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- Title
Structure of IgE Epitopes on a New 39-kD Allergen Molecule from the House Dust Mite, Dermatophagoides farinae.
- Authors
Aki, Tsunehiro; Ono, Kazuhisa; Hidaka, Yuuji; Shimonishi, Yasutsugu; Jyo, Toshihiko; Wada, Takeshi; Yamashita, Mitsuo; Shigeta, Seiko; Murooka, Yoshikatsu; Oka, Satoru
- Abstract
Two IgE epitope sequences comprising Ser56-Pro-Val-Thr-Lys-Arg-Ala-Ser-Leu-Lys-Ile-Asp-Ser-Lys-Lys70 and Asp104-Val-Glu-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 synthetic dodecapeptide 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. Copyright © 1994 S. Karger AG, Basel
- Publication
International Archives of Allergy & Immunology, 1994, Vol 103, Issue 4, p357
- ISSN
1018-2438
- Publication type
Article
- DOI
10.1159/000236654