Synthesis and characterization of a native, oligomeric form of recombinant severe acute respiratory syndrome coronavirus spike glycoprotein
Identifieur interne : 005A59 ( Main/Curation ); précédent : 005A58; suivant : 005A60Synthesis and characterization of a native, oligomeric form of recombinant severe acute respiratory syndrome coronavirus spike glycoprotein
Auteurs : HYUN CHUL SONG [Italie] ; Mi-Young Seo [Italie] ; Konrad Stadler [Italie] ; Byoung J. Yoo [Corée du Sud] ; Qui-Lim Choo [Italie] ; Stephen R. Coates [Italie] ; Yasushi Uematsu [Italie] ; Takashi Harada [Italie] ; Catherine E. Greer [Italie] ; John M. Polo [Italie] ; Piero Pileri [Italie] ; Markus Eickmann [Allemagne] ; Rino Rappuoli [Italie] ; Sergio Abrignani [Italie] ; Michael Houghton [Italie] ; Jang H. Han [Italie]Source :
- Journal of virology [ 0022-538X ] ; 2004.
Descripteurs français
- Pascal (Inist)
English descriptors
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Abstract
We have expressed and characterized the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein in cDNA-transfected mammalian cells. The full-length spike protein (S) was newly synthesized as an endoglycosidase H (endo H)-sensitive glycoprotein (gp170) that is further modified into an endo H-resistant glycoprotein (gp180) in the Golgi apparatus. No substantial proteolytic cleavage of S was observed, suggesting that S is not processed into head (S1) and stalk (S2) domains as observed for certain other coronaviruses. While the expressed full-length S glycoprotein was exclusively cell associated, a truncation of S by excluding the C-terminal transmembrane and cytoplasmic tail domains resulted in the expression of an endoplasmic reticulum-localized glycoprotein (gp160) as well as a Golgi-specific form (gp170) which was ultimately secreted into the cell culture medium. Chemical cross-linking, thermal denaturation, and size fractionation analyses suggested that the full-length S glycoprotein of SARS-CoV forms a higher order structure of ∼500 kDa, which is consistent with it being an S homotrimer. The latter was also observed in purified virions. The intracellular form of the C-terminally truncated S protein (but not the secreted form) also forms trimers, but with much less efficiency than full-length S. Deglycosylation of the full-length homotrimer with peptide N-glycosidase-F under native conditions abolished recognition of the protein by virus-neutralizing antisera raised against purified virions, suggesting the importance of the carbohydrate in the correct folding of the S protein. These data should aid in the design of recombinant vaccine antigens to prevent the spread of this emerging pathogen.
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Pascal:04-0528575Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Synthesis and characterization of a native, oligomeric form of recombinant severe acute respiratory syndrome coronavirus spike glycoprotein</title>
<author><name sortKey="Hyun Chul Song" sort="Hyun Chul Song" uniqKey="Hyun Chul Song" last="Hyun Chul Song">HYUN CHUL SONG</name>
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<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>13 aut.</sZ>
<sZ>14 aut.</sZ>
</inist:fA14>
<country>Italie</country>
<wicri:noRegion>Siena</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Eickmann, Markus" sort="Eickmann, Markus" uniqKey="Eickmann M" first="Markus" last="Eickmann">Markus Eickmann</name>
<affiliation wicri:level="3"><inist:fA14 i1="04"><s1>Institute for Virology, University of Marburg</s1>
<s2>Marburg</s2>
<s3>DEU</s3>
<sZ>12 aut.</sZ>
</inist:fA14>
<country>Allemagne</country>
<placeName><region type="land" nuts="1">Hesse (Land)</region>
<region type="district" nuts="2">District de Giessen</region>
<settlement type="city">Marbourg</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Rappuoli, Rino" sort="Rappuoli, Rino" uniqKey="Rappuoli R" first="Rino" last="Rappuoli">Rino Rappuoli</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Vaccines Research, Chiron Corporation</s1>
<s2>Emeryville, California</s2>
<s3>ITA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
<sZ>13 aut.</sZ>
<sZ>15 aut.</sZ>
<sZ>16 aut.</sZ>
</inist:fA14>
<country>Italie</country>
