Abstract：
BACKGROUND:Allergen epitope characterization provides valuable information useful for the understanding of proteins as food allergens. It is believed that IgE epitopes in general are conformational, nevertheless, for food allergens known to sensitize through the gastrointestinal tract linear epitopes have been suggested to be of great importance. OBJECTIVE:The aim of this study was to identify IgE specific epitopes of intact and digested Ara h 1, and to compare epitope patterns between humans and rats. METHODS:Sera from five peanut allergic patients and five Brown Norway rats were used to identify intact and digested Ara h 1-specific IgE epitopes by competitive immunoscreening of a phage-displayed random hepta-mer peptide library using polyclonal IgE from the individual sera. The resulting peptide sequences were mapped on the surface of a three-dimensional structure of the Ara h 1 molecule to mimic epitopes using a computer-based algorithm. RESULTS:Patients as well as rats were shown to have individual IgE epitope patterns. All epitope mimics were conformational and found to cluster into three different areas of the Ara h 1 molecule. Five epitope motifs were identified by patient IgE, which by far accounted for most of the eluted peptide sequences. Epitope patterns were rather similar for both intact and digested Ara h 1 as well as for humans and rats. CONCLUSIONS:Individual patient specific epitope patterns have been identified for the major allergen Ara h 1. IgE binding epitopes have been suggested as biomarkers for persistency and severity of food allergy, wherefore recognition of particular epitope patterns or motifs could be a valuable tool for prevention, diagnosis, and treatment of food allergy.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Bøgh KL,Nielsen H,Madsen CB,Mills EN,Rigby N,Eiwegger T,Szépfalusi Z,Roggen ELdoi
10.1016/j.molimm.2012.04.002subject
Has Abstractpub_date
2012-07-01 00:00:00pages
337-46issue
3-4eissn
0161-5890issn
1872-9142pii
S0161-5890(12)00233-7journal_volume
51pub_type
杂志文章abstract：:The site of the murine IgG1 molecule that regulates catabolism has recently been shown to encompass amino acids that are located at the CH2-CH3 domain interface. The CH2 and CH3 domains are connected to each other by a relatively flexible "mini-hinge" region, and flexibility in this region could clearly affect the ori...
journal_title：Molecular immunology
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journal_title：Molecular immunology
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更新日期：1986-12-01 00:00:00
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pub_type： 杂志文章,评审
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pub_type： 杂志文章
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更新日期：1997-10-01 00:00:00
