Inhibition of the interaction between the SARS-CoV spike protein and its cellular receptor by anti-histo-blood group antibodies.
Identifieur interne : 001B08 ( PubMed/Checkpoint ); précédent : 001B07; suivant : 001B09Inhibition 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 ; Véronique Sébille ; Jean-Gérard Rivain ; Chih-Fong Chou ; Nathalie Ruvoën-Clouet ; Jacques Le PenduSource :
- Glycobiology [ 1460-2423 ] ; 2008.
Descripteurs français
- KwdFr :
- Adhérence cellulaire (immunologie), Animaux, Antigènes viraux (immunologie), Autoanticorps (immunologie), Cellules CHO, Cellules Vero, Cricetinae, Cricetulus, Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (antagonistes et inhibiteurs), Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Humains, Protéines de l'enveloppe virale (antagonistes et inhibiteurs), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Système ABO de groupes sanguins (immunologie).
- MESH :
- antagonistes et inhibiteurs : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- immunologie : Adhérence cellulaire, Antigènes viraux, Autoanticorps, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Système ABO de groupes sanguins.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- Animaux, Cellules CHO, Cellules Vero, Cricetinae, Cricetulus, Cytométrie en flux, Glycoprotéine de spicule des coronavirus, Humains.
English descriptors
- KwdEn :
- ABO Blood-Group System (immunology), Animals, Antigens, Viral (immunology), Autoantibodies (immunology), CHO Cells, Cell Adhesion (immunology), Chlorocebus aethiops, Cricetinae, Cricetulus, Flow Cytometry, Humans, Membrane Glycoproteins (antagonists & inhibitors), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (antagonists & inhibitors), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : ABO Blood-Group System, Antigens, Viral, Autoantibodies, Membrane Glycoproteins, Viral Envelope Proteins.
- immunology : Cell Adhesion.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- Animals, CHO Cells, Chlorocebus aethiops, Cricetinae, Cricetulus, Flow Cytometry, Humans, Spike Glycoprotein, Coronavirus, Vero Cells.
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 alpha1,2-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.
DOI: 10.1093/glycob/cwn093
PubMed: 18818423
Affiliations:
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flux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 alpha1,2-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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18818423</PMID><DateCompleted><Year>2009</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2423</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>12</Issue><PubDate><Year>2008</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Glycobiology</Title><ISOAbbreviation>Glycobiology</ISOAbbreviation></Journal><ArticleTitle>Inhibition of the interaction between the SARS-CoV spike protein and its cellular receptor by anti-histo-blood group antibodies.</ArticleTitle><Pagination><MedlinePgn>1085-93</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/glycob/cwn093</ELocationID><Abstract><AbstractText>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 alpha1,2-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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guillon</LastName><ForeName>Patrice</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>French National Institute for Health and Medical Research (INSERM), U892, University of Nantes, 44035 Nantes, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Clément</LastName><ForeName>Monique</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Sébille</LastName><ForeName>Véronique</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Rivain</LastName><ForeName>Jean-Gérard</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Chou</LastName><ForeName>Chih-Fong</ForeName><Initials>CF</Initials></Author><Author ValidYN="Y"><LastName>Ruvoën-Clouet</LastName><ForeName>Nathalie</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Le Pendu</LastName><ForeName>Jacques</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>09</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Glycobiology</MedlineTA><NlmUniqueID>9104124</NlmUniqueID><ISSNLinking>0959-6658</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000017">ABO Blood-Group System</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000956">Antigens, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001323">Autoantibodies</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000017" MajorTopicYN="N">ABO Blood-Group System</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000956" MajorTopicYN="N">Antigens, Viral</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001323" MajorTopicYN="N">Autoantibodies</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016466" MajorTopicYN="N">CHO Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002448" MajorTopicYN="N">Cell Adhesion</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006224" MajorTopicYN="N">Cricetinae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003412" MajorTopicYN="N">Cricetulus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005434" MajorTopicYN="N">Flow Cytometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>9</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>2</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>9</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18818423</ArticleId><ArticleId IdType="pii">cwn093</ArticleId><ArticleId IdType="doi">10.1093/glycob/cwn093</ArticleId><ArticleId 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IdType="pubmed">17243893</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Pays de la Loire</li></region><settlement><li>Nantes</li></settlement></list><tree><noCountry><name sortKey="Chou, Chih Fong" sort="Chou, Chih Fong" uniqKey="Chou C" first="Chih-Fong" last="Chou">Chih-Fong Chou</name><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="Ruvoen Clouet, Nathalie" sort="Ruvoen Clouet, Nathalie" uniqKey="Ruvoen Clouet N" first="Nathalie" last="Ruvoën-Clouet">Nathalie Ruvoën-Clouet</name><name sortKey="Sebille, Veronique" sort="Sebille, Veronique" uniqKey="Sebille V" first="Véronique" last="Sébille">Véronique Sébille</name></noCountry><country name="France"><region name="Pays de la Loire"><name sortKey="Guillon, Patrice" sort="Guillon, Patrice" uniqKey="Guillon P" first="Patrice" last="Guillon">Patrice Guillon</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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