Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
Identifieur interne : 000464 ( PascalFrancis/Checkpoint ); précédent : 000463; suivant : 000465Important 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
- Pascal (Inist)
English descriptors
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.
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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>Coronavirus</term><term>Microbiology</term><term>Protein</term><term>Severe acute respiratory syndrome</term><term>Virology</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term><term>Protéine</term><term>Microbiologie</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><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>80</s2></fA05><fA06><s2>3</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry</s1></fA08><fA11 i1="01" i2="1"><s1>BROER (Rene)</s1></fA11><fA11 i1="02" i2="1"><s1>BOSON (Bertrand)</s1></fA11><fA11 i1="03" i2="1"><s1>SPAAN (Willy)</s1></fA11><fA11 i1="04" i2="1"><s1>COSSET (Francois-Loïc)</s1></fA11><fA11 i1="05" i2="1"><s1>CORVER (Jeroen)</s1></fA11><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></fA14><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></fA14><fA20><s1>1302-1310</s1></fA20><fA21><s1>2006</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>13592</s2><s5>354000132908470240</s5></fA43><fA44><s0>0000</s0><s1>© 2006 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>52 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>06-0108274</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 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.</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>Protéine</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Protein</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Proteína</s0><s5>05</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Microbiologie</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Microbiology</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Microbiología</s0><s5>06</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Virologie</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Virology</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Virología</s0><s5>07</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0><s2>NM</s2><s5>14</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><fC07 i1="04" i2="X" l="FRE"><s0>Appareil respiratoire pathologie</s0><s5>13</s5></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Respiratory disease</s0><s5>13</s5></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0><s5>13</s5></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Virose</s0></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Viral disease</s0></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Virosis</s0></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Infection</s0></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Infection</s0></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Infección</s0></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Poumon pathologie</s0><s5>16</s5></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Lung disease</s0><s5>16</s5></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Pulmón patología</s0><s5>16</s5></fC07><fN21><s1>065</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard></inist><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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