Receptor and viral determinants of SARS‐coronavirus adaptation to human ACE2
Identifieur interne : 000293 ( Istex/Curation ); précédent : 000292; suivant : 000294Receptor and viral determinants of SARS‐coronavirus adaptation to human ACE2
Auteurs : Wenhui Li [États-Unis] ; Chengsheng Zhang [Canada, République populaire de Chine] ; Jianhua Sui [États-Unis] ; Jens H. Kuhn [États-Unis, Allemagne] ; Michael J. Moore [États-Unis] ; Shiwen Luo [République populaire de Chine] ; Swee-Kee Wong [États-Unis] ; I-Chueh Huang [États-Unis] ; Keming Xu [République populaire de Chine] ; Natalya Vasilieva [États-Unis] ; Akikazu Murakami [États-Unis] ; Yaqing He [République populaire de Chine] ; Wayne A. Marasco [États-Unis] ; Yi Guan [République populaire de Chine, Hong Kong] ; Hyeryun Choe [États-Unis, Hong Kong] ; Michael Farzan [États-Unis, Hong Kong]Source :
- The EMBO Journal [ 0261-4189 ] ; 2005-04-20.
English descriptors
- Teeft :
- Accession number, Ace2, Ace2 variants, Asparagine, Biology organization, Biology organization adaptation, Cells transfected, Chimera, Civet, Civet ace2, Collectrin, Collectrin domain, Coronavirus, Cytometry, Embo, Embo journal, Encoding, Farzan, Functional receptor, Glycoprotein, Guan, Human ace2, Liang, Lysine, Murine, Outbreak, Palm civet, Palm civets, Plasmid, Plasmid encoding, Plasmids encoding, Pseudotyped, Rbds, Receptor, Residue, Respiratory syndrome, Respiratory syndrome coronavirus, Sars, Sars coronavirus, Syndrome, Threonine, Tor2, Transfected, Variant, Virol, Wang, Wong, Zhang, Zheng.
Abstract
Human angiotensin‐converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS‐CoV). Here we identify the SARS‐CoV spike (S)‐protein‐binding site on ACE2. We also compare S proteins of SARS‐CoV isolated during the 2002–2003 SARS outbreak and during the much less severe 2003–2004 outbreak, and from palm civets, a possible source of SARS‐CoV found in humans. All three S proteins bound to and utilized palm‐civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S‐protein‐binding site of human ACE2 to those of civet ACE2, or by altering S‐protein residues 479 and 487 to residues conserved during the 2002–2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS‐CoV to human cells, and provide insight into the severity of the 2002–2003 SARS epidemic.
Url:
DOI: 10.1038/sj.emboj.7600640
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<author><name sortKey="Wong, Swee Ee" sort="Wong, Swee Ee" uniqKey="Wong S" first="Swee-Kee" last="Wong">Swee-Kee Wong</name>
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<author><name sortKey="Huang, I Hueh" sort="Huang, I Hueh" uniqKey="Huang I" first="I-Chueh" last="Huang">I-Chueh Huang</name>
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<author><name sortKey="Xu, Keming" sort="Xu, Keming" uniqKey="Xu K" first="Keming" last="Xu">Keming Xu</name>
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<author><name sortKey="He, Yaqing" sort="He, Yaqing" uniqKey="He Y" first="Yaqing" last="He">Yaqing He</name>
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<author><name sortKey="Marasco, Wayne A" sort="Marasco, Wayne A" uniqKey="Marasco W" first="Wayne A" last="Marasco">Wayne A. Marasco</name>
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<author><name sortKey="Guan, Yi" sort="Guan, Yi" uniqKey="Guan Y" first="Yi" last="Guan">Yi Guan</name>
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<author><name sortKey="Choe, Hyeryun" sort="Choe, Hyeryun" uniqKey="Choe H" first="Hyeryun" last="Choe">Hyeryun Choe</name>
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<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Accession number</term>
<term>Ace2</term>
<term>Ace2 variants</term>
<term>Asparagine</term>
<term>Biology organization</term>
<term>Biology organization adaptation</term>
<term>Cells transfected</term>
<term>Chimera</term>
<term>Civet</term>
<term>Civet ace2</term>
<term>Collectrin</term>
<term>Collectrin domain</term>
<term>Coronavirus</term>
<term>Cytometry</term>
<term>Embo</term>
<term>Embo journal</term>
<term>Encoding</term>
<term>Farzan</term>
<term>Functional receptor</term>
<term>Glycoprotein</term>
<term>Guan</term>
<term>Human ace2</term>
<term>Liang</term>
<term>Lysine</term>
<term>Murine</term>
<term>Outbreak</term>
<term>Palm civet</term>
<term>Palm civets</term>
<term>Plasmid</term>
<term>Plasmid encoding</term>
<term>Plasmids encoding</term>
<term>Pseudotyped</term>
<term>Rbds</term>
<term>Receptor</term>
<term>Residue</term>
<term>Respiratory syndrome</term>
<term>Respiratory syndrome coronavirus</term>
<term>Sars</term>
<term>Sars coronavirus</term>
<term>Syndrome</term>
<term>Threonine</term>
<term>Tor2</term>
<term>Transfected</term>
<term>Variant</term>
<term>Virol</term>
<term>Wang</term>
<term>Wong</term>
<term>Zhang</term>
<term>Zheng</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract">Human angiotensin‐converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS‐CoV). Here we identify the SARS‐CoV spike (S)‐protein‐binding site on ACE2. We also compare S proteins of SARS‐CoV isolated during the 2002–2003 SARS outbreak and during the much less severe 2003–2004 outbreak, and from palm civets, a possible source of SARS‐CoV found in humans. All three S proteins bound to and utilized palm‐civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S‐protein‐binding site of human ACE2 to those of civet ACE2, or by altering S‐protein residues 479 and 487 to residues conserved during the 2002–2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS‐CoV to human cells, and provide insight into the severity of the 2002–2003 SARS epidemic.</div>
</front>
</TEI>
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