Inhibition of the interaction between the SARS-CoV Spike protein and its cellular receptor by anti-histo-blood group antibodies
Identifieur interne : 000E13 ( Pmc/Checkpoint ); précédent : 000E12; suivant : 000E14Inhibition of the interaction between the SARS-CoV Spike protein and its cellular receptor by anti-histo-blood group antibodies
Auteurs : Patrice Guillon [France] ; Monique Clément [France] ; Véronique Sébille [France] ; Jean-Gérard Rivain [France] ; Chih-Fong Chou [Singapour] ; Nathalie Ruvoën-Clouet ; Jacques Le Pendu [France]Source :
- Glycobiology [ 0959-6658 ] ; 2008.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) is a highly pathogenic emergent virus which replicates in cells that can express ABH histo-blood group antigens. The heavily glycosylated SARS-CoV spike (S) protein binds to angiotensin-converting enzyme 2 which serves as a cellular receptor. Epidemiological analysis of a hospital outbreak in Hong Kong revealed that blood group O was associated with a low risk of infection. In this study, we used a cellular model of adhesion to investigate whether natural antibodies of the ABO system could block the S protein and angiotensin-converting enzyme 2 interaction. To this aim, a C-terminally EGFP-tagged S protein was expressed in chinese hamster ovary cells cotransfected with an α1,2-fucosyltransferase and an A-transferase in order to coexpress the S glycoprotein ectodomain and the A antigen at the cell surface. We observed that the S protein/angiotensin-converting enzyme 2-dependent adhesion of these cells to an angiotensin-converting enzyme 2 expressing cell line was specifically inhibited by either a monoclonal or human natural anti-A antibodies, indicating that these antibodies may block the interaction between the virus and its receptor, thereby providing protection. In order to more fully appreciate the potential effect of the ABO polymorphism on the epidemiology of SARS, we built a mathematical model of the virus transmission dynamics that takes into account the protective effect of ABO natural antibodies. The model indicated that the ABO polymorphism could contribute to substantially reduce the virus transmission, affecting both the number of infected individuals and the kinetics of the epidemic.
Url:
DOI: 10.1093/glycob/cwn093
PubMed: 18818423
PubMed Central: 7108609
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uniqKey="Clement M" first="Monique" last="Clément">Monique Clément</name><affiliation wicri:level="1"><nlm:aff id="af1"><addr-line>French National Institute for Health and Medical Research (INSERM), U892</addr-line>,<institution>University of Nantes</institution>,<addr-line>44035 Nantes</addr-line>,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Sebille, Veronique" sort="Sebille, Veronique" uniqKey="Sebille V" first="Véronique" last="Sébille">Véronique Sébille</name><affiliation wicri:level="1"><nlm:aff id="af2"><addr-line>EA 4275</addr-line>,<institution>University of Nantes</institution>,<addr-line>44035 Nantes</addr-line>,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Rivain, Jean Gerard" sort="Rivain, Jean Gerard" uniqKey="Rivain J" first="Jean-Gérard" last="Rivain">Jean-Gérard Rivain</name><affiliation wicri:level="1"><nlm:aff id="af2"><addr-line>EA 4275</addr-line>,<institution>University of Nantes</institution>,<addr-line>44035 Nantes</addr-line>,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Chou, Chih Fong" sort="Chou, Chih Fong" uniqKey="Chou C" first="Chih-Fong" last="Chou">Chih-Fong Chou</name><affiliation wicri:level="1"><nlm:aff id="af3"><institution>Institute of Molecular and Cell Biology</institution>,<addr-line>Singapore 138673</addr-line>,<country>Singapore</country></nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Ruvoen Clouet, Nathalie" sort="Ruvoen Clouet, Nathalie" uniqKey="Ruvoen Clouet N" first="Nathalie" last="Ruvoën-Clouet">Nathalie Ruvoën-Clouet</name></author><author><name sortKey="Le Pendu, Jacques" sort="Le Pendu, Jacques" uniqKey="Le Pendu J" first="Jacques" last="Le Pendu">Jacques Le Pendu</name><affiliation wicri:level="1"><nlm:aff id="af1"><addr-line>French National Institute for Health and Medical Research (INSERM), U892</addr-line>,<institution>University of Nantes</institution>,<addr-line>44035 Nantes</addr-line>,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Glycobiology</title><idno type="ISSN">0959-6658</idno><idno type="eISSN">1460-2423</idno><imprint><date when="2008">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Severe acute respiratory syndrome coronavirus (SARS-CoV) is a highly pathogenic emergent virus which replicates in cells that can express ABH histo-blood group antigens. The heavily glycosylated SARS-CoV spike (S) protein