Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
Identifieur interne : 000327 ( France/Analysis ); précédent : 000326; suivant : 000328Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
Auteurs : Rene Broer [Pays-Bas] ; Bertrand Boson [France] ; Willy Spaan [Pays-Bas] ; Francois-Loïc Cosset [France] ; Jeroen Corver [Pays-Bas]Source :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- ADN viral (génétique), Animaux, Cellules Vero, Données de séquences moléculaires, Fusion membranaire (physiologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (physiologie), Humains, Lignée cellulaire, Luciférases de Renilla (génétique), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (physiologie), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (physiologie), Récepteurs viraux (génétique), Structure quaternaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Séquence nucléotidique, Virus du SRAS (génétique), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie).
- MESH :
- génétique : ADN viral, Glycoprotéines membranaires, Luciférases de Renilla, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- pathogénicité : Virus du SRAS.
- physiologie : Fusion membranaire, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Virus du SRAS.
- Pascal (Inist)
- Animaux, Cellules Vero, Coronavirus, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Lignée cellulaire, Protéine, Microbiologie, Protéines de l'enveloppe virale, Structure quaternaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Séquence nucléotidique, Virologie, Syndrome respiratoire aigu sévère.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Chlorocebus aethiops, Coronavirus, DNA, Viral (genetics), Humans, Luciferases, Renilla (genetics), Membrane Fusion (physiology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Microbiology, Molecular Sequence Data, Protein, Protein Structure, Quaternary, Protein Structure, Tertiary, Receptors, Virus (genetics), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (physiology), SARS Virus (genetics), SARS Virus (pathogenicity), SARS Virus (physiology), Severe acute respiratory syndrome, Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology), Virology.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : DNA, Viral, Luciferases, Renilla, Membrane Glycoproteins, Receptors, Virus, Recombinant Fusion Proteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- pathogenicity : SARS Virus.
- physiology : Membrane Fusion, Membrane Glycoproteins, Recombinant Fusion Proteins, SARS Virus, Viral Envelope Proteins.
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Chlorocebus aethiops, Humans, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Vero Cells.
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. SVSV-Cyt, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and SMBV-TMDCyt, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. SVSV-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 SVSV-TMDCyt trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.
Affiliations:
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Pascal:06-0108274Le document en format XML
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Infectious Diseases, Leiden University Medical Center</s1><s2>2300 RC Leiden</s2><s3>NLD</s3><sZ>1 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Pays-Bas</country><wicri:noRegion>2300 RC Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Boson, Bertrand" sort="Boson, Bertrand" uniqKey="Boson B" first="Bertrand" last="Boson">Bertrand Boson</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Laboratoire de Vectorologie Rétrovirale et Thérapie Génique, INSERM U412, IFR128 BioSciences Lyon-Gerland, Ecole Normale Supérieure de Lyon, 46 allée d'Italie</s1><s2>69364 Lyon</s2><s3>FRA</s3><sZ>2 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Lyon</settlement></placeName></affiliation></author><author><name sortKey="Spaan, Willy" sort="Spaan, Willy" uniqKey="Spaan W" first="Willy" last="Spaan">Willy Spaan</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center</s1><s2>2300 RC Leiden</s2><s3>NLD</s3><sZ>1 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Pays-Bas</country><wicri:noRegion>2300 RC Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Cosset, Francois Loic" sort="Cosset, Francois Loic" uniqKey="Cosset F" first="Francois-Loïc" last="Cosset">Francois-Loïc Cosset</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Laboratoire de Vectorologie Rétrovirale et Thérapie Génique, INSERM U412, IFR128 BioSciences Lyon-Gerland, Ecole Normale Supérieure de Lyon, 46 allée d'Italie</s1><s2>69364 Lyon</s2><s3>FRA</s3><sZ>2 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Lyon</settlement></placeName></affiliation></author><author><name sortKey="Corver, Jeroen" sort="Corver, Jeroen" uniqKey="Corver J" first="Jeroen" last="Corver">Jeroen Corver</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center</s1><s2>2300 RC Leiden</s2><s3>NLD</s3><sZ>1 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Pays-Bas</country><wicri:noRegion>2300 RC Leiden</wicri:noRegion></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="2006">2006</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>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Coronavirus</term><term>DNA, Viral (genetics)</term><term>Humans</term><term>Luciferases, Renilla (genetics)</term><term>Membrane Fusion (physiology)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (physiology)</term><term>Microbiology</term><term>Molecular Sequence Data</term><term>Protein</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Receptors, Virus (genetics)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (physiology)</term><term>SARS Virus (genetics)</term><term>SARS Virus (pathogenicity)</term><term>SARS Virus (physiology)</term><term>Severe acute respiratory syndrome</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (physiology)</term><term>Virology</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN viral (génétique)</term><term>Animaux</term><term>Cellules Vero</term><term>Données de séquences moléculaires</term><term>Fusion membranaire (physiologie)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (physiologie)</term><term>Humains</term><term>Lignée cellulaire</term><term>Luciférases de Renilla (génétique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (physiologie)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (physiologie)</term><term>Récepteurs viraux (génétique)</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (pathogénicité)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Viral</term><term>Luciferases, Renilla</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN viral</term><term>Glycoprotéines membranaires</term><term>Luciférases de Renilla</term><term>Protéines de fusion recombinantes</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Fusion membranaire</term><term>Glycoprotéines membranaires</term><term>Protéines de fusion recombinantes</term><term>Protéines de l'enveloppe virale</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Membrane Fusion</term><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>SARS Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Coronavirus</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéine</term><term>Microbiologie</term><term>Protéines de l'enveloppe virale</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>France</li><li>Pays-Bas</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Lyon</li></settlement></list><tree><country name="Pays-Bas"><noRegion><name sortKey="Broer, Rene" sort="Broer, Rene" uniqKey="Broer R" first="Rene" last="Broer">Rene Broer</name></noRegion><name sortKey="Corver, Jeroen" sort="Corver, Jeroen" uniqKey="Corver J" first="Jeroen" last="Corver">Jeroen Corver</name><name sortKey="Spaan, Willy" sort="Spaan, Willy" uniqKey="Spaan W" first="Willy" last="Spaan">Willy Spaan</name></country><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Boson, Bertrand" sort="Boson, Bertrand" uniqKey="Boson B" first="Bertrand" last="Boson">Bertrand Boson</name></region><name sortKey="Cosset, Francois Loic" sort="Cosset, Francois Loic" uniqKey="Cosset F" first="Francois-Loïc" last="Cosset">Francois-Loïc Cosset</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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