Amino acids 270 to 510 of the severe acute respiratory syndrome coronavirus spike protein are required for interaction with receptor
Identifieur interne : 005B79 ( Main/Exploration ); précédent : 005B78; suivant : 005B80Amino acids 270 to 510 of the severe acute respiratory syndrome coronavirus spike protein are required for interaction with receptor
Auteurs : Gregory J. Babcock [Jamaïque] ; Diana J. Esshaki [Jamaïque] ; William D. Jr Thomas [Jamaïque] ; Donna M. Ambrosino [Jamaïque]Source :
- Journal of virology [ 0022-538X ] ; 2004.
Descripteurs français
- KwdFr :
- Acides aminés (), Acides aminés (génétique), Animaux, Cellules Vero, Codon, Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Glycoprotéines membranaires (synthèse chimique), Humains, Ligands, Lignée cellulaire, Mutation, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines de l'enveloppe virale (synthèse chimique), Relation structure-activité, Récepteurs viraux (métabolisme), Virus du SRAS (métabolisme), Virus du SRAS (pathogénicité).
- MESH :
- génétique : Acides aminés, Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- pathogénicité : Virus du SRAS.
- synthèse chimique : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- Pascal (Inist)
- Acides aminés, Animaux, Cellules Vero, Codon, Coronavirus, Aminoacide, Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Ligands, Lignée cellulaire, Mutation, Protéine, Microbiologie, Protéines de l'enveloppe virale, Relation structure-activité, Virologie, Syndrome respiratoire aigu sévère.
English descriptors
- KwdEn :
- Amino Acids (chemistry), Amino Acids (genetics), Aminoacid, Animals, Cell Line, Chlorocebus aethiops, Codon, Coronavirus, Flow Cytometry, Humans, Ligands, Membrane Glycoproteins (chemical synthesis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Microbiology, Mutation, Protein, Receptors, Virus (metabolism), SARS Virus (metabolism), SARS Virus (pathogenicity), Severe acute respiratory syndrome, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Vero Cells, Viral Envelope Proteins (chemical synthesis), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virology.
- MESH :
- chemical , chemical synthesis : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , chemistry : Amino Acids, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Amino Acids, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- metabolism : SARS Virus.
- pathogenicity : SARS Virus.
- Animals, Cell Line, Chlorocebus aethiops, Codon, Flow Cytometry, Humans, Ligands, Mutation, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Vero Cells.
Abstract
A novel coronavirus, severe acute respiratory syndrome coronavirus (SARS-CoV), has recently been identified as the causative agent of severe acute respiratory syndrome (SARS). SARS-CoV appears similar to other coronaviruses in both virion structure and genome organization. It is known for other coronaviruses that the spike (S) glycoprotein is required for both viral attachment to permissive cells and for fusion of the viral envelope with the host cell membrane. Here we describe the construction and expression of a soluble codon-optimized SARS-CoV S glycoprotein comprising the first 1,190 amino acids of the native S glycoprotein (S1190). The codon-optimized and native S glycoproteins exhibit similar molecular weight as determined by Western blot analysis, indicating that synthetic S glycoprotein is modified correctly in a mammalian expression system. S1190 binds to the surface of Vero E6 cells, a cell permissive to infection, as demonstrated by fluorescence-activated cell sorter analysis, suggesting that S1190 maintains the biologic activity present in native S glycoprotein. This interaction is blocked with serum obtained from recovering SARS patients, indicating that the binding is specific. In an effort to map the ligand-binding domain of the SARS-CoV S glycoprotein, carboxy-and amino-terminal truncations of the S1190 glycoprotein were constructed. Amino acids 270 to 510 were the minimal receptor-binding region of the SARS-CoV S glycoprotein as determined by flow cytometry. We speculate that amino acids 1 to 510 of the SARS-CoV S glycoprotein represent a unique domain containing the receptor-binding site (amino acids 270 to 510), analogous to the S1 subunit of other coronavirus S glycoproteins.
