Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV.
Identifieur interne : 002D80 ( PubMed/Corpus ); précédent : 002D79; suivant : 002D81Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV.
Auteurs : Denong Wang ; Jiahai LuSource :
- Physiological genomics [ 1531-2267 ] ; 2004.
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
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pubmed:15161967Le document en format XML
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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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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></record>Pour manipuler ce document sous Unix (Dilib)
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