| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-89 |
Sentence |
denotes |
Molecular and immunological characterization of the glycosylated orange allergen Cit s 1. |
| TextSentencer_T2 |
90-262 |
Sentence |
denotes |
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. |
| TextSentencer_T3 |
263-362 |
Sentence |
denotes |
In the present study, we have analyzed its immunological cross-reactivity and its molecular nature. |
| TextSentencer_T4 |
363-531 |
Sentence |
denotes |
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. |
| TextSentencer_T5 |
532-808 |
Sentence |
denotes |
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. |
| TextSentencer_T6 |
809-924 |
Sentence |
denotes |
In parallel, we examined the peptide sequence and glycan structure of Cit s 1, using mass spectrometric techniques. |
| TextSentencer_T7 |
925-1191 |
Sentence |
denotes |
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. |
| TextSentencer_T8 |
1192-1557 |
Sentence |
denotes |
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. |
| T1 |
0-89 |
Sentence |
denotes |
Molecular and immunological characterization of the glycosylated orange allergen Cit s 1. |
| T2 |
90-262 |
Sentence |
denotes |
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. |
| T3 |
263-362 |
Sentence |
denotes |
In the present study, we have analyzed its immunological cross-reactivity and its molecular nature. |
| T4 |
363-531 |
Sentence |
denotes |
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. |
| T5 |
532-808 |
Sentence |
denotes |
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. |
| T6 |
809-924 |
Sentence |
denotes |
In parallel, we examined the peptide sequence and glycan structure of Cit s 1, using mass spectrometric techniques. |
| T7 |
925-1191 |
Sentence |
denotes |
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. |
| T8 |
1192-1557 |
Sentence |
denotes |
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. |
| T1 |
0-89 |
Sentence |
denotes |
Molecular and immunological characterization of the glycosylated orange allergen Cit s 1. |
| T2 |
90-262 |
Sentence |
denotes |
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. |
| T3 |
263-362 |
Sentence |
denotes |
In the present study, we have analyzed its immunological cross-reactivity and its molecular nature. |
| T4 |
363-531 |
Sentence |
denotes |
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. |
| T5 |
532-808 |
Sentence |
denotes |
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. |
| T6 |
809-924 |
Sentence |
denotes |
In parallel, we examined the peptide sequence and glycan structure of Cit s 1, using mass spectrometric techniques. |
| T7 |
925-1191 |
Sentence |
denotes |
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. |
| T8 |
1192-1557 |
Sentence |
denotes |
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. |
