Susceptibility to SARS coronavirus S protein-driven infection correlates with expression of angiotensin converting enzyme 2 and infection can be blocked by soluble receptor.
Identifieur interne : 005043 ( Main/Exploration ); précédent : 005042; suivant : 005044Susceptibility to SARS coronavirus S protein-driven infection correlates with expression of angiotensin converting enzyme 2 and infection can be blocked by soluble receptor.
Auteurs : Heike Hofmann [Allemagne] ; Martina Geier ; Andrea Marzi ; Mandy Krumbiegel ; Matthias Peipp ; Georg H. Fey ; Thomas Gramberg ; Stefan PöhlmannSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Antiviraux (), Antiviraux (métabolisme), Carboxypeptidases (), Carboxypeptidases (génétique), Carboxypeptidases (métabolisme), Humains, Lignée cellulaire, Mutation, Peptidyl-Dipeptidase A, Protéines virales (métabolisme), Récepteurs viraux (métabolisme), Solubilité, Structure tertiaire des protéines, Susceptibilité à une maladie, Syndrome respiratoire aigu sévère (métabolisme), Séquence d'acides aminés, Virus du SRAS (métabolisme), Virus du SRAS (pathogénicité).
- MESH :
- génétique : Carboxypeptidases.
- métabolisme : Antiviraux, Carboxypeptidases, Protéines virales, Récepteurs viraux, Syndrome respiratoire aigu sévère, Virus du SRAS.
- pathogénicité : Virus du SRAS.
- Alignement de séquences, Animaux, Antiviraux, Carboxypeptidases, Humains, Lignée cellulaire, Mutation, Peptidyl-Dipeptidase A, Solubilité, Structure tertiaire des protéines, Susceptibilité à une maladie, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antiviral Agents (chemistry), Antiviral Agents (metabolism), Carboxypeptidases (chemistry), Carboxypeptidases (genetics), Carboxypeptidases (metabolism), Cell Line, Disease Susceptibility, Humans, Mutation, Peptidyl-Dipeptidase A, Protein Structure, Tertiary, Receptors, Virus (metabolism), SARS Virus (metabolism), SARS Virus (pathogenicity), Sequence Alignment, Severe Acute Respiratory Syndrome (metabolism), Solubility, Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Antiviral Agents, Carboxypeptidases.
- chemical , genetics : Carboxypeptidases.
- chemical , metabolism : Antiviral Agents, Carboxypeptidases, Receptors, Virus, Viral Proteins.
- metabolism : SARS Virus, Severe Acute Respiratory Syndrome.
- pathogenicity : SARS Virus.
- Amino Acid Sequence, Animals, Cell Line, Disease Susceptibility, Humans, Mutation, Peptidyl-Dipeptidase A, Protein Structure, Tertiary, Sequence Alignment, Solubility.
Abstract
The angiotensin converting enzyme 2 (ACE2) has been identified as a receptor for the severe acute respiratory syndrome associated coronavirus (SARS-CoV). Here we show that ACE2 expression on cell lines correlates with susceptibility to SARS-CoV S-driven infection, suggesting that ACE2 is a major receptor for SARS-CoV. The soluble ectodomain of ACE2 specifically abrogated S-mediated infection and might therefore be exploited for the generation of inhibitors. Deletion of a major portion of the cytoplasmic domain of ACE2 had no effect on S-driven infection, indicating that this domain is not important for receptor function. Our results point to a central role of ACE2 in SARS-CoV infection and suggest a minor contribution of the cytoplasmic domain to receptor function.