Affiliations:
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Le document en format XML
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Babcock</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Massachusetts Biologic Laboratories, University of Massachusetts Medical School</s1><s2>Plain, Massachusetts 02130</s2><s3>JAM</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>Jamaïque</country><wicri:noRegion>Plain, Massachusetts 02130</wicri:noRegion></affiliation></author><author><name sortKey="Esshaki, Diana J" sort="Esshaki, Diana J" uniqKey="Esshaki D" first="Diana J." last="Esshaki">Diana J. Esshaki</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Massachusetts Biologic Laboratories, University of Massachusetts Medical School</s1><s2>Plain, Massachusetts 02130</s2><s3>JAM</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>Jamaïque</country><wicri:noRegion>Plain, Massachusetts 02130</wicri:noRegion></affiliation></author><author><name sortKey="Thomas, William D Jr" sort="Thomas, William D Jr" uniqKey="Thomas W" first="William D. Jr" last="Thomas">William D. Jr Thomas</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Massachusetts Biologic Laboratories, University of Massachusetts Medical School</s1><s2>Plain, Massachusetts 02130</s2><s3>JAM</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>Jamaïque</country><wicri:noRegion>Plain, Massachusetts 02130</wicri:noRegion></affiliation></author><author><name sortKey="Ambrosino, Donna M" sort="Ambrosino, Donna M" uniqKey="Ambrosino D" first="Donna M." last="Ambrosino">Donna M. Ambrosino</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Massachusetts Biologic Laboratories, University of Massachusetts Medical School</s1><s2>Plain, Massachusetts 02130</s2><s3>JAM</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>Jamaïque</country><wicri:noRegion>Plain, Massachusetts 02130</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>Amino Acids (chemistry)</term><term>Amino Acids (genetics)</term><term>Aminoacid</term><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Codon</term><term>Coronavirus</term><term>Flow Cytometry</term><term>Humans</term><term>Ligands</term><term>Membrane Glycoproteins (chemical synthesis)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Microbiology</term><term>Mutation</term><term>Protein</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (pathogenicity)</term><term>Severe acute respiratory syndrome</term><term>Spike Glycoprotein, Coronavirus</term><term>Structure-Activity Relationship</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemical synthesis)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virology</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés ()</term><term>Acides aminés (génétique)</term><term>Animaux</term><term>Cellules Vero</term><term>Codon</term><term>Cytométrie en flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Glycoprotéines membranaires (synthèse chimique)</term><term>Humains</term><term>Ligands</term><term>Lignée cellulaire</term><term>Mutation</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines de l'enveloppe virale (synthèse chimique)</term><term>Relation structure-activité</term><term>Récepteurs viraux (métabolisme)</term><term>Virus du SRAS (métabolisme)</term><term>Virus du SRAS (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acids</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acides aminés</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Codon</term><term>Flow Cytometry</term><term>Humans</term><term>Ligands</term><term>Mutation</term><term>Spike Glycoprotein, Coronavirus</term><term>Structure-Activity Relationship</term><term>Vero Cells</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Acides aminés</term><term>Animaux</term><term>Cellules Vero</term><term>Codon</term><term>Coronavirus</term><term>Aminoacide</term><term>Cytométrie en flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Ligands</term><term>Lignée cellulaire</term><term>Mutation</term><term>Protéine</term><term>Microbiologie</term><term>Protéines de l'enveloppe virale</term><term>Relation structure-activité</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A novel coronavirus, severe acute respiratory syndrome coronavirus (SARS-CoV), has recently been identified as the causative agent of severe acute respiratory syndrome (SARS). SARS-CoV appears similar to other coronaviruses in both virion structure and genome organization. It is known for other coronaviruses that the spike (S) glycoprotein is required for both viral attachment to permissive cells and for fusion of the viral envelope with the host cell membrane. Here we describe the construction and expression of a soluble codon-optimized SARS-CoV S glycoprotein comprising the first 1,190 amino acids of the native S glycoprotein (S<sub>1190</sub>). The codon-optimized and native S glycoproteins exhibit similar molecular weight as determined by Western blot analysis, indicating that synthetic S glycoprotein is modified correctly in a mammalian expression system. S<sub>1190</sub> binds to the surface of Vero E6 cells, a cell permissive to infection, as demonstrated by fluorescence-activated cell sorter analysis, suggesting that S<sub>1190</sub> maintains the biologic activity present in native S glycoprotein. This interaction is blocked with serum obtained from recovering SARS patients, indicating that the binding is specific. In an effort to map the ligand-binding domain of the SARS-CoV S glycoprotein, carboxy-and amino-terminal truncations of the S<sub>1190</sub> glycoprotein were constructed. Amino acids 270 to 510 were the minimal receptor-binding region of the SARS-CoV S glycoprotein as determined by flow cytometry. We speculate that amino acids 1 to 510 of the SARS-CoV S glycoprotein represent a unique domain containing the receptor-binding site (amino acids 270 to 510), analogous to the S1 subunit of other coronavirus S glycoproteins.</div></front></TEI><affiliations><list><country><li>Jamaïque</li></country></list><tree><country name="Jamaïque"><noRegion><name sortKey="Babcock, Gregory J" sort="Babcock, Gregory J" uniqKey="Babcock G" first="Gregory J." last="Babcock">Gregory J. Babcock</name></noRegion><name sortKey="Ambrosino, Donna M" sort="Ambrosino, Donna M" uniqKey="Ambrosino D" first="Donna M." last="Ambrosino">Donna M. Ambrosino</name><name sortKey="Esshaki, Diana J" sort="Esshaki, Diana J" uniqKey="Esshaki D" first="Diana J." last="Esshaki">Diana J. Esshaki</name><name sortKey="Thomas, William D Jr" sort="Thomas, William D Jr" uniqKey="Thomas W" first="William D. Jr" last="Thomas">William D. Jr Thomas</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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