Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium‐binding allergen from Bermuda grass pollen

FEBS Letters

Knox, R.Bruce²  Ferreira, Fatima¹  Suphioglu, Cenk² 

[1] Inst. f. Genetik u. Allg. Biologie, Universität Salzburg, A-5020 Salzburg, Austria;Pollen and Allergen Research Group, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia

关键词: Cynodon dactylon;    cDNA cloning;    Calcium-binding protein;    IgE;    Cross-reactivity;    Amino acid sequence;    aa;    amino acid(s);    Ab;    antibody(ies);    Bet v 3;    major allergen(s) of birch pollen;    Bet v 4;    major allergen(s) of birch pollen;    bp;    base pair(s);    BSA;    bovine serum albumin;    cDNA;    DNA complementary to RNA;    Cyn d 1;    major allergen(s) of Bermuda grass pollen;    Cyn d 7;    major allergen(s) of Bermuda grass pollen;    Ig;    immunoglobulin(s);    IUIS;    International Union of Immunological Societies;    Lol p 1;    major allergen of rye-grass pollen;    nt;    nucleotide(s);    ORF;    open reading frame;    PAGE;    polyacrylamide gel electrophoresis;    PBS;    phosphate-buffered saline;    PEG;    poly(ethylene glycol);    rCyn d 7;    recombinant Cyn d 7;    rBet v 4;    recombinant Bet v 4;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/S0014-5793(96)01520-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A cDNA coding for a newly identified Bermuda grass pollen allergen, Cyn d 7, with significant sequence similarity to Ca²⁺-binding proteins, was isolated from a cDNA expression library using serum IgE from an allergic individual. The deduced amino acid sequence of Cyn d 7 contained two typical Ca²⁺-binding sites (EF hand domains). Depletion of Ca²⁺ with EGTA led to a loss of IgE-binding capacity of rCyn d 7. A synthetic peptide based on domain II showed high IgE reactivity. Cyn d 7 therefore represents a grass pollen allergen that belongs to a novel class of Ca²⁺-binding proteins.

【 授权许可】

Unknown