What’s new in the renin-angiotensin system?
Identifieur interne : 005607 ( Main/Exploration ); précédent : 005606; suivant : 005608What’s new in the renin-angiotensin system?
Auteurs : J. H. Kuhn [États-Unis, Allemagne] ; W. Li [États-Unis, Allemagne] ; H. Choe [États-Unis] ; M. Farzan [États-Unis]Source :
- Cellular and Molecular Life Sciences CMLS [ 1420-682X ] ; 2004-11-01.
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 :
- ACE2, Animals, Carboxypeptidases (metabolism), Humans, Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A, Receptors, Virus (metabolism), SARS, SARS Virus (chemistry), SARS Virus (physiology), Severe Acute Respiratory Syndrome (virology), Severe acute respiratory syndrome, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), angiotensin-converting enzyme 2, coronavirus, viral fusion.
- 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
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.
Url:
DOI: 10.1007/s00018-004-4242-5
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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