The SARS-CoV S glycoprotein: expression and functional characterization.
Identifieur interne : 005D51 ( Main/Exploration ); précédent : 005D50; suivant : 005D52The SARS-CoV S glycoprotein: expression and functional characterization.
Auteurs : Xiaodong Xiao [États-Unis] ; Samitabh Chakraborti ; Anthony S. Dimitrov ; Kosi Gramatikoff ; Dimiter S. DimitrovSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2003.
Descripteurs français
- KwdFr :
- Adhérence cellulaire (physiologie), Animaux, Cellules Vero, Concentration en ions d'hydrogène, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (isolement et purification), Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Masse moléculaire, Protéines de fusion virale (), Protéines de fusion virale (isolement et purification), Protéines de fusion virale (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (isolement et purification), Protéines de l'enveloppe virale (métabolisme), Protéines recombinantes (), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Sites de fixation, Spécificité d'espèce, Virus du SRAS (), Virus du SRAS (isolement et purification), Virus du SRAS (métabolisme).
- MESH :
- isolement et purification : Glycoprotéines membranaires, Protéines de fusion virale, Protéines de l'enveloppe virale, Protéines recombinantes, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de fusion virale, Protéines de l'enveloppe virale, Protéines recombinantes, Virus du SRAS.
- physiologie : Adhérence cellulaire.
- Animaux, Cellules Vero, Concentration en ions d'hydrogène, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Masse moléculaire, Protéines de fusion virale, Protéines de l'enveloppe virale, Protéines recombinantes, Sites de fixation, Spécificité d'espèce, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Binding Sites, Cell Adhesion (physiology), Chlorocebus aethiops, Humans, Hydrogen-Ion Concentration, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (isolation & purification), Membrane Glycoproteins (metabolism), Molecular Weight, Protein Binding, Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), SARS Virus (chemistry), SARS Virus (isolation & purification), SARS Virus (metabolism), Species Specificity, Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (isolation & purification), Viral Envelope Proteins (metabolism), Viral Fusion Proteins (chemistry), Viral Fusion Proteins (isolation & purification), Viral Fusion Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , isolation & purification : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , metabolism : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemistry : SARS Virus.
- isolation & purification : SARS Virus.
- metabolism : SARS Virus.
- physiology : Cell Adhesion.
- Animals, Binding Sites, Chlorocebus aethiops, Humans, Hydrogen-Ion Concentration, Molecular Weight, Protein Binding, Species Specificity, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
We have cloned, expressed, and characterized the full-length and various soluble fragments of the SARS-CoV (Tor2 isolate) S glycoprotein. Cells expressing S fused with receptor-expressing cells at neutral pH suggesting that the recombinant glycoprotein is functional, its membrane fusogenic activity does not require other viral proteins, and that low pH is not required for triggering membrane fusion; fusion was not observed at low receptor concentrations. S and its soluble ectodomain, S(e), were not cleaved to any significant degree. They ran at about 180-200kDa in SDS gels suggesting post-translational modifications as predicted by previous computer analysis and observed for other coronaviruses. Fragments containing the N-terminal amino acid residues 17-537 and 272-537 but not 17-276 bound specifically to Vero E6 cells and purified soluble receptor, ACE2, recently identified by M. Farzan and co-workers [Nature 426 (2003) 450-454]. Together with data for inhibition of binding by antibodies developed against peptides from S, these findings suggest that the receptor-binding domain is located between amino acid residues 303 and 537. These results also confirm that ACE2 is a functional receptor for the SARS virus and may help in the elucidation of the mechanisms of SARS-CoV entry and in the development of vaccine immunogens and entry inhibitors.
DOI: 10.1016/j.bbrc.2003.11.054
PubMed: 14651994
Affiliations:
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Le document en format XML
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Dimitrov</name></author><author><name sortKey="Gramatikoff, Kosi" sort="Gramatikoff, Kosi" uniqKey="Gramatikoff K" first="Kosi" last="Gramatikoff">Kosi Gramatikoff</name></author><author><name sortKey="Dimitrov, Dimiter S" sort="Dimitrov, Dimiter S" uniqKey="Dimitrov D" first="Dimiter S" last="Dimitrov">Dimiter S. 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Dimitrov</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cell Adhesion (physiology)</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (isolation & purification)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Weight</term><term>Protein Binding</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (isolation & purification)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (isolation & purification)</term><term>SARS Virus (metabolism)</term><term>Species Specificity</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (isolation & purification)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Fusion Proteins (chemistry)</term><term>Viral Fusion Proteins (isolation & purification)</term><term>Viral Fusion Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adhérence cellulaire (physiologie)</term><term>Animaux</term><term>Cellules Vero</term><term>Concentration en ions d'hydrogène</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (isolement et purification)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Masse moléculaire</term><term>Protéines de fusion virale ()</term><term>Protéines de fusion virale (isolement et purification)</term><term>Protéines de fusion virale (métabolisme)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (isolement et purification)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (isolement et purification)</term><term>Protéines recombinantes (métabolisme)</term><term>Sites de fixation</term><term>Spécificité d'espèce</term><term>Virus du SRAS ()</term><term>Virus du SRAS (isolement et purification)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant 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protéines</term><term>Masse moléculaire</term><term>Protéines de fusion virale</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term><term>Sites de fixation</term><term>Spécificité d'espèce</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have cloned, expressed, and characterized the full-length and various soluble fragments of the SARS-CoV (Tor2 isolate) S glycoprotein. Cells expressing S fused with receptor-expressing cells at neutral pH suggesting that the recombinant glycoprotein is functional, its membrane fusogenic activity does not require other viral proteins, and that low pH is not required for triggering membrane fusion; fusion was not observed at low receptor concentrations. S and its soluble ectodomain, S(e), were not cleaved to any significant degree. They ran at about 180-200kDa in SDS gels suggesting post-translational modifications as predicted by previous computer analysis and observed for other coronaviruses. Fragments containing the N-terminal amino acid residues 17-537 and 272-537 but not 17-276 bound specifically to Vero E6 cells and purified soluble receptor, ACE2, recently identified by M. Farzan and co-workers [Nature 426 (2003) 450-454]. Together with data for inhibition of binding by antibodies developed against peptides from S, these findings suggest that the receptor-binding domain is located between amino acid residues 303 and 537. These results also confirm that ACE2 is a functional receptor for the SARS virus and may help in the elucidation of the mechanisms of SARS-CoV entry and in the development of vaccine immunogens and entry inhibitors.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><noCountry><name sortKey="Chakraborti, Samitabh" sort="Chakraborti, Samitabh" uniqKey="Chakraborti S" first="Samitabh" last="Chakraborti">Samitabh Chakraborti</name><name sortKey="Dimitrov, Anthony S" sort="Dimitrov, Anthony S" uniqKey="Dimitrov A" first="Anthony S" last="Dimitrov">Anthony S. Dimitrov</name><name sortKey="Dimitrov, Dimiter S" sort="Dimitrov, Dimiter S" uniqKey="Dimitrov D" first="Dimiter S" last="Dimitrov">Dimiter S. Dimitrov</name><name sortKey="Gramatikoff, Kosi" sort="Gramatikoff, Kosi" uniqKey="Gramatikoff K" first="Kosi" last="Gramatikoff">Kosi Gramatikoff</name></noCountry><country name="États-Unis"><region name="Maryland"><name sortKey="Xiao, Xiaodong" sort="Xiao, Xiaodong" uniqKey="Xiao X" first="Xiaodong" last="Xiao">Xiaodong Xiao</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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