Synthesis and Characterization of a Native, Oligomeric Form of Recombinant Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein
Identifieur interne : 005041 ( Main/Curation ); précédent : 005040; suivant : 005042Synthesis 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.
Descripteurs français
- KwdFr :
- ADN complémentaire, ADN viral (génétique), ADN viral (métabolisme), Animaux, Antigènes viraux (), Antigènes viraux (génétique), Antigènes viraux (immunologie), Antigènes viraux (métabolisme), Appareil de Golgi (), Cellules COS, Cricetinae, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Glycosidases (métabolisme), Lignée cellulaire, Masse moléculaire, Maturation post-traductionnelle des protéines, Milieux de culture (), Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (métabolisme), Pliage des protéines, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (immunologie), Protéines recombinantes (métabolisme), Réticulum endoplasmique (), Sous-unités de protéines (analyse), Structure tertiaire des protéines, Transport de protéines, Virus du SRAS (génétique).
- MESH :
- analyse : Sous-unités de protéines.
- génétique : ADN viral, Antigènes viraux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes, Virus du SRAS.
- immunologie : Antigènes viraux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- métabolisme : ADN viral, Antigènes viraux, Glycoprotéines membranaires, Glycosidases, Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase, Protéines de l'enveloppe virale, Protéines recombinantes.
- ADN complémentaire, Animaux, Antigènes viraux, Appareil de Golgi, Cellules COS, Cricetinae, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Lignée cellulaire, Masse moléculaire, Maturation post-traductionnelle des protéines, Milieux de culture, Pliage des protéines, Protéines de l'enveloppe virale, Protéines recombinantes, Réticulum endoplasmique, Structure tertiaire des protéines, Transport de protéines.
English descriptors
- KwdEn :
- Animals, Antigens, Viral (chemistry), Antigens, Viral (genetics), Antigens, Viral (immunology), Antigens, Viral (metabolism), COS Cells, Cell Line, Chlorocebus aethiops, Cricetinae, Culture Media (chemistry), DNA, Complementary, DNA, Viral (genetics), DNA, Viral (metabolism), Endoplasmic Reticulum (chemistry), Glycoside Hydrolases (metabolism), Golgi Apparatus (chemistry), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Molecular Weight, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism), Protein Folding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Protein Subunits (analysis), Protein Transport, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (immunology), Recombinant Proteins (metabolism), SARS Virus (genetics), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , analysis : Protein Subunits.
- chemical , chemistry : Antigens, Viral, Culture Media, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , genetics : Antigens, Viral, DNA, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Antigens, Viral, DNA, Viral, Glycoside Hydrolases, Membrane Glycoproteins, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Recombinant Proteins, Viral Envelope Proteins.
- chemistry : Endoplasmic Reticulum, Golgi Apparatus.
- genetics : SARS Virus.
- Animals, COS Cells, Cell Line, Chlorocebus aethiops, Cricetinae, DNA, Complementary, Molecular Weight, Protein Folding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Protein Transport, Spike Glycoprotein, Coronavirus.
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
Url:
DOI: 10.1128/JVI.78.19.10328-10335.2004
PubMed: 15367599
PubMed Central: 516425
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PMC:516425Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Antigens, Viral (chemistry)</term>
<term>Antigens, Viral (genetics)</term>
<term>Antigens, Viral (immunology)</term>
<term>Antigens, Viral (metabolism)</term>
<term>COS Cells</term>
<term>Cell Line</term>
<term>Chlorocebus aethiops</term>
<term>Cricetinae</term>
<term>Culture Media (chemistry)</term>
<term>DNA, Complementary</term>
<term>DNA, Viral (genetics)</term>
<term>DNA, Viral (metabolism)</term>
<term>Endoplasmic Reticulum (chemistry)</term>
<term>Glycoside Hydrolases (metabolism)</term>
<term>Golgi Apparatus (chemistry)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Molecular Weight</term>
<term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism)</term>
<term>Protein Folding</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Structure, Tertiary</term>
<term>Protein Subunits (analysis)</term>
<term>Protein Transport</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (immunology)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (immunology)</term>
<term>Viral Envelope Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire</term>
<term>ADN viral (génétique)</term>
<term>ADN viral (métabolisme)</term>
<term>Animaux</term>
<term>Antigènes viraux ()</term>
<term>Antigènes viraux (génétique)</term>
<term>Antigènes viraux (immunologie)</term>
<term>Antigènes viraux (métabolisme)</term>
<term>Appareil de Golgi ()</term>
<term>Cellules COS</term>
<term>Cricetinae</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Glycosidases (métabolisme)</term>
<term>Lignée cellulaire</term>
<term>Masse moléculaire</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Milieux de culture ()</term>
<term>Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (métabolisme)</term>
<term>Pliage des protéines</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (immunologie)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Réticulum endoplasmique ()</term>
<term>Sous-unités de protéines (analyse)</term>
<term>Structure tertiaire des protéines</term>
<term>Transport de protéines</term>
<term>Virus du SRAS (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Protein Subunits</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Viral</term>
<term>Culture Media</term>
<term>Membrane Glycoproteins</term>
<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antigens, Viral</term>
<term>DNA, Viral</term>
<term>Membrane Glycoproteins</term>
<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Viral</term>
<term>Membrane Glycoproteins</term>
<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antigens, Viral</term>
<term>DNA, Viral</term>
<term>Glycoside Hydrolases</term>
<term>Membrane Glycoproteins</term>
<term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</term>
<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Sous-unités de protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Endoplasmic Reticulum</term>
<term>Golgi Apparatus</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>Antigènes viraux</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes viraux</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN viral</term>
<term>Antigènes viraux</term>
<term>Glycoprotéines membranaires</term>
<term>Glycosidases</term>
<term>Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>COS Cells</term>
<term>Cell Line</term>
<term>Chlorocebus aethiops</term>
<term>Cricetinae</term>
<term>DNA, Complementary</term>
<term>Molecular Weight</term>
<term>Protein Folding</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Structure, Tertiary</term>
<term>Protein Transport</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>ADN complémentaire</term>
<term>Animaux</term>
<term>Antigènes viraux</term>
<term>Appareil de Golgi</term>
<term>Cellules COS</term>
<term>Cricetinae</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Lignée cellulaire</term>
<term>Masse moléculaire</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Milieux de culture</term>
<term>Pliage des protéines</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
<term>Réticulum endoplasmique</term>
<term>Structure tertiaire des protéines</term>
<term>Transport de protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</TEI>
</record>
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