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

doi:10.1159/000236654

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

研究成果: Article › 査読

7 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	357-364
ページ数	8
ジャーナル	International Archives of Allergy and Immunology
巻	103
号	4
DOI	https://doi.org/10.1159/000236654
出版ステータス	Published - 1994
外部発表	はい

ASJC Scopus subject areas

免疫アレルギー学
免疫学

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10.1159/000236654

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

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.",

keywords = "Dermatophagoides farina, Epitope mapping, IgE epitope, Mite allergen",

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

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doi = "10.1159/000236654",

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T1 - Structure of ige epitopes on a new 39-KD allergen molecule from the house dust mite, dermatophagoides farina

AU - Aki, Tsunehiro

AU - Ono, Kazuhisa

AU - Hidaka, Yuuji

AU - Shimonishi, Yasutsugu

AU - Jyo, Toshihiko

AU - Wada, Takeshi

AU - Yamashita, Mitsuo

AU - Shigeta, Seiko

AU - Murooka, Yoshikatsu

AU - Oka, Satoru

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-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.

AB - 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.

KW - Dermatophagoides farina

KW - Epitope mapping

KW - IgE epitope

KW - Mite allergen

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

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