The S proteins of human coronavirus NL63 and severe acute respiratory syndrome coronavirus bind overlapping regions of ACE2.
Identifieur interne : 001A18 ( Ncbi/Merge ); précédent : 001A17; suivant : 001A19The S proteins of human coronavirus NL63 and severe acute respiratory syndrome coronavirus bind overlapping regions of ACE2.
Auteurs : Wenhui Li [États-Unis] ; Jianhua Sui ; I-Chueh Huang ; Jens H. Kuhn ; Sheli R. Radoshitzky ; Wayne A. Marasco ; Hyeryun Choe ; Michael FarzanSource :
- Virology [ 0042-6822 ] ; 2007.
Descripteurs français
- KwdFr :
- Coronavirus humain 229E (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Infections à coronavirus (métabolisme), Lignée cellulaire, Peptidyl-Dipeptidase A (métabolisme), Protéines de l'enveloppe virale (métabolisme), Récepteurs de surface cellulaire (métabolisme), Sites de fixation, Virus du SRAS (métabolisme), Virus du SRAS (pathogénicité).
- MESH :
- métabolisme : Coronavirus humain 229E, Glycoprotéines membranaires, Infections à coronavirus, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Récepteurs de surface cellulaire, Virus du SRAS.
- pathogénicité : Virus du SRAS.
- Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire, Sites de fixation.
English descriptors
- KwdEn :
- Binding Sites, Cell Line, Coronavirus 229E, Human (metabolism), Coronavirus Infections (metabolism), Humans, Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A (metabolism), Receptors, Cell Surface (metabolism), SARS Virus (metabolism), SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Cell Surface, Viral Envelope Proteins.
- metabolism : Coronavirus 229E, Human, Coronavirus Infections, SARS Virus.
- pathogenicity : SARS Virus.
- Binding Sites, Cell Line, Humans, Spike Glycoprotein, Coronavirus.
Abstract
The cellular receptor for human coronavirus NL63 (HCoV-NL63), a group I coronavirus, is angiotensin-converting enzyme2 (ACE2). ACE2 is also the receptor for the SARS coronavirus (SARS-CoV), a group II coronavirus. Here we describe the ability of HCoV-NL63 to utilize a number of ACE2 variants previously characterized as SARS-CoV receptors. Several ACE2 variants that reduced SARS-CoV S-protein association similarly reduced that of HCoV-NL63, whereas alteration of a number of solvent-exposed ACE2 residues did not interfere with binding by either S protein. One notable exception is ACE2 residue 354, at the boundary of the SARS-CoV binding site, whose alteration markedly inhibited utilization by the HCoV-NL63 but not SARS-CoV S proteins. In addition, the SARS-CoV S-protein receptor-binding domain inhibited entry mediated by the HCoV-NL63 S protein. These studies indicate that HCoV-NL63, like SARS-CoV, associates region of human ACE2 that includes a key loop formed by beta-strands 4 and 5.
DOI: 10.1016/j.virol.2007.04.035
PubMed: 17631932
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pubmed:17631932Le document en format XML
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<front><div type="abstract" xml:lang="en">The cellular receptor for human coronavirus NL63 (HCoV-NL63), a group I coronavirus, is angiotensin-converting enzyme2 (ACE2). ACE2 is also the receptor for the SARS coronavirus (SARS-CoV), a group II coronavirus. Here we describe the ability of HCoV-NL63 to utilize a number of ACE2 variants previously characterized as SARS-CoV receptors. Several ACE2 variants that reduced SARS-CoV S-protein association similarly reduced that of HCoV-NL63, whereas alteration of a number of solvent-exposed ACE2 residues did not interfere with binding by either S protein. One notable exception is ACE2 residue 354, at the boundary of the SARS-CoV binding site, whose alteration markedly inhibited utilization by the HCoV-NL63 but not SARS-CoV S proteins. In addition, the SARS-CoV S-protein receptor-binding domain inhibited entry mediated by the HCoV-NL63 S protein. These studies indicate that HCoV-NL63, like SARS-CoV, associates region of human ACE2 that includes a key loop formed by beta-strands 4 and 5.</div>
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<Abstract><AbstractText>The cellular receptor for human coronavirus NL63 (HCoV-NL63), a group I coronavirus, is angiotensin-converting enzyme2 (ACE2). ACE2 is also the receptor for the SARS coronavirus (SARS-CoV), a group II coronavirus. Here we describe the ability of HCoV-NL63 to utilize a number of ACE2 variants previously characterized as SARS-CoV receptors. Several ACE2 variants that reduced SARS-CoV S-protein association similarly reduced that of HCoV-NL63, whereas alteration of a number of solvent-exposed ACE2 residues did not interfere with binding by either S protein. One notable exception is ACE2 residue 354, at the boundary of the SARS-CoV binding site, whose alteration markedly inhibited utilization by the HCoV-NL63 but not SARS-CoV S proteins. In addition, the SARS-CoV S-protein receptor-binding domain inhibited entry mediated by the HCoV-NL63 S protein. These studies indicate that HCoV-NL63, like SARS-CoV, associates region of human ACE2 that includes a key loop formed by beta-strands 4 and 5.</AbstractText>
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<affiliations><list><country><li>États-Unis</li>
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<name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name>
<name sortKey="Huang, I Chueh" sort="Huang, I Chueh" uniqKey="Huang I" first="I-Chueh" last="Huang">I-Chueh Huang</name>
<name sortKey="Kuhn, Jens H" sort="Kuhn, Jens H" uniqKey="Kuhn J" first="Jens H" last="Kuhn">Jens H. Kuhn</name>
<name sortKey="Marasco, Wayne A" sort="Marasco, Wayne A" uniqKey="Marasco W" first="Wayne A" last="Marasco">Wayne A. Marasco</name>
<name sortKey="Radoshitzky, Sheli R" sort="Radoshitzky, Sheli R" uniqKey="Radoshitzky S" first="Sheli R" last="Radoshitzky">Sheli R. Radoshitzky</name>
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