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Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2

Identifieur interne : 003493 ( Main/Exploration ); précédent : 003492; suivant : 003494

Interaction 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 :

RBID : Pascal:08-0506391

Descripteurs français

English descriptors

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.


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Le document en format XML

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<term>Interaction</term>
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</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="Pascal" xml:lang="fr">
<term>Cinétique</term>
<term>Coronavirus</term>
<term>Cytométrie en flux</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Humains</term>
<term>Indice de gravité médicale</term>
<term>Interaction</term>
<term>Liaison aux protéines</term>
<term>Protéine</term>
<term>Microbiologie</term>
<term>Solutions</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Angiotensin converting enzyme 2</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>
<affiliations>
<list>
<country>
<li>Pays-Bas</li>
<li>Royaume-Uni</li>
</country>
<region>
<li>Hollande-Septentrionale</li>
</region>
<settlement>
<li>Amsterdam</li>
</settlement>
<orgName>
<li>Université d'Amsterdam</li>
</orgName>
</list>
<tree>
<country name="Royaume-Uni">
<noRegion>
<name sortKey="Mathewson, Alison C" sort="Mathewson, Alison C" uniqKey="Mathewson A" first="Alison C." last="Mathewson">Alison C. Mathewson</name>
</noRegion>
<name sortKey="Bishop, Alexandra" sort="Bishop, Alexandra" uniqKey="Bishop A" first="Alexandra" last="Bishop">Alexandra Bishop</name>
<name sortKey="Hongying Chen" sort="Hongying Chen" uniqKey="Hongying Chen" last="Hongying Chen">HONGYING CHEN</name>
<name sortKey="Jones, Ian M" sort="Jones, Ian M" uniqKey="Jones I" first="Ian M." last="Jones">Ian M. Jones</name>
<name sortKey="Junyuan Ren" sort="Junyuan Ren" uniqKey="Junyuan Ren" last="Junyuan Ren">JUNYUAN REN</name>
<name sortKey="Kemp, Fred" sort="Kemp, Fred" uniqKey="Kemp F" first="Fred" last="Kemp">Fred Kemp</name>
<name sortKey="Xiaodong Xu" sort="Xiaodong Xu" uniqKey="Xiaodong Xu" last="Xiaodong Xu">XIAODONG XU</name>
<name sortKey="Yongxiu Yao" sort="Yongxiu Yao" uniqKey="Yongxiu Yao" last="Yongxiu Yao">YONGXIU YAO</name>
</country>
<country name="Pays-Bas">
<region name="Hollande-Septentrionale">
<name sortKey="Berkhout, Ben" sort="Berkhout, Ben" uniqKey="Berkhout B" first="Ben" last="Berkhout">Ben Berkhout</name>
</region>
<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>
</country>
</tree>
</affiliations>
</record>

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