Molecular and immunological characterization of the glycosylated orange allergen Cit s 1
Identifieur interne : 002348 ( Main/Exploration ); précédent : 002347; suivant : 002349Molecular and immunological characterization of the glycosylated orange allergen Cit s 1
Auteurs : Gerald Pltl [Autriche] ; Oussama Ahrazem [Espagne] ; Katharina Paschinger [Autriche] ; M. Dolores Ibaez [Espagne] ; Gabriel Salcedo [Espagne] ; Iain B. H. Wilson [Autriche]Source :
- Glycobiology [ 0959-6658 ] ; 2007-02.
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 1,2-xylose and core 1,3-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.
Url:
- https://api.istex.fr/document/EDEA3504B402F35FDE423511061506F9B887B45D/fulltext/pdf
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848330
DOI: 10.1093/glycob/cwl068
Affiliations:
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<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>
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<term>Plant Proteins (immunology)</term>
<term>Polysaccharides (chemistry)</term>
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<term>Peptide Fragments</term>
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<term>Immune Sera</term>
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<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Glycosylation</term>
<term>Humans</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
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<front><div type="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 1,2-xylose and core 1,3-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>
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<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>
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<country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Ahrazem, Oussama" sort="Ahrazem, Oussama" uniqKey="Ahrazem O" first="Oussama" last="Ahrazem">Oussama Ahrazem</name>
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