Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2.
Identifieur interne : 003171 ( Main/Merge ); précédent : 003170; suivant : 003172Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2.
Auteurs : Alison C. Mathewson [Royaume-Uni] ; Alexandra Bishop [Royaume-Uni] ; Yongxiu Yao [Royaume-Uni] ; Fred Kemp [Royaume-Uni] ; Junyuan Ren [Royaume-Uni] ; Hongying Chen [Royaume-Uni] ; Xiaodong Xu [Royaume-Uni] ; Ben Berkhout [Pays-Bas] ; Lia Van Der Hoek [Pays-Bas] ; Ian M. Jones [Royaume-Uni]Source :
- The Journal of general virology [ 0022-1317 ] ; 2008.
Descripteurs français
- KwdFr :
- Cinétique, Coronavirus (physiologie), Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Indice de gravité médicale, Infections à coronavirus (physiopathologie), Liaison aux protéines, Peptidyl-Dipeptidase A (métabolisme), Protéines de l'enveloppe virale (métabolisme), Solutions, Syndrome respiratoire aigu sévère (physiopathologie), Virus du SRAS (physiologie).
- MESH :
- métabolisme : Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale.
- physiologie : Coronavirus, Virus du SRAS.
- physiopathologie : Infections à coronavirus, Syndrome respiratoire aigu sévère.
- Cinétique, Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Humains, Indice de gravité médicale, Liaison aux protéines, Solutions.
English descriptors
- KwdEn :
- Coronavirus (physiology), Coronavirus Infections (physiopathology), Flow Cytometry, Humans, Kinetics, Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A (metabolism), Protein Binding, SARS Virus (physiology), Severe Acute Respiratory Syndrome (physiopathology), Severity of Illness Index, Solutions, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Viral Envelope Proteins.
- physiology : Coronavirus, SARS Virus.
- physiopathology : Coronavirus Infections, Severe Acute Respiratory Syndrome.
- Flow Cytometry, Humans, Kinetics, Protein Binding, Severity of Illness Index, Solutions, Spike Glycoprotein, Coronavirus.
Abstract
Although in different groups, the coronaviruses severe acute respiratory syndrome-coronavirus (SARS-CoV) and NL63 use the same receptor, angiotensin converting enzyme (ACE)-2, for entry into the host cell. Despite this common receptor, the consequence of entry is very different; severe respiratory distress in the case of SARS-CoV but frequently only a mild respiratory infection for NL63. Using a wholly recombinant system, we have investigated the ability of each virus receptor-binding protein, spike or S protein, to bind to ACE-2 in solution and on the cell surface. In both assays, we find that the NL63 S protein has a weaker interaction with ACE-2 than the SARS-CoV S protein, particularly in solution binding, but the residues required for contact are similar. We also confirm that the ACE-2-binding site of NL63 S lies between residues 190 and 739. A lower-affinity interaction with ACE-2 might partly explain the different pathological consequences of infection by SARS-CoV and NL63.
DOI: 10.1099/vir.0.2008/003962-0
PubMed: 18931070
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Mathewson</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author><author><name sortKey="Bishop, Alexandra" sort="Bishop, Alexandra" uniqKey="Bishop A" first="Alexandra" last="Bishop">Alexandra Bishop</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author><author><name sortKey="Yao, Yongxiu" sort="Yao, Yongxiu" uniqKey="Yao Y" first="Yongxiu" last="Yao">Yongxiu 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wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author><author><name sortKey="Chen, Hongying" sort="Chen, Hongying" uniqKey="Chen H" first="Hongying" last="Chen">Hongying Chen</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author><author><name sortKey="Xu, Xiaodong" sort="Xu, Xiaodong" uniqKey="Xu X" first="Xiaodong" last="Xu">Xiaodong Xu</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author><author><name sortKey="Berkhout, Ben" sort="Berkhout, Ben" uniqKey="Berkhout B" first="Ben" last="Berkhout">Ben Berkhout</name><affiliation wicri:level="4"><nlm:affiliation>Laboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam (CINIMA), Academic Medical Center of the University of Amsterdam, K3-110, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam (CINIMA), Academic Medical Center of the University of Amsterdam, K3-110, Meibergdreef 15, 1105 AZ Amsterdam</wicri:regionArea><orgName type="university">Université d'Amsterdam</orgName><placeName><settlement type="city">Amsterdam</settlement><region>Hollande-Septentrionale</region></placeName></affiliation></author><author><name sortKey="Van Der Hoek, Lia" sort="Van Der Hoek, Lia" uniqKey="Van Der Hoek L" first="Lia" last="Van Der Hoek">Lia Van Der Hoek</name><affiliation wicri:level="4"><nlm:affiliation>Laboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam (CINIMA), Academic Medical Center of the University of Amsterdam, K3-110, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam (CINIMA), Academic Medical Center of the University of Amsterdam, K3-110, Meibergdreef 15, 1105 AZ Amsterdam</wicri:regionArea><orgName type="university">Université d'Amsterdam</orgName><placeName><settlement type="city">Amsterdam</settlement><region>Hollande-Septentrionale</region></placeName></affiliation></author><author><name sortKey="Jones, Ian M" sort="Jones, Ian M" uniqKey="Jones I" first="Ian M" last="Jones">Ian M. Jones</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of general virology</title><idno type="ISSN">0022-1317</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus (physiology)</term><term>Coronavirus Infections (physiopathology)</term><term>Flow Cytometry</term><term>Humans</term><term>Kinetics</term><term>Membrane Glycoproteins (metabolism)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Protein Binding</term><term>SARS Virus (physiology)</term><term>Severe Acute Respiratory Syndrome (physiopathology)</term><term>Severity of Illness Index</term><term>Solutions</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique</term><term>Coronavirus (physiologie)</term><term>Cytométrie en flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Indice de gravité médicale</term><term>Infections à coronavirus (physiopathologie)</term><term>Liaison aux protéines</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Solutions</term><term>Syndrome respiratoire aigu sévère (physiopathologie)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="physiopathologie" xml:lang="fr"><term>Infections à coronavirus</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Coronavirus Infections</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Flow Cytometry</term><term>Humans</term><term>Kinetics</term><term>Protein Binding</term><term>Severity of Illness Index</term><term>Solutions</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Cytométrie en flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Indice de gravité médicale</term><term>Liaison aux protéines</term><term>Solutions</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Although in different groups, the coronaviruses severe acute respiratory syndrome-coronavirus (SARS-CoV) and NL63 use the same receptor, angiotensin converting enzyme (ACE)-2, for entry into the host cell. Despite this common receptor, the consequence of entry is very different; severe respiratory distress in the case of SARS-CoV but frequently only a mild respiratory infection for NL63. Using a wholly recombinant system, we have investigated the ability of each virus receptor-binding protein, spike or S protein, to bind to ACE-2 in solution and on the cell surface. In both assays, we find that the NL63 S protein has a weaker interaction with ACE-2 than the SARS-CoV S protein, particularly in solution binding, but the residues required for contact are similar. We also confirm that the ACE-2-binding site of NL63 S lies between residues 190 and 739. A lower-affinity interaction with ACE-2 might partly explain the different pathological consequences of infection by SARS-CoV and NL63.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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