DOI: 10.1016/j.bbrc.2004.05.114
PubMed: 15194496
Affiliations:
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Le document en format XML
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Fey</name></author><author><name sortKey="Gramberg, Thomas" sort="Gramberg, Thomas" uniqKey="Gramberg T" first="Thomas" last="Gramberg">Thomas Gramberg</name></author><author><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antiviral Agents (chemistry)</term><term>Antiviral Agents (metabolism)</term><term>Carboxypeptidases (chemistry)</term><term>Carboxypeptidases (genetics)</term><term>Carboxypeptidases (metabolism)</term><term>Cell Line</term><term>Disease Susceptibility</term><term>Humans</term><term>Mutation</term><term>Peptidyl-Dipeptidase A</term><term>Protein Structure, Tertiary</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (pathogenicity)</term><term>Sequence Alignment</term><term>Severe Acute Respiratory Syndrome (metabolism)</term><term>Solubility</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Antiviraux ()</term><term>Antiviraux (métabolisme)</term><term>Carboxypeptidases ()</term><term>Carboxypeptidases (génétique)</term><term>Carboxypeptidases (métabolisme)</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutation</term><term>Peptidyl-Dipeptidase A</term><term>Protéines virales (métabolisme)</term><term>Récepteurs viraux (métabolisme)</term><term>Solubilité</term><term>Structure tertiaire des protéines</term><term>Susceptibilité à une maladie</term><term>Syndrome respiratoire aigu sévère (métabolisme)</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (métabolisme)</term><term>Virus du SRAS (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term><term>Carboxypeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carboxypeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antiviral Agents</term><term>Carboxypeptidases</term><term>Receptors, Virus</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Carboxypeptidases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antiviraux</term><term>Carboxypeptidases</term><term>Protéines virales</term><term>Récepteurs viraux</term><term>Syndrome respiratoire aigu sévère</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" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Disease Susceptibility</term><term>Humans</term><term>Mutation</term><term>Peptidyl-Dipeptidase A</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Solubility</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Antiviraux</term><term>Carboxypeptidases</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutation</term><term>Peptidyl-Dipeptidase A</term><term>Solubilité</term><term>Structure tertiaire des protéines</term><term>Susceptibilité à une maladie</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The angiotensin converting enzyme 2 (ACE2) has been identified as a receptor for the severe acute respiratory syndrome associated coronavirus (SARS-CoV). Here we show that ACE2 expression on cell lines correlates with susceptibility to SARS-CoV S-driven infection, suggesting that ACE2 is a major receptor for SARS-CoV. The soluble ectodomain of ACE2 specifically abrogated S-mediated infection and might therefore be exploited for the generation of inhibitors. Deletion of a major portion of the cytoplasmic domain of ACE2 had no effect on S-driven infection, indicating that this domain is not important for receptor function. Our results point to a central role of ACE2 in SARS-CoV infection and suggest a minor contribution of the cytoplasmic domain to receptor function.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Bavière</li><li>District de Moyenne-Franconie</li></region><settlement><li>Erlangen</li></settlement></list><tree><noCountry><name sortKey="Fey, Georg H" sort="Fey, Georg H" uniqKey="Fey G" first="Georg H" last="Fey">Georg H. Fey</name><name sortKey="Geier, Martina" sort="Geier, Martina" uniqKey="Geier M" first="Martina" last="Geier">Martina Geier</name><name sortKey="Gramberg, Thomas" sort="Gramberg, Thomas" uniqKey="Gramberg T" first="Thomas" last="Gramberg">Thomas Gramberg</name><name sortKey="Krumbiegel, Mandy" sort="Krumbiegel, Mandy" uniqKey="Krumbiegel M" first="Mandy" last="Krumbiegel">Mandy Krumbiegel</name><name sortKey="Marzi, Andrea" sort="Marzi, Andrea" uniqKey="Marzi A" first="Andrea" last="Marzi">Andrea Marzi</name><name sortKey="Peipp, Matthias" sort="Peipp, Matthias" uniqKey="Peipp M" first="Matthias" last="Peipp">Matthias Peipp</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name></noCountry><country name="Allemagne"><region name="Bavière"><name sortKey="Hofmann, Heike" sort="Hofmann, Heike" uniqKey="Hofmann H" first="Heike" last="Hofmann">Heike Hofmann</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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