Abstract
Two IgE epitope sequences comprising Ser56-Pro-Val-Thr-Lys-Arg-Ala-Ser- Leu-Lys-Ile-Asp-Ser-Lys-Lys70 and Asp104-Val-GIu-Leu-Ser-Leu-Arg-Ser-Ser-Asp-Ile-Ala115 were identified by deletion analysis of the cDNA encoding a new 39-kD protein of mite allergen. A syntheticdodecapeptide corresponding to the latter epitope sequence functioned as a monovalent and mite-specific hapten. Replacement of each of the 12 amino acid residues with Gly, using site-directed mutagenesis, indicated that Arg110 may play a central role in IgE binding. However, the 8 allergic sera tested exhibited a wide variation in their amino acid residues required for reactivity to IgE in allergic sera.
Original language | English |
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Pages (from-to) | 357-364 |
Number of pages | 8 |
Journal | International Archives of Allergy and Immunology |
Volume | 103 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1994 |
Externally published | Yes |
Keywords
- Dermatophagoides farina
- Epitope mapping
- IgE epitope
- Mite allergen
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology