A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2.
Identifieur interne : 000A97 ( 2020/Analysis ); précédent : 000A96; suivant : 000A98A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2.
Auteurs : Swee Kee Wong [États-Unis] ; Wenhui Li ; Michael J. Moore ; Hyeryun Choe ; Michael FarzanSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2004.
Descripteurs français
- KwdFr :
- Acide glutamique (), Alanine (), Carboxypeptidases (), Carboxypeptidases (métabolisme), Concentration inhibitrice 50, Cystéine (), Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Humains, Liaison aux protéines, Lignée cellulaire, Mutation, Mutation ponctuelle, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale (), Relation dose-effet des médicaments, Structure tertiaire des protéines, Transfection, Virus du SRAS (métabolisme), Électrophorèse sur gel de polyacrylamide.
- MESH :
- métabolisme : Carboxypeptidases, Virus du SRAS.
- Acide glutamique, Alanine, Carboxypeptidases, Concentration inhibitrice 50, Cystéine, Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Lignée cellulaire, Mutation, Mutation ponctuelle, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Relation dose-effet des médicaments, Structure tertiaire des protéines, Transfection, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Alanine (chemistry), Carboxypeptidases (chemistry), Carboxypeptidases (metabolism), Cell Line, Cysteine (chemistry), Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Glutamic Acid (chemistry), Humans, Inhibitory Concentration 50, Membrane Glycoproteins (chemistry), Mutation, Peptidyl-Dipeptidase A, Point Mutation, Protein Binding, Protein Structure, Tertiary, SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Transfection, Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Alanine, Carboxypeptidases, Cysteine, Glutamic Acid, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Carboxypeptidases.
- metabolism : SARS Virus.
- Cell Line, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Humans, Inhibitory Concentration 50, Mutation, Peptidyl-Dipeptidase A, Point Mutation, Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Transfection.
Abstract
The coronavirus spike (S) protein mediates infection of receptor-expressing host cells and is a critical target for antiviral neutralizing antibodies. Angiotensin-converting enzyme 2 (ACE2) is a functional receptor for the coronavirus (severe acute respiratory syndrome (SARS)-CoV) that causes SARS. Here we demonstrate that a 193-amino acid fragment of the S protein (residues 318-510) bound ACE2 more efficiently than did the full S1 domain (residues 12-672). Smaller S protein fragments, expressing residues 327-510 or 318-490, did not detectably bind ACE2. A point mutation at aspartic acid 454 abolished association of the full S1 domain and of the 193-residue fragment with ACE2. The 193-residue fragment blocked S protein-mediated infection with an IC(50) of less than 10 nm, whereas the IC(50) of the S1 domain was approximately 50 nm. These data identify an independently folded receptor-binding domain of the SARS-CoV S protein.
DOI: 10.1074/jbc.C300520200
PubMed: 14670965
Affiliations:
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pubmed:14670965Le document en format XML
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Moore</name></author><author><name sortKey="Choe, Hyeryun" sort="Choe, Hyeryun" uniqKey="Choe H" first="Hyeryun" last="Choe">Hyeryun Choe</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alanine (chemistry)</term><term>Carboxypeptidases (chemistry)</term><term>Carboxypeptidases (metabolism)</term><term>Cell Line</term><term>Cysteine (chemistry)</term><term>Dose-Response Relationship, Drug</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Flow Cytometry</term><term>Glutamic Acid (chemistry)</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Membrane Glycoproteins (chemistry)</term><term>Mutation</term><term>Peptidyl-Dipeptidase A</term><term>Point Mutation</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>SARS Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide glutamique ()</term><term>Alanine ()</term><term>Carboxypeptidases ()</term><term>Carboxypeptidases (métabolisme)</term><term>Concentration inhibitrice 50</term><term>Cystéine ()</term><term>Cytométrie en flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Mutation</term><term>Mutation ponctuelle</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale ()</term><term>Relation dose-effet des médicaments</term><term>Structure tertiaire des protéines</term><term>Transfection</term><term>Virus du SRAS (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alanine</term><term>Carboxypeptidases</term><term>Cysteine</term><term>Glutamic Acid</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carboxypeptidases</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Dose-Response Relationship, Drug</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Flow Cytometry</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Mutation</term><term>Peptidyl-Dipeptidase A</term><term>Point Mutation</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acide glutamique</term><term>Alanine</term><term>Carboxypeptidases</term><term>Concentration inhibitrice 50</term><term>Cystéine</term><term>Cytométrie en flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Mutation</term><term>Mutation ponctuelle</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Relation dose-effet des médicaments</term><term>Structure tertiaire des protéines</term><term>Transfection</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus spike (S) protein mediates infection of receptor-expressing host cells and is a critical target for antiviral neutralizing antibodies. Angiotensin-converting enzyme 2 (ACE2) is a functional receptor for the coronavirus (severe acute respiratory syndrome (SARS)-CoV) that causes SARS. Here we demonstrate that a 193-amino acid fragment of the S protein (residues 318-510) bound ACE2 more efficiently than did the full S1 domain (residues 12-672). Smaller S protein fragments, expressing residues 327-510 or 318-490, did not detectably bind ACE2. A point mutation at aspartic acid 454 abolished association of the full S1 domain and of the 193-residue fragment with ACE2. The 193-residue fragment blocked S protein-mediated infection with an IC(50) of less than 10 nm, whereas the IC(50) of the S1 domain was approximately 50 nm. These data identify an independently folded receptor-binding domain of the SARS-CoV S protein.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Choe, Hyeryun" sort="Choe, Hyeryun" uniqKey="Choe H" first="Hyeryun" last="Choe">Hyeryun Choe</name><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name><name sortKey="Moore, Michael J" sort="Moore, Michael J" uniqKey="Moore M" first="Michael J" last="Moore">Michael J. Moore</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Wong, Swee Kee" sort="Wong, Swee Kee" uniqKey="Wong S" first="Swee Kee" last="Wong">Swee Kee Wong</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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