Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Identifieur interne : 006418 ( Main/Exploration ); précédent : 006417; suivant : 006419Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Auteurs : WENHUI LI [États-Unis] ; Michael J. Moore [États-Unis] ; Natalya Vasilleva [États-Unis] ; JIANHUA SUI [États-Unis] ; SWEE KEE WONG [États-Unis] ; Michael A. Berne [États-Unis] ; Mohan Somasundaran [États-Unis] ; John L. Sullivan [États-Unis] ; Katherine Luzuriaga [États-Unis] ; Thomas C. Greenough [États-Unis] ; HYERYUN CHOE [États-Unis] ; Michael Farzan [États-Unis]Source :
- Nature : (London) [ 0028-0836 ] ; 2003.
Descripteurs français
- Pascal (Inist)
English descriptors
Abstract
Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells1,2. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2)3,4, isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.
Affiliations:
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Berne</name><affiliation wicri:level="1"><inist:fA14 i1="04"><s1>Tufts University Core Facility, Tufts University School of Medicine</s1><s2>Boston, Massachusetts 02111</s2><s3>USA</s3><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Boston, Massachusetts 02111</wicri:noRegion></affiliation></author><author><name sortKey="Somasundaran, Mohan" sort="Somasundaran, Mohan" uniqKey="Somasundaran M" first="Mohan" last="Somasundaran">Mohan Somasundaran</name><affiliation wicri:level="1"><inist:fA14 i1="05"><s1>Program in Molecular Medicine, University of Massachusetts Medical School</s1><s2>Worcester, Massachusetts 01605</s2><s3>USA</s3><sZ>7 aut.</sZ><sZ>8 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Worcester, Massachusetts 01605</wicri:noRegion></affiliation></author><author><name sortKey="Sullivan, John L" sort="Sullivan, John L" uniqKey="Sullivan J" first="John L." last="Sullivan">John L. 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Greenough</name><affiliation wicri:level="1"><inist:fA14 i1="05"><s1>Program in Molecular Medicine, University of Massachusetts Medical School</s1><s2>Worcester, Massachusetts 01605</s2><s3>USA</s3><sZ>7 aut.</sZ><sZ>8 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Worcester, Massachusetts 01605</wicri:noRegion></affiliation></author><author><name sortKey="Hyeryun Choe" sort="Hyeryun Choe" uniqKey="Hyeryun Choe" last="Hyeryun Choe">HYERYUN CHOE</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Perlmutter Laboratory, Pulmonary Division, Children's Hospital, Department of Pediatrics, Harvard Medical School</s1><s2>Boston, Massachusetts 02115</s2><s3>USA</s3><sZ>3 aut.</sZ><sZ>11 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Boston, Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Partners AIDS Research Center, Brigham and Women's Hospital, Department of Medicine (Microbiology and Molecular Genetics), Harvard Medical School</s1><s2>Boston, Massachusetts 02115</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>5 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Boston, Massachusetts 02115</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Nature : (London)</title><title level="j" type="abbreviated">Nature : (Lond.)</title><idno type="ISSN">0028-0836</idno><imprint><date when="2003">2003</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Nature : (London)</title><title level="j" type="abbreviated">Nature : (Lond.)</title><idno type="ISSN">0028-0836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological receptor</term><term>Coronavirus</term><term>Peptidyl-dipeptidase A</term><term>Respiratory disease</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term><term>Récepteur biologique</term><term>Peptidyl-dipeptidase A</term><term>Appareil respiratoire pathologie</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells<sup>1,2</sup>. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2)<sup>3,4</sup>, isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Wenhui Li" sort="Wenhui Li" uniqKey="Wenhui Li" last="Wenhui Li">WENHUI LI</name></noRegion><name sortKey="Berne, Michael A" sort="Berne, Michael A" uniqKey="Berne M" first="Michael A." last="Berne">Michael A. Berne</name><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name><name sortKey="Greenough, Thomas C" sort="Greenough, Thomas C" uniqKey="Greenough T" first="Thomas C." last="Greenough">Thomas C. Greenough</name><name sortKey="Hyeryun Choe" sort="Hyeryun Choe" uniqKey="Hyeryun Choe" last="Hyeryun Choe">HYERYUN CHOE</name><name sortKey="Jianhua Sui" sort="Jianhua Sui" uniqKey="Jianhua Sui" last="Jianhua Sui">JIANHUA SUI</name><name sortKey="Luzuriaga, Katherine" sort="Luzuriaga, Katherine" uniqKey="Luzuriaga K" first="Katherine" last="Luzuriaga">Katherine Luzuriaga</name><name sortKey="Moore, Michael J" sort="Moore, Michael J" uniqKey="Moore M" first="Michael J." last="Moore">Michael J. Moore</name><name sortKey="Somasundaran, Mohan" sort="Somasundaran, Mohan" uniqKey="Somasundaran M" first="Mohan" last="Somasundaran">Mohan Somasundaran</name><name sortKey="Sullivan, John L" sort="Sullivan, John L" uniqKey="Sullivan J" first="John L." last="Sullivan">John L. Sullivan</name><name sortKey="Swee Kee Wong" sort="Swee Kee Wong" uniqKey="Swee Kee Wong" last="Swee Kee Wong">SWEE KEE WONG</name><name sortKey="Vasilleva, Natalya" sort="Vasilleva, Natalya" uniqKey="Vasilleva N" first="Natalya" last="Vasilleva">Natalya Vasilleva</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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