Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV.
Identifieur interne : 002C88 ( PubMed/Checkpoint ); précédent : 002C87; suivant : 002C89Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV.
Auteurs : Denong Wang [États-Unis] ; Jiahai LuSource :
- Physiological genomics [ 1531-2267 ] ; 2004.
Descripteurs français
- KwdFr :
- Anticorps antiviraux (immunologie), Asialoglycoprotéines (immunologie), Asialoglycoprotéines (sang), Autoanticorps (biosynthèse), Humains, Oligosaccharides, Orosomucoïde (analogues et dérivés), Orosomucoïde (immunologie), Polyosides (immunologie), Syndrome respiratoire aigu sévère (), Techniques de sonde moléculaire, Vaccins antiviraux (effets indésirables), Vaccins antiviraux (usage thérapeutique), Vaccins inactivés (effets indésirables), Vaccins inactivés (usage thérapeutique), Virus du SRAS (immunologie), Épitopes (immunologie).
- MESH :
- analogues et dérivés : Orosomucoïde.
- biosynthèse : Autoanticorps.
- effets indésirables : Vaccins antiviraux, Vaccins inactivés.
- immunologie : Anticorps antiviraux, Asialoglycoprotéines, Orosomucoïde, Polyosides, Virus du SRAS, Épitopes.
- sang : Asialoglycoprotéines.
- usage thérapeutique : Vaccins antiviraux, Vaccins inactivés.
- Humains, Oligosaccharides, Syndrome respiratoire aigu sévère, Techniques de sonde moléculaire.
English descriptors
- KwdEn :
- Antibodies, Viral (immunology), Asialoglycoproteins (blood), Asialoglycoproteins (immunology), Autoantibodies (biosynthesis), Epitopes (immunology), Humans, Molecular Probe Techniques, Oligosaccharides, Orosomucoid (analogs & derivatives), Orosomucoid (immunology), Polysaccharides (immunology), SARS Virus (immunology), Severe Acute Respiratory Syndrome (complications), Severe Acute Respiratory Syndrome (prevention & control), Vaccines, Inactivated (adverse effects), Vaccines, Inactivated (therapeutic use), Viral Vaccines (adverse effects), Viral Vaccines (therapeutic use).
- MESH :
- chemical , adverse effects : Vaccines, Inactivated, Viral Vaccines.
- chemical , analogs & derivatives : Orosomucoid.
- chemical , biosynthesis : Autoantibodies.
- chemical , blood : Asialoglycoproteins.
- chemical , immunology : Antibodies, Viral, Asialoglycoproteins, Epitopes, Orosomucoid, Polysaccharides.
- complications : Severe Acute Respiratory Syndrome.
- immunology : SARS Virus.
- prevention & control : Severe Acute Respiratory Syndrome.
- chemical , therapeutic use : Vaccines, Inactivated, Viral Vaccines.
- Humans, Molecular Probe Techniques, Oligosaccharides.
Abstract
Using carbohydrate microarrays, we characterized the carbohydrate binding activity of SARS-CoV neutralizing antibodies elicited by an inactivated SARS-CoV vaccine. In these antibodies, we detected undesired autoantibody reactivity specific for the carbohydrate moieties of an abundant human serum glycoprotein asialo-orosomucoid (ASOR). This observation provides important clues for the selection of specific immunologic probes to examine whether SARS-CoV expresses antigenic structures that mimic the host glycan. We found that lectin PHA-L (Phaseolus vulgaris L.), which is specific for a defined complex carbohydrate of ASOR, stained the SARS-CoV-infected cells specifically and intensively. Taken together, we present immunologic evidence that a carbohydrate structure of SARS-CoV shares antigenic similarity with host glycan complex carbohydrates. The experimental approaches we applied in this study are likely applicable for the identification of immunologic targets of other viral pathogens.
