Angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus.
Identifieur interne : 002A44 ( PubMed/Curation ); précédent : 002A43; suivant : 002A45Angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus.
Auteurs : J H Kuhn [États-Unis] ; W. Li ; H. Choe ; M. FarzanSource :
- Cellular and molecular life sciences : CMLS [ 1420-682X ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux, Carboxypeptidases (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (métabolisme), Syndrome respiratoire aigu sévère (virologie), Virus du SRAS (), Virus du SRAS (physiologie).
- MESH :
- métabolisme : Carboxypeptidases, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux.
- physiologie : Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Animaux, Glycoprotéine de spicule des coronavirus, Humains, Peptidyl-Dipeptidase A, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Carboxypeptidases (metabolism), Humans, Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A, Receptors, Virus (metabolism), SARS Virus (chemistry), SARS Virus (physiology), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , metabolism : Carboxypeptidases, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemistry : SARS Virus.
- physiology : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Humans, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus.
Abstract
Cellular entry of enveloped viruses is often dependent on attachment proteins expressed on the host cell surface. Viral envelope proteins bind these receptors, and, in an incompletely understood process, facilitate fusion of the cellular and viral membranes so as to introduce the viral core into the cytoplasm. Only a small fraction of viral receptors have been identified so far. Recently, a novel coronavirus was identified as the etiological agent of severe acute respiratory syndrome (SARS). The fusion protein gene of SARS coronavirus (SARS-CoV) was cloned and characterized, and shortly thereafter, angiotensin-converting enzyme 2 (ACE2) was shown to be its functional receptor. Identification of ACE2 as a receptor for SARS-CoV will likely contribute to the development of antivirals and vaccines. It may also contribute to the development of additional animal models for studying SARS pathogenesis, and could help identify the animal reservoir of SARS-CoV.
DOI: 10.1007/s00018-004-4242-5
PubMed: 15549175
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Farzan</name></author></analytic><series><title level="j">Cellular and molecular life sciences : CMLS</title><idno type="ISSN">1420-682X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Carboxypeptidases (metabolism)</term><term>Humans</term><term>Membrane Glycoproteins (metabolism)</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (physiology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Carboxypeptidases (métabolisme)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Récepteurs viraux (métabolisme)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carboxypeptidases</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Peptidyl-Dipeptidase A</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Peptidyl-Dipeptidase A</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellular entry of enveloped viruses is often dependent on attachment proteins expressed on the host cell surface. Viral envelope proteins bind these receptors, and, in an incompletely understood process, facilitate fusion of the cellular and viral membranes so as to introduce the viral core into the cytoplasm. Only a small fraction of viral receptors have been identified so far. Recently, a novel coronavirus was identified as the etiological agent of severe acute respiratory syndrome (SARS). The fusion protein gene of SARS coronavirus (SARS-CoV) was cloned and characterized, and shortly thereafter, angiotensin-converting enzyme 2 (ACE2) was shown to be its functional receptor. Identification of ACE2 as a receptor for SARS-CoV will likely contribute to the development of antivirals and vaccines. It may also contribute to the development of additional animal models for studying SARS pathogenesis, and could help identify the animal reservoir of SARS-CoV.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15549175</PMID><DateCompleted><Year>2004</Year><Month>12</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1420-682X</ISSN><JournalIssue CitedMedium="Print"><Volume>61</Volume><Issue>21</Issue><PubDate><Year>2004</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Cellular and molecular life sciences : CMLS</Title><ISOAbbreviation>Cell. Mol. Life Sci.</ISOAbbreviation></Journal><ArticleTitle>Angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus.</ArticleTitle><Pagination><MedlinePgn>2738-43</MedlinePgn></Pagination><Abstract><AbstractText>Cellular entry of enveloped viruses is often dependent on attachment proteins expressed on the host cell surface. Viral envelope proteins bind these receptors, and, in an incompletely understood process, facilitate fusion of the cellular and viral membranes so as to introduce the viral core into the cytoplasm. Only a small fraction of viral receptors have been identified so far. Recently, a novel coronavirus was identified as the etiological agent of severe acute respiratory syndrome (SARS). The fusion protein gene of SARS coronavirus (SARS-CoV) was cloned and characterized, and shortly thereafter, angiotensin-converting enzyme 2 (ACE2) was shown to be its functional receptor. Identification of ACE2 as a receptor for SARS-CoV will likely contribute to the development of antivirals and vaccines. 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