binds to angiotensin-converting enzyme 2 which serves as a cellular receptor. Epidemiological analysis of a hospital outbreak in Hong Kong revealed that blood group O was associated with a low risk of infection. In this study, we used a cellular model of adhesion to investigate whether natural antibodies of the ABO system could block the S protein and angiotensin-converting enzyme 2 interaction. To this aim, a C-terminally EGFP-tagged S protein was expressed in chinese hamster ovary cells cotransfected with an α1,2-fucosyltransferase and an A-transferase in order to coexpress the S glycoprotein ectodomain and the A antigen at the cell surface. We observed that the S protein/angiotensin-converting enzyme 2-dependent adhesion of these cells to an angiotensin-converting enzyme 2 expressing cell line was specifically inhibited by either a monoclonal or human natural anti-A antibodies, indicating that these antibodies may block the interaction between the virus and its receptor, thereby providing protection. In order to more fully appreciate the potential effect of the ABO polymorphism on the epidemiology of SARS, we built a mathematical model of the virus transmission dynamics that takes into account the protective effect of ABO natural antibodies. The model indicated that the ABO polymorphism could contribute to substantially reduce the virus transmission, affecting both the number of infected individuals and the kinetics of the epidemic.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Anderson, Rm" uniqKey="Anderson R">RM Anderson</name></author><author><name sortKey="Fraser, C" uniqKey="Fraser C">C Fraser</name></author><author><name sortKey="Ghani, Ac" uniqKey="Ghani A">AC Ghani</name></author><author><name sortKey="Donnelly, Ca" uniqKey="Donnelly C">CA Donnelly</name></author><author><name sortKey="Riley, S" uniqKey="Riley S">S Riley</name></author><author><name sortKey="Fergusson, Nm" uniqKey="Fergusson N">NM Fergusson</name></author><author><name sortKey="Leung, Gm" uniqKey="Leung G">GM Leung</name></author><author><name sortKey="Lam, Th" uniqKey="Lam T">TH Lam</name></author><author><name sortKey="Hedley, Aj" uniqKey="Hedley A">AJ 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Glycobiology</journal-id><journal-id journal-id-type="iso-abbrev">Glycobiology</journal-id><journal-id journal-id-type="publisher-id">glycob</journal-id><journal-id journal-id-type="hwp">glycob</journal-id><journal-title-group><journal-title>Glycobiology</journal-title></journal-title-group><issn pub-type="ppub">0959-6658</issn><issn pub-type="epub">1460-2423</issn><publisher><publisher-name>Oxford University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">18818423</article-id><article-id pub-id-type="pmc">7108609</article-id><article-id pub-id-type="doi">10.1093/glycob/cwn093</article-id><article-id pub-id-type="publisher-id">cwn093</article-id><article-categories><subj-group subj-group-type="heading"><subject>Original Articles</subject></subj-group></article-categories><title-group><article-title>Inhibition of the interaction between the SARS-CoV Spike protein and its cellular receptor by anti-histo-blood group antibodies</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Guillon</surname><given-names>Patrice</given-names></name><xref ref-type="aff" rid="af1">3</xref></contrib><contrib contrib-type="author"><name><surname>Clément</surname><given-names>Monique</given-names></name><xref ref-type="aff" rid="af1">3</xref></contrib><contrib contrib-type="author"><name><surname>Sébille</surname><given-names>Véronique</given-names></name><xref ref-type="aff" rid="af2">4</xref></contrib><contrib contrib-type="author"><name><surname>Rivain</surname><given-names>Jean-Gérard</given-names></name><xref ref-type="aff" rid="af2">4</xref></contrib><contrib contrib-type="author"><name><surname>Chou</surname><given-names>Chih-Fong</given-names></name><xref ref-type="aff" rid="af3">5</xref></contrib><contrib contrib-type="author"><name><surname>Ruvoën-Clouet</surname><given-names>Nathalie</given-names></name><xref ref-type="aff" rid="af1 af4">3,6</xref></contrib><contrib contrib-type="author"><name><surname>Le Pendu</surname><given-names>Jacques</given-names></name><xref ref-type="corresp" rid="COR1">1</xref><xref ref-type="aff" rid="af1">3</xref><pmc-comment>jlependu@nantes.inserm.fr </pmc-comment>
