Synthesis and Characterization of a Native, Oligomeric Form of Recombinant Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein
Identifieur interne : 001458 ( Pmc/Checkpoint ); précédent : 001457; suivant : 001459Synthesis and Characterization of a Native, Oligomeric Form of Recombinant Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein
Auteurs : Hyun Chul Song ; Mi-Young Seo ; Konrad Stadler ; Byoung J. Yoo ; Qui-Lim Choo ; Stephen R. Coates ; Yasushi Uematsu ; Takashi Harada ; Catherine E. Greer ; John M. Polo ; Piero Pileri ; Markus Eickmann ; Rino Rappuoli ; Sergio Abrignani ; Michael Houghton ; Jang H. HanSource :
- Journal of Virology [ 0022-538X ] ; 2004.
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
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DOI: 10.1128/JVI.78.19.10328-10335.2004
PubMed: 15367599
PubMed Central: 516425
Affiliations:
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<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
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<front><div type="abstract" xml:lang="en"><p>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 <italic>N-</italic>
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.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id>
<journal-id journal-id-type="publisher-id">jvi</journal-id>
<journal-title>Journal of Virology</journal-title>
<issn pub-type="ppub">0022-538X</issn>
<issn pub-type="epub">1098-5514</issn>
<publisher><publisher-name>American Society for Microbiology</publisher-name>
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<article-meta><article-id pub-id-type="pmid">15367599</article-id>
<article-id pub-id-type="pmc">516425</article-id>
<article-id pub-id-type="publisher-id">0737-04</article-id>
<article-id pub-id-type="doi">10.1128/JVI.78.19.10328-10335.2004</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Structure and Assembly</subject>
</subj-group>
</article-categories>
<title-group><article-title>Synthesis and Characterization of a Native, Oligomeric Form of Recombinant Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Song</surname>
<given-names>Hyun Chul</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Seo</surname>
<given-names>Mi-Young</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Stadler</surname>
<given-names>Konrad</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Yoo</surname>
<given-names>Byoung J.</given-names>
</name>
<xref ref-type="aff" rid="aff1">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Choo</surname>
<given-names>Qui-Lim</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Coates</surname>
<given-names>Stephen R.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Uematsu</surname>
<given-names>Yasushi</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Harada</surname>
<given-names>Takashi</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Greer</surname>
<given-names>Catherine E.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Polo</surname>
<given-names>John M.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Pileri</surname>
<given-names>Piero</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Eickmann</surname>
<given-names>Markus</given-names>
</name>
<xref ref-type="aff" rid="aff1">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Rappuoli</surname>
<given-names>Rino</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Abrignani</surname>
<given-names>Sergio</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Houghton</surname>
<given-names>Michael</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Han</surname>
<given-names>Jang H.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="corresp" rid="cor1">*</xref>
</contrib>
</contrib-group>
<aff id="aff1">Vaccines Research, Chiron Corporation, Emeryville, California,<label>1</label>
IRIS, Chiron Vaccines, Siena, Italy,<label>2</label>
Division of Natural Sciences, Daegu University, Kyungbuk, Korea,<label>3</label>
Institute for Virology, University of Marburg, Marburg, Germany<label>4</label>
</aff>
<author-notes><fn id="cor1"><label>*</label>
<p>Corresponding author. Mailing address: Vaccines Research, Chiron Corporation, 4560 Horton St., Emeryville, CA 94608. Phone: (510) 923-2937. Fax: (510) 923-2586. E-mail: <email>jang_han@chiron.com</email>
.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>10</month>
<year>2004</year>
</pub-date>
<volume>78</volume>
<issue>19</issue>
<fpage>10328</fpage>
<lpage>10335</lpage>
<history><date date-type="received"><day>30</day>
<month>3</month>
<year>2004</year>
</date>
<date date-type="accepted"><day>18</day>
<month>5</month>
<year>2004</year>
</date>
</history>
<copyright-statement>Copyright © 2004, American Society for Microbiology</copyright-statement>
<copyright-year>2004</copyright-year>
<abstract><p>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 <italic>N-</italic>
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.</p>
</abstract>
</article-meta>
</front>
</pmc>
<affiliations><list></list>
<tree><noCountry><name sortKey="Abrignani, Sergio" sort="Abrignani, Sergio" uniqKey="Abrignani S" first="Sergio" last="Abrignani">Sergio Abrignani</name>
<name sortKey="Choo, Qui Lim" sort="Choo, Qui Lim" uniqKey="Choo Q" first="Qui-Lim" last="Choo">Qui-Lim Choo</name>
<name sortKey="Coates, Stephen R" sort="Coates, Stephen R" uniqKey="Coates S" first="Stephen R." last="Coates">Stephen R. Coates</name>
<name sortKey="Eickmann, Markus" sort="Eickmann, Markus" uniqKey="Eickmann M" first="Markus" last="Eickmann">Markus Eickmann</name>
<name sortKey="Greer, Catherine E" sort="Greer, Catherine E" uniqKey="Greer C" first="Catherine E." last="Greer">Catherine E. Greer</name>
<name sortKey="Han, Jang H" sort="Han, Jang H" uniqKey="Han J" first="Jang H." last="Han">Jang H. Han</name>
<name sortKey="Harada, Takashi" sort="Harada, Takashi" uniqKey="Harada T" first="Takashi" last="Harada">Takashi Harada</name>
<name sortKey="Houghton, Michael" sort="Houghton, Michael" uniqKey="Houghton M" first="Michael" last="Houghton">Michael Houghton</name>
<name sortKey="Pileri, Piero" sort="Pileri, Piero" uniqKey="Pileri P" first="Piero" last="Pileri">Piero Pileri</name>
<name sortKey="Polo, John M" sort="Polo, John M" uniqKey="Polo J" first="John M." last="Polo">John M. Polo</name>
<name sortKey="Rappuoli, Rino" sort="Rappuoli, Rino" uniqKey="Rappuoli R" first="Rino" last="Rappuoli">Rino Rappuoli</name>
<name sortKey="Seo, Mi Young" sort="Seo, Mi Young" uniqKey="Seo M" first="Mi-Young" last="Seo">Mi-Young Seo</name>
<name sortKey="Song, Hyun Chul" sort="Song, Hyun Chul" uniqKey="Song H" first="Hyun Chul" last="Song">Hyun Chul Song</name>
<name sortKey="Stadler, Konrad" sort="Stadler, Konrad" uniqKey="Stadler K" first="Konrad" last="Stadler">Konrad Stadler</name>
<name sortKey="Uematsu, Yasushi" sort="Uematsu, Yasushi" uniqKey="Uematsu Y" first="Yasushi" last="Uematsu">Yasushi Uematsu</name>
<name sortKey="Yoo, Byoung J" sort="Yoo, Byoung J" uniqKey="Yoo B" first="Byoung J." last="Yoo">Byoung J. Yoo</name>
</noCountry>
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