抄録
The Brassica pollen allergen Bra r 1 belongs to a new family of Ca2+-binding proteins, characterized by the presence of two potential EF-hand calcium-binding domains. Disruption of these EF-hand motifs by amino acid substitutions demonstrated that both domains of Bra r 1 constitute functional Ca2+-binding sites. Calcium-binding deficient mutants displayed significantly reduced IgE-binding activity. Injection of these mutated Bra r 1 variants into a murine model system showed that mouse IgG raised against the mutants recognized native Bra r 1 in Brassica pollen extracts suggesting the potential use of the engineered allergens for effective immunotherapy. Copyright (C) 1998 Federation of European Biochemical Societies.
本文言語 | English |
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ページ(範囲) | 255-260 |
ページ数 | 6 |
ジャーナル | FEBS Letters |
巻 | 434 |
号 | 3 |
DOI | |
出版ステータス | Published - 1998 9 4 |
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology