Molecular and immunological characterization of the glycosylated orange allergen Cit s 1.
Identifieur interne : 000B55 ( PubMed/Corpus ); précédent : 000B54; suivant : 000B56Molecular and immunological characterization of the glycosylated orange allergen Cit s 1.
Auteurs : Gerald Pöltl ; Oussama Ahrazem ; Katharina Paschinger ; M Dolores Iba Ez ; Gabriel Salcedo ; Iain B H. WilsonSource :
- Glycobiology [ 0959-6658 ] ; 2007.
English descriptors
- KwdEn :
- Allergens (chemistry), Allergens (immunology), Amino Acid Sequence, Citrus sinensis (immunology), Cross Reactions, Enzyme-Linked Immunosorbent Assay, Fucose (analysis), Glycoproteins (chemistry), Glycoproteins (immunology), Glycosylation, Humans, Immune Sera (immunology), Immunoglobulin E (blood), Mass Spectrometry, Molecular Sequence Data, Peptide Fragments (chemistry), Plant Proteins (chemistry), Plant Proteins (immunology), Polysaccharides (chemistry), Polysaccharides (immunology), Sequence Analysis, Protein, Trypsin (chemistry), Xylose (analysis).
- MESH :
- chemical , analysis : Fucose, Xylose.
- chemical , blood : Immunoglobulin E.
- chemical , chemistry : Allergens, Glycoproteins, Peptide Fragments, Plant Proteins, Polysaccharides, Trypsin.
- chemical , immunology : Allergens, Glycoproteins, Immune Sera, Plant Proteins, Polysaccharides.
- immunology : Citrus sinensis.
- Amino Acid Sequence, Cross Reactions, Enzyme-Linked Immunosorbent Assay, Glycosylation, Humans, Mass Spectrometry, Molecular Sequence Data, Sequence Analysis, Protein.
Abstract
The IgE of sera from patients with a history of allergy to oranges (Citrus sinensis) binds a number of proteins in orange extract, including Cit s 1, a germin-like protein. In the present study, we have analyzed its immunological cross-reactivity and its molecular nature. Sera from many of the patients examined recognize a range of glycoproteins and neoglycoconjugates containing beta1,2-xylose and core alpha1,3-fucose on their N-glycans. These reagents also inhibited the interaction of Cit s 1 with patients' sera, thus underlining the critical role of glycosylation in the recognition of this protein by patients' IgE and extending previous data showing that deglycosylated Cit s 1 does not possess IgE epitopes. In parallel, we examined the peptide sequence and glycan structure of Cit s 1, using mass spectrometric techniques. Indeed, we achieved complete sequence coverage of the mature protein compared with the translation of an expressed sequence tag cDNA clone and demonstrated that the single N-glycosylation site of this protein carries oligosaccharides with xylose and fucose residues. Owing to the presumed requirement for multivalency for in vivo allergenicity, our molecular data showing that Cit s 1 is monovalent as regards glycosylation and that the single N-glycan is the target of the IgE response to this protein explain the immunological cross-reactive properties of Cit s 1 as well as its equivocal nature as a clinically relevant allergen.
DOI: 10.1093/glycob/cwl068
PubMed: 17095532
Links to Exploration step
pubmed:17095532Le document en format XML
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Wilson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17095532</idno><idno type="pmid">17095532</idno><idno type="doi">10.1093/glycob/cwl068</idno><idno type="wicri:Area/PubMed/Corpus">000B55</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular and immunological characterization of the glycosylated orange allergen Cit s 1.</title><author><name sortKey="Poltl, Gerald" sort="Poltl, Gerald" uniqKey="Poltl G" first="Gerald" last="Pöltl">Gerald Pöltl</name><affiliation><nlm:affiliation>Department für Chemie, Universität für Bodenkultur, Muthgasse 18, A-1190 Wien, Austria.</nlm:affiliation></affiliation></author><author><name sortKey="Ahrazem, Oussama" sort="Ahrazem, Oussama" uniqKey="Ahrazem O" first="Oussama" last="Ahrazem">Oussama Ahrazem</name></author><author><name sortKey="Paschinger, Katharina" sort="Paschinger, Katharina" uniqKey="Paschinger K" first="Katharina" last="Paschinger">Katharina Paschinger</name></author><author><name sortKey="Iba Ez, M Dolores" sort="Iba Ez, M Dolores" uniqKey="Iba Ez M" first="M Dolores" last="Iba Ez">M Dolores Iba Ez</name></author><author><name sortKey="Salcedo, Gabriel" sort="Salcedo, Gabriel" uniqKey="Salcedo G" first="Gabriel" last="Salcedo">Gabriel Salcedo</name></author><author><name sortKey="Wilson, Iain B H" sort="Wilson, Iain B H" uniqKey="Wilson I" first="Iain B H" last="Wilson">Iain B H. Wilson</name></author></analytic><series><title level="j">Glycobiology</title><idno type="ISSN">0959-6658</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allergens (chemistry)</term><term>Allergens (immunology)</term><term>Amino Acid Sequence</term><term>Citrus sinensis (immunology)</term><term>Cross Reactions</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Fucose (analysis)</term><term>Glycoproteins (chemistry)</term><term>Glycoproteins (immunology)</term><term>Glycosylation</term><term>Humans</term><term>Immune Sera (immunology)</term><term>Immunoglobulin E (blood)</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Peptide Fragments (chemistry)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (immunology)</term><term>Polysaccharides (chemistry)</term><term>Polysaccharides (immunology)</term><term>Sequence Analysis, Protein</term><term>Trypsin (chemistry)</term><term>Xylose (analysis)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Fucose</term><term>Xylose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Immunoglobulin E</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Allergens</term><term>Glycoproteins</term><term>Peptide Fragments</term><term>Plant Proteins</term><term>Polysaccharides</term><term>Trypsin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Allergens</term><term>Glycoproteins</term><term>Immune Sera</term><term>Plant Proteins</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Citrus sinensis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cross Reactions</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Glycosylation</term><term>Humans</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Sequence Analysis, Protein</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The IgE of sera from patients with a history of allergy to oranges (Citrus sinensis) binds a number of proteins in orange extract, including Cit s 1, a germin-like protein. In the present study, we have analyzed its immunological cross-reactivity and its molecular nature. Sera from many of the patients examined recognize a range of glycoproteins and neoglycoconjugates containing beta1,2-xylose and core alpha1,3-fucose on their N-glycans. These reagents also inhibited the interaction of Cit s 1 with patients' sera, thus underlining the critical role of glycosylation in the recognition of this protein by patients' IgE and extending previous data showing that deglycosylated Cit s 1 does not possess IgE epitopes. In parallel, we examined the peptide sequence and glycan structure of Cit s 1, using mass spectrometric techniques. Indeed, we achieved complete sequence coverage of the mature protein compared with the translation of an expressed sequence tag cDNA clone and demonstrated that the single N-glycosylation site of this protein carries oligosaccharides with xylose and fucose residues. Owing to the presumed requirement for multivalency for in vivo allergenicity, our molecular data showing that Cit s 1 is monovalent as regards glycosylation and that the single N-glycan is the target of the IgE response to this protein explain the immunological cross-reactive properties of Cit s 1 as well as its equivocal nature as a clinically relevant allergen.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17095532</PMID><DateCreated><Year>2007</Year><Month>1</Month><Day>11</Day></DateCreated><DateCompleted><Year>2007</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>7</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0959-6658</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>2</Issue><PubDate><Year>2007</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Glycobiology</Title><ISOAbbreviation>Glycobiology</ISOAbbreviation></Journal><ArticleTitle>Molecular and immunological characterization of the glycosylated orange allergen Cit s 1.</ArticleTitle><Pagination><MedlinePgn>220-30</MedlinePgn></Pagination><Abstract><AbstractText>The IgE of sera from patients with a history of allergy to oranges (Citrus sinensis) binds a number of proteins in orange extract, including Cit s 1, a germin-like protein. In the present study, we have analyzed its immunological cross-reactivity and its molecular nature. Sera from many of the patients examined recognize a range of glycoproteins and neoglycoconjugates containing beta1,2-xylose and core alpha1,3-fucose on their N-glycans. These reagents also inhibited the interaction of Cit s 1 with patients' sera, thus underlining the critical role of glycosylation in the recognition of this protein by patients' IgE and extending previous data showing that deglycosylated Cit s 1 does not possess IgE epitopes. In parallel, we examined the peptide sequence and glycan structure of Cit s 1, using mass spectrometric techniques. Indeed, we achieved complete sequence coverage of the mature protein compared with the translation of an expressed sequence tag cDNA clone and demonstrated that the single N-glycosylation site of this protein carries oligosaccharides with xylose and fucose residues. Owing to the presumed requirement for multivalency for in vivo allergenicity, our molecular data showing that Cit s 1 is monovalent as regards glycosylation and that the single N-glycan is the target of the IgE response to this protein explain the immunological cross-reactive properties of Cit s 1 as well as its equivocal nature as a clinically relevant allergen.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pöltl</LastName><ForeName>Gerald</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department für Chemie, Universität für Bodenkultur, Muthgasse 18, A-1190 Wien, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahrazem</LastName><ForeName>Oussama</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Paschinger</LastName><ForeName>Katharina</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Ibañez</LastName><ForeName>M Dolores</ForeName><Initials>MD</Initials></Author><Author ValidYN="Y"><LastName>Salcedo</LastName><ForeName>Gabriel</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Iain B H</ForeName><Initials>IB</Initials></Author></AuthorList><Language>ENG</Language><GrantList CompleteYN="Y"><Grant><GrantID>FWF_P 18447</GrantID><Agency>Austrian Science Fund FWF</Agency><Country>Austria</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>Nov</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Glycobiology</MedlineTA><NlmUniqueID>9104124</NlmUniqueID><ISSNLinking>0959-6658</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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