Structure of ige epitopes on a new 39-KD allergen molecule from the house dust mite, dermatophagoides farina

Tsunehiro Aki, Kazuhisa Ono, Yuuji Hidaka, Yasutsugu Shimonishi, Toshihiko Jyo, Takeshi Wada, Mitsuo Yamashita, Seiko Shigeta, Yoshikatsu Murooka, Satoru Oka

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16 Citations (Scopus)


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 languageEnglish
Pages (from-to)357-364
Number of pages8
JournalInternational Archives of Allergy and Immunology
Issue number4
Publication statusPublished - 1994 Jan 1



  • Dermatophagoides farina
  • Epitope mapping
  • IgE epitope
  • Mite allergen

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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