Severe acute respiratory syndrome coronavirus entry into host cells: Opportunities for therapeutic intervention.
Identifieur interne : 003D11 ( Main/Exploration ); précédent : 003D10; suivant : 003D12Severe acute respiratory syndrome coronavirus entry into host cells: Opportunities for therapeutic intervention.
Auteurs : Kap-Sun Yeung [États-Unis] ; Gregory A. Yamanaka ; Nicholas A. MeanwellSource :
- Medicinal research reviews [ 0198-6325 ] ; 2006.
Descripteurs français
- KwdFr :
- Anticorps monoclonaux (), Antiviraux (pharmacologie), Concentration inhibitrice 50, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Modèles chimiques, Modèles génétiques, Modèles moléculaires, Peptidyl-Dipeptidase A (physiologie), Protéines de l'enveloppe virale (métabolisme), Structure tertiaire des protéines, Syndrome respiratoire aigu sévère (), Syndrome respiratoire aigu sévère (anatomopathologie), Syndrome respiratoire aigu sévère (virologie), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie).
- MESH :
- anatomopathologie : Syndrome respiratoire aigu sévère.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- pathogénicité : Virus du SRAS.
- pharmacologie : Antiviraux.
- physiologie : Peptidyl-Dipeptidase A, Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Anticorps monoclonaux, Concentration inhibitrice 50, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Modèles chimiques, Modèles génétiques, Modèles moléculaires, Structure tertiaire des protéines, Syndrome respiratoire aigu sévère.
English descriptors
- KwdEn :
- Antibodies, Monoclonal (chemistry), Antiviral Agents (pharmacology), Crystallography, X-Ray, Inhibitory Concentration 50, Membrane Glycoproteins (metabolism), Models, Chemical, Models, Genetic, Models, Molecular, Peptidyl-Dipeptidase A (physiology), Protein Structure, Tertiary, SARS Virus (pathogenicity), SARS Virus (physiology), Severe Acute Respiratory Syndrome (pathology), Severe Acute Respiratory Syndrome (therapy), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Antibodies, Monoclonal.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , pharmacology : Antiviral Agents.
- chemical , physiology : Peptidyl-Dipeptidase A.
- pathogenicity : SARS Virus.
- pathology : Severe Acute Respiratory Syndrome.
- physiology : SARS Virus.
- therapy : Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Crystallography, X-Ray, Inhibitory Concentration 50, Models, Chemical, Models, Genetic, Models, Molecular, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus.
Abstract
A novel human coronavirus (CoV) has been identified as the etiological agent that caused the severe acute respiratory syndrome (SARS) outbreak in 2003. The spike (S) protein of this virus is a type I surface glycoprotein that mediates binding of the virus to the host receptor and the subsequent fusion between the viral and host membranes. Because of its critical role in viral entry, the S protein is an important target for the development of anti-SARS CoV therapeutics and prophylactics. This article reviews the structure and function of the SARS CoV S protein in the context of its role in virus entry. Topics that are discussed include: the interaction between the S1 domain of the SARS spike protein and the cellular receptor, angiotensin converting enzyme 2 (ACE2), and the structural features of the ectodomain of ACE2; the antigenic determinants presented by the S protein and the nature of neutralizing monoclonal antibodies that are elicited in vivo; the structure of the 4,3-hydrophobic heptad repeats HR1 and HR2 of the S2 domain and their interaction to form a six-helical bundle during the final stages of fusion. Opportunities for the design and development of anti-SARS agents based on the inhibition of receptor binding, the therapeutic uses of S-directed monoclonal antibodies and inhibitors of HR1-HR2 complex formation are presented.
DOI: 10.1002/med.20055
PubMed: 16521129
Affiliations:
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Le document en format XML
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<term>Inhibitory Concentration 50</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Models, Chemical</term>
<term>Models, Genetic</term>
<term>Models, Molecular</term>
<term>Peptidyl-Dipeptidase A (physiology)</term>
<term>Protein Structure, Tertiary</term>
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<term>SARS Virus (physiology)</term>
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<term>Severe Acute Respiratory Syndrome (therapy)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
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<term>Viral Envelope Proteins (metabolism)</term>
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<term>Concentration inhibitrice 50</term>
<term>Cristallographie aux rayons X</term>
<term>Glycoprotéine de spicule des coronavirus</term>
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<term>Modèles moléculaires</term>
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<term>Syndrome respiratoire aigu sévère ()</term>
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<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Virus du SRAS (pathogénicité)</term>
<term>Virus du SRAS (physiologie)</term>
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<front><div type="abstract" xml:lang="en">A novel human coronavirus (CoV) has been identified as the etiological agent that caused the severe acute respiratory syndrome (SARS) outbreak in 2003. The spike (S) protein of this virus is a type I surface glycoprotein that mediates binding of the virus to the host receptor and the subsequent fusion between the viral and host membranes. Because of its critical role in viral entry, the S protein is an important target for the development of anti-SARS CoV therapeutics and prophylactics. This article reviews the structure and function of the SARS CoV S protein in the context of its role in virus entry. Topics that are discussed include: the interaction between the S1 domain of the SARS spike protein and the cellular receptor, angiotensin converting enzyme 2 (ACE2), and the structural features of the ectodomain of ACE2; the antigenic determinants presented by the S protein and the nature of neutralizing monoclonal antibodies that are elicited in vivo; the structure of the 4,3-hydrophobic heptad repeats HR1 and HR2 of the S2 domain and their interaction to form a six-helical bundle during the final stages of fusion. Opportunities for the design and development of anti-SARS agents based on the inhibition of receptor binding, the therapeutic uses of S-directed monoclonal antibodies and inhibitors of HR1-HR2 complex formation are presented.</div>
</front>
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