<wicri:noRegion>Emeryville, California</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><inist:fA14 i1="02"><s1>IRIS, Chiron Vaccines</s1>
<s2>Siena</s2>
<s3>ITA</s3>
<sZ>3 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>13 aut.</sZ>
<sZ>14 aut.</sZ>
</inist:fA14>
<country>Italie</country>
<wicri:noRegion>Siena</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Abrignani, Sergio" sort="Abrignani, Sergio" uniqKey="Abrignani S" first="Sergio" last="Abrignani">Sergio Abrignani</name>
<affiliation wicri:level="1"><inist:fA14 i1="02"><s1>IRIS, Chiron Vaccines</s1>
<s2>Siena</s2>
<s3>ITA</s3>
<sZ>3 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>13 aut.</sZ>
<sZ>14 aut.</sZ>
</inist:fA14>
<country>Italie</country>
<wicri:noRegion>Siena</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Houghton, Michael" sort="Houghton, Michael" uniqKey="Houghton M" first="Michael" last="Houghton">Michael Houghton</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Vaccines Research, Chiron Corporation</s1>
<s2>Emeryville, California</s2>
<s3>ITA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
<sZ>13 aut.</sZ>
<sZ>15 aut.</sZ>
<sZ>16 aut.</sZ>
</inist:fA14>
<country>Italie</country>
<wicri:noRegion>Emeryville, California</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Han, Jang H" sort="Han, Jang H" uniqKey="Han J" first="Jang H." last="Han">Jang H. Han</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Vaccines Research, Chiron Corporation</s1>
<s2>Emeryville, California</s2>
<s3>ITA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
<sZ>13 aut.</sZ>
<sZ>15 aut.</sZ>
<sZ>16 aut.</sZ>
</inist:fA14>
<country>Italie</country>
<wicri:noRegion>Emeryville, California</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="2004">2004</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>Acute</term>
<term>Characterization</term>
<term>Coronavirus</term>
<term>Critically ill</term>
<term>Glycoprotein</term>
<term>Microbiology</term>
<term>Oligomerization</term>
<term>Respiratory tract</term>
<term>Severe</term>
<term>Severe acute respiratory syndrome</term>
<term>Synthesis</term>
<term>Virology</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term>
<term>Synthèse</term>
<term>Caractérisation</term>
<term>Oligomérisation</term>
<term>Grave</term>
<term>Malade état grave</term>
<term>Aigu</term>
<term>Voie respiratoire</term>
<term>Glycoprotéine</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Microbiologie</term>
<term>Virologie</term>
<term>Forme grave</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">We have expressed and characterized the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein in cDNA-transfected mammalian cells. The full-length spike protein (S) was newly synthesized as an endoglycosidase H (endo H)-sensitive glycoprotein (gp170) that is further modified into an endo H-resistant glycoprotein (gp180) in the Golgi apparatus. No substantial proteolytic cleavage of S was observed, suggesting that S is not processed into head (S1) and stalk (S2) domains as observed for certain other coronaviruses. While the expressed full-length S glycoprotein was exclusively cell associated, a truncation of S by excluding the C-terminal transmembrane and cytoplasmic tail domains resulted in the expression of an endoplasmic reticulum-localized glycoprotein (gp160) as well as a Golgi-specific form (gp170) which was ultimately secreted into the cell culture medium. Chemical cross-linking, thermal denaturation, and size fractionation analyses suggested that the full-length S glycoprotein of SARS-CoV forms a higher order structure of ∼500 kDa, which is consistent with it being an S homotrimer. The latter was also observed in purified virions. The intracellular form of the C-terminally truncated S protein (but not the secreted form) also forms trimers, but with much less efficiency than full-length S. Deglycosylation of the full-length homotrimer with peptide N-glycosidase-F under native conditions abolished recognition of the protein by virus-neutralizing antisera raised against purified virions, suggesting the importance of the carbohydrate in the correct folding of the S protein. These data should aid in the design of recombinant vaccine antigens to prevent the spread of this emerging pathogen.</div>
</front>
</TEI>
</record>
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