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.
| Original language | English |
|---|---|
| Pages (from-to) | 357-364 |
| Number of pages | 8 |
| Journal | International Archives of Allergy and Immunology |
| Volume | 103 |
| Issue number | 4 |
| Publication status | Published - 1994 |
| Externally published | Yes |
Keywords
- Dermatophagoides farinae
- Epitope mapping
- IgE epitope
- Mite allergen
ASJC Scopus subject areas
- Immunology
- Immunology and Allergy
Cite this
Structure of IgE epitopes on a new 39-kD allergen molecule from the house dust mite, Dermatophagoides farinae. / Aki, T.; Ono, K.; Hidaka, Y.; Shimonishi, Y.; Jyo, T.; Wada, T.; Yamashita, Mitsuo; Shigeta, S.; Murooka, Y.; Oka, S.
In: International Archives of Allergy and Immunology, Vol. 103, No. 4, 1994, p. 357-364.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure of IgE epitopes on a new 39-kD allergen molecule from the house dust mite, Dermatophagoides farinae
AU - Aki, T.
AU - Ono, K.
AU - Hidaka, Y.
AU - Shimonishi, Y.
AU - Jyo, T.
AU - Wada, T.
AU - Yamashita, Mitsuo
AU - Shigeta, S.
AU - Murooka, Y.
AU - Oka, S.
PY - 1994
Y1 - 1994
N2 - 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.
AB - 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.
KW - Dermatophagoides farinae
KW - Epitope mapping
KW - IgE epitope
KW - Mite allergen
UR - http://www.scopus.com/inward/record.url?scp=0028208462&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028208462&partnerID=8YFLogxK
M3 - Article
VL - 103
SP - 357
EP - 364
JO - International Archives of Allergy and Immunology
JF - International Archives of Allergy and Immunology
SN - 1018-2438
IS - 4
ER -