DOI: 10.1152/physiolgenomics.00102.2004
PubMed: 15161967
Affiliations:
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pubmed:15161967Le document en format XML
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scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Viral</term><term>Asialoglycoproteins</term><term>Epitopes</term><term>Orosomucoid</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Orosomucoïde</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Autoanticorps</term></keywords><keywords scheme="MESH" qualifier="complications" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="effets indésirables" xml:lang="fr"><term>Vaccins antiviraux</term><term>Vaccins inactivés</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Asialoglycoprotéines</term><term>Orosomucoïde</term><term>Polyosides</term><term>Virus du SRAS</term><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS 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the carbohydrate binding activity of SARS-CoV neutralizing antibodies elicited by an inactivated SARS-CoV vaccine. In these antibodies, we detected undesired autoantibody reactivity specific for the carbohydrate moieties of an abundant human serum glycoprotein asialo-orosomucoid (ASOR). This observation provides important clues for the selection of specific immunologic probes to examine whether SARS-CoV expresses antigenic structures that mimic the host glycan. We found that lectin PHA-L (Phaseolus vulgaris L.), which is specific for a defined complex carbohydrate of ASOR, stained the SARS-CoV-infected cells specifically and intensively. Taken together, we present immunologic evidence that a carbohydrate structure of SARS-CoV shares antigenic similarity with host glycan complex carbohydrates. The experimental approaches we applied in this study are likely applicable for the identification of immunologic targets of other viral pathogens.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15161967</PMID><DateCompleted><Year>2004</Year><Month>10</Month><Day>18</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1531-2267</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Jul</Month><Day>08</Day></PubDate></JournalIssue><Title>Physiological genomics</Title><ISOAbbreviation>Physiol. Genomics</ISOAbbreviation></Journal><ArticleTitle>Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV.</ArticleTitle><Pagination><MedlinePgn>245-8</MedlinePgn></Pagination><Abstract><AbstractText>Using carbohydrate microarrays, we characterized the carbohydrate binding activity of SARS-CoV neutralizing antibodies elicited by an inactivated SARS-CoV vaccine. In these antibodies, we detected undesired autoantibody reactivity specific for the carbohydrate moieties of an abundant human serum glycoprotein asialo-orosomucoid (ASOR). This observation provides important clues for the selection of specific immunologic probes to examine whether SARS-CoV expresses antigenic structures that mimic the host glycan. We found that lectin PHA-L (Phaseolus vulgaris L.), which is specific for a defined complex carbohydrate of ASOR, stained the SARS-CoV-infected cells specifically and intensively. Taken together, we present immunologic evidence that a carbohydrate structure of SARS-CoV shares antigenic similarity with host glycan complex carbohydrates. The experimental approaches we applied in this study are likely applicable for the identification of immunologic targets of other viral pathogens.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Denong</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Columbia Genome Center, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Jiahai</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2004</Year><Month>07</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Physiol 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UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015164">Vaccines, Inactivated</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014765">Viral Vaccines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C017030">asialoorosomucoid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001212" MajorTopicYN="N">Asialoglycoproteins</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001323" 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MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000150" MajorTopicYN="N">complications</QualifierName><QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015164" MajorTopicYN="N">Vaccines, Inactivated</DescriptorName><QualifierName UI="Q000009" MajorTopicYN="Y">adverse effects</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014765" MajorTopicYN="N">Viral Vaccines</DescriptorName><QualifierName UI="Q000009" MajorTopicYN="Y">adverse effects</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>5</Month><Day>27</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>10</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>5</Month><Day>27</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15161967</ArticleId><ArticleId IdType="doi">10.1152/physiolgenomics.00102.2004</ArticleId><ArticleId IdType="pii">00102.2004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region><settlement><li>New York</li></settlement><orgName><li>Université Columbia</li></orgName></list><tree><noCountry><name sortKey="Lu, Jiahai" sort="Lu, Jiahai" uniqKey="Lu J" first="Jiahai" last="Lu">Jiahai Lu</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Wang, Denong" sort="Wang, Denong" uniqKey="Wang D" first="Denong" last="Wang">Denong Wang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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