Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.
Identifieur interne : 006082 ( Main/Exploration ); précédent : 006081; suivant : 006083Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.
Auteurs : Wenhui Li [États-Unis] ; Michael J. Moore ; Natalya Vasilieva ; Jianhua Sui ; Swee Kee Wong ; Michael A. Berne ; Mohan Somasundaran ; John L. Sullivan ; Katherine Luzuriaga ; Thomas C. Greenough ; Hyeryun Choe ; Michael FarzanSource :
- Nature [ 1476-4687 ] ; 2003.
Descripteurs français
- KwdFr :
- Animaux, Anticorps (immunologie), Anticorps (pharmacologie), Carboxypeptidases (antagonistes et inhibiteurs), Carboxypeptidases (génétique), Carboxypeptidases (immunologie), Carboxypeptidases (métabolisme), Cellules Vero, Cellules géantes (cytologie), Cellules géantes (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Lignée cellulaire, Masse moléculaire, Peptidyl-Dipeptidase A (immunologie), Peptidyl-Dipeptidase A (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (antagonistes et inhibiteurs), Récepteurs viraux (génétique), Récepteurs viraux (immunologie), Récepteurs viraux (métabolisme), Réplication virale (), Solubilité, Structure tertiaire des protéines, Transfection, Virus du SRAS (croissance et développement), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Carboxypeptidases, Récepteurs viraux.
- croissance et développement : Virus du SRAS.
- cytologie : Cellules géantes.
- génétique : Carboxypeptidases, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- immunologie : Anticorps, Carboxypeptidases, Peptidyl-Dipeptidase A, Récepteurs viraux.
- métabolisme : Carboxypeptidases, Cellules géantes, Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- pharmacologie : Anticorps.
- Animaux, Cellules Vero, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Lignée cellulaire, Masse moléculaire, Protéines de l'enveloppe virale, Réplication virale, Solubilité, Structure tertiaire des protéines, Transfection.
English descriptors
- KwdEn :
- Animals, Antibodies (immunology), Antibodies (pharmacology), Carboxypeptidases (antagonists & inhibitors), Carboxypeptidases (genetics), Carboxypeptidases (immunology), Carboxypeptidases (metabolism), Cell Line, Chlorocebus aethiops, Giant Cells (cytology), Giant Cells (metabolism), Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Molecular Weight, Peptidyl-Dipeptidase A (immunology), Peptidyl-Dipeptidase A (metabolism), Protein Binding, Protein Structure, Tertiary, Receptors, Virus (antagonists & inhibitors), Receptors, Virus (genetics), Receptors, Virus (immunology), Receptors, Virus (metabolism), SARS Virus (genetics), SARS Virus (growth & development), SARS Virus (metabolism), Solubility, Spike Glycoprotein, Coronavirus, Transfection, Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Replication (drug effects).
- MESH :
- chemical , antagonists & inhibitors : Carboxypeptidases, Receptors, Virus.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Carboxypeptidases, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Carboxypeptidases, Peptidyl-Dipeptidase A, Receptors, Virus.
- chemical , metabolism : Carboxypeptidases, Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Virus, Viral Envelope Proteins.
- chemical , pharmacology : Antibodies.
- cytology : Giant Cells.
- drug effects : Virus Replication.
- genetics : SARS Virus.
- growth & development : SARS Virus.
- metabolism : Giant Cells, SARS Virus.
- Animals, Cell Line, Chlorocebus aethiops, Humans, Molecular Weight, Protein Binding, Protein Structure, Tertiary, Solubility, Spike Glycoprotein, Coronavirus, Transfection, Vero Cells.
Abstract
Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2), isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.
DOI: 10.1038/nature02145
PubMed: 14647384
Affiliations:
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Le document en format XML
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Moore</name></author><author><name sortKey="Vasilieva, Natalya" sort="Vasilieva, Natalya" uniqKey="Vasilieva N" first="Natalya" last="Vasilieva">Natalya Vasilieva</name></author><author><name sortKey="Sui, Jianhua" sort="Sui, Jianhua" uniqKey="Sui J" first="Jianhua" last="Sui">Jianhua Sui</name></author><author><name sortKey="Wong, Swee Kee" sort="Wong, Swee Kee" uniqKey="Wong S" first="Swee Kee" last="Wong">Swee Kee Wong</name></author><author><name sortKey="Berne, Michael A" sort="Berne, Michael A" uniqKey="Berne M" first="Michael A" last="Berne">Michael A. Berne</name></author><author><name sortKey="Somasundaran, Mohan" sort="Somasundaran, Mohan" uniqKey="Somasundaran M" first="Mohan" last="Somasundaran">Mohan Somasundaran</name></author><author><name sortKey="Sullivan, John L" sort="Sullivan, John L" uniqKey="Sullivan J" first="John L" last="Sullivan">John L. 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Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Weight</term><term>Peptidyl-Dipeptidase A (immunology)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Receptors, Virus (antagonists & inhibitors)</term><term>Receptors, Virus (genetics)</term><term>Receptors, Virus (immunology)</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (genetics)</term><term>SARS Virus (growth & development)</term><term>SARS Virus (metabolism)</term><term>Solubility</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="KwdFr" 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scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies</term><term>Carboxypeptidases</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antibodies</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Carboxypeptidases</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cellules géantes</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Giant 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géantes</term><term>Glycoprotéines membranaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Anticorps</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Molecular Weight</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Solubility</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</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>Masse moléculaire</term><term>Protéines de l'enveloppe virale</term><term>Réplication virale</term><term>Solubilité</term><term>Structure tertiaire des protéines</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2), isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Berne, Michael A" sort="Berne, Michael A" uniqKey="Berne M" first="Michael A" last="Berne">Michael A. Berne</name><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="Greenough, Thomas C" sort="Greenough, Thomas C" uniqKey="Greenough T" first="Thomas C" last="Greenough">Thomas C. Greenough</name><name sortKey="Luzuriaga, Katherine" sort="Luzuriaga, Katherine" uniqKey="Luzuriaga K" first="Katherine" last="Luzuriaga">Katherine Luzuriaga</name><name sortKey="Moore, Michael J" sort="Moore, Michael J" uniqKey="Moore M" first="Michael J" last="Moore">Michael J. Moore</name><name sortKey="Somasundaran, Mohan" sort="Somasundaran, Mohan" uniqKey="Somasundaran M" first="Mohan" last="Somasundaran">Mohan Somasundaran</name><name sortKey="Sui, Jianhua" sort="Sui, Jianhua" uniqKey="Sui J" first="Jianhua" last="Sui">Jianhua Sui</name><name sortKey="Sullivan, John L" sort="Sullivan, John L" uniqKey="Sullivan J" first="John L" last="Sullivan">John L. Sullivan</name><name sortKey="Vasilieva, Natalya" sort="Vasilieva, Natalya" uniqKey="Vasilieva N" first="Natalya" last="Vasilieva">Natalya Vasilieva</name><name sortKey="Wong, Swee Kee" sort="Wong, Swee Kee" uniqKey="Wong S" first="Swee Kee" last="Wong">Swee Kee Wong</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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