Journal of virology [ 0022-538X ] ; 2006.

RBID : Pascal:06-0108274

Descripteurs français

Pascal (Inist)
- Coronavirus, Protéine, Microbiologie, Virologie, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Microbiology, Protein, Severe acute respiratory syndrome, Virology.

Abstract

The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. S_VSV-Cyt, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and S_MBV-TMDCyt, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. S_VSV-TMDCry, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that S_VSV-TMDCyt trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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Format Inist (serveur)

NO :	PASCAL 06-0108274 INIST
ET :	Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
AU :	BROER (Rene); BOSON (Bertrand); SPAAN (Willy); COSSET (Francois-Loïc); CORVER (Jeroen)
AF :	Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center/2300 RC Leiden/Pays-Bas (1 aut., 3 aut., 5 aut.); Laboratoire de Vectorologie Rétrovirale et Thérapie Génique, INSERM U412, IFR128 BioSciences Lyon-Gerland, Ecole Normale Supérieure de Lyon, 46 allée d'Italie/69364 Lyon/France (2 aut., 4 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 3; Pp. 1302-1310; Bibl. 52 ref.
LA :	Anglais
EA :	The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. S_VSV-Cyt, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and S_MBV-TMDCyt, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. S_VSV-TMDCry, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that S_VSV-TMDCyt trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.
CC :	002A05C10
FD :	Coronavirus; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère
FG :	Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie
ED :	Coronavirus; Protein; Microbiology; Virology; Severe acute respiratory syndrome
EG :	Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease
SD :	Coronavirus; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo
LO :	INIST-13592.354000132908470240
ID :	06-0108274

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Pascal:06-0108274

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<front><div type="abstract" xml:lang="en">The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. S<sub>VSV-Cyt</sub>
, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and S<sub>MBV-TMDCyt</sub>
, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. S<sub>VSV-TMDCry</sub>
, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that S<sub>VSV-TMDCyt</sub>
 trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.</div>
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<fC01 i1="01" l="ENG"><s0>The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. S<sub>VSV-Cyt</sub>
, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and S<sub>MBV-TMDCyt</sub>
, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. S<sub>VSV-TMDCry</sub>
, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that S<sub>VSV-TMDCyt</sub>
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<server><NO>PASCAL 06-0108274 INIST</NO>
<ET>Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry</ET>
<AU>BROER (Rene); BOSON (Bertrand); SPAAN (Willy); COSSET (Francois-Loïc); CORVER (Jeroen)</AU>
<AF>Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center/2300 RC Leiden/Pays-Bas (1 aut., 3 aut., 5 aut.); Laboratoire de Vectorologie Rétrovirale et Thérapie Génique, INSERM U412, IFR128 BioSciences Lyon-Gerland, Ecole Normale Supérieure de Lyon, 46 allée d'Italie/69364 Lyon/France (2 aut., 4 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 3; Pp. 1302-1310; Bibl. 52 ref.</SO>
<LA>Anglais</LA>
<EA>The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. S<sub>VSV-Cyt</sub>
, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and S<sub>MBV-TMDCyt</sub>
, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. S<sub>VSV-TMDCry</sub>
, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that S<sub>VSV-TMDCyt</sub>
 trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère</FD>
<FG>Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie</FG>
<ED>Coronavirus; Protein; Microbiology; Virology; Severe acute respiratory syndrome</ED>
<EG>Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease</EG>
<SD>Coronavirus; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo</SD>
<LO>INIST-13592.354000132908470240</LO>
<ID>06-0108274</ID>
</server>
</inist>
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Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry

Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry

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