</contrib></contrib-group><aff id="af1"><label>3</label><addr-line>French National Institute for Health and Medical Research (INSERM), U892</addr-line>,<institution>University of Nantes</institution>,<addr-line>44035 Nantes</addr-line>,<country>France</country></aff><aff id="af2"><label>4</label><addr-line>EA 4275</addr-line>,<institution>University of Nantes</institution>,<addr-line>44035 Nantes</addr-line>,<country>France</country></aff><aff id="af3"><label>5</label><institution>Institute of Molecular and Cell Biology</institution>,<addr-line>Singapore 138673</addr-line>,<country>Singapore</country></aff><aff id="af4"><label>6</label><addr-line>Ecole Nationale Vétérinaire de Nantes, 44035 Nantes</addr-line>,<country>France</country></aff><author-notes><corresp id="COR1"><label>1</label>To whom correspondence should be addressed: Tel: <phone>+33-240-08-40-99</phone>; Fax: <fax>+33-240-08-40-82</fax>; e-mail: <email>jlependu@nantes.inserm.fr</email></corresp><fn id="AFN1"><label>2</label><p>These authors contributed equally to the work.</p></fn></author-notes><pub-date pub-type="ppub"><month>12</month><year>2008</year></pub-date><pub-date pub-type="epub" iso-8601-date="2008-09-25"><day>25</day><month>9</month><year>2008</year></pub-date><volume>18</volume><issue>12</issue><fpage>1085</fpage><lpage>1093</lpage><history><date date-type="received"><day>4</day><month>6</month><year>2008</year></date><date date-type="rev-recd"><day>15</day><month>9</month><year>2008</year></date><date date-type="accepted"><day>22</day><month>9</month><year>2008</year></date></history><permissions><copyright-statement>© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org</copyright-statement><copyright-year>2008</copyright-year><copyright-holder>Oxford University Press</copyright-holder><license><license-p>This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.</license-p></license></permissions><self-uri xlink:href="cwn093.pdf"></self-uri><abstract><title>Abstract</title><p>Severe acute respiratory syndrome coronavirus (SARS-CoV) is a highly pathogenic emergent virus which replicates in cells that can express ABH histo-blood group antigens. The heavily glycosylated SARS-CoV spike (S) protein binds to angiotensin-converting enzyme 2 which serves as a cellular receptor. Epidemiological analysis of a hospital outbreak in Hong Kong revealed that blood group O was associated with a low risk of infection. In this study, we used a cellular model of adhesion to investigate whether natural antibodies of the ABO system could block the S protein and angiotensin-converting enzyme 2 interaction. To this aim, a C-terminally EGFP-tagged S protein was expressed in chinese hamster ovary cells cotransfected with an α1,2-fucosyltransferase and an A-transferase in order to coexpress the S glycoprotein ectodomain and the A antigen at the cell surface. We observed that the S protein/angiotensin-converting enzyme 2-dependent adhesion of these cells to an angiotensin-converting enzyme 2 expressing cell line was specifically inhibited by either a monoclonal or human natural anti-A antibodies, indicating that these antibodies may block the interaction between the virus and its receptor, thereby providing protection. In order to more fully appreciate the potential effect of the ABO polymorphism on the epidemiology of SARS, we built a mathematical model of the virus transmission dynamics that takes into account the protective effect of ABO natural antibodies. The model indicated that the ABO polymorphism could contribute to substantially reduce the virus transmission, affecting both the number of infected individuals and the kinetics of the epidemic.</p></abstract><kwd-group><kwd>ABO</kwd><kwd>cellular receptor</kwd><kwd>histo-blood group antigens</kwd><kwd>natural antibodies</kwd><kwd>SARS</kwd></kwd-group></article-meta></front></pmc><affiliations><list><country><li>France</li><li>Singapour</li></country></list><tree><noCountry><name sortKey="Ruvoen Clouet, Nathalie" sort="Ruvoen Clouet, Nathalie" uniqKey="Ruvoen Clouet N" first="Nathalie" last="Ruvoën-Clouet">Nathalie Ruvoën-Clouet</name></noCountry><country name="France"><noRegion><name sortKey="Guillon, Patrice" sort="Guillon, Patrice" uniqKey="Guillon P" first="Patrice" last="Guillon">Patrice Guillon</name></noRegion><name sortKey="Clement, Monique" sort="Clement, Monique" uniqKey="Clement M" first="Monique" last="Clément">Monique Clément</name><name sortKey="Le Pendu, Jacques" sort="Le Pendu, Jacques" uniqKey="Le Pendu J" first="Jacques" last="Le Pendu">Jacques Le Pendu</name><name sortKey="Rivain, Jean Gerard" sort="Rivain, Jean Gerard" uniqKey="Rivain J" first="Jean-Gérard" last="Rivain">Jean-Gérard Rivain</name><name sortKey="Sebille, Veronique" sort="Sebille, Veronique" uniqKey="Sebille V" first="Véronique" last="Sébille">Véronique Sébille</name></country><country name="Singapour"><noRegion><name sortKey="Chou, Chih Fong" sort="Chou, Chih Fong" uniqKey="Chou C" first="Chih-Fong" last="Chou">Chih-Fong Chou</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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