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IgE‐binding and cross‐reactivity of a new 41 kDa allergen of codfish
Author(s) -
Das Dores S.,
Chopin C.,
Romano A.,
GallandIrmouli A.V.,
Quaratino D.,
Pascual C.,
Fleurence J.,
Guéant J.L.
Publication year - 2002
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1034/j.1398-9995.57.s72.6.x
Subject(s) - rigor mortis , immunoglobulin e , allergen , chemistry , western blot , sepharose , enzyme , biochemistry , microbiology and biotechnology , biology , allergy , immunology , antibody , gene
Background: A 41‐kDa IgE‐reactive protein (p41) was purified from raw cod extract. This protein is homologous to an aldehyde phosphate dehydrogenase (APDH). The present study aims to evaluate the IgE‐binding and the cross‐reactivity of this protein in 13 patients allergic to codfish. Methods: IgE binding of sera from 13 patients allergic to codfish was tested by Sepharose RIA and by Western blot. Results: Among the 13 patients, only 4 had specific IgE to APDH detected by APDH‐Sepharose RIA. The two patients who had the highest level of specific IgE to human APDH also had a class 5–6 CAP‐RAST IgE level to codfish, but two other patients with a class 5 had a negative APDH‐Sepharose IgE‐RIA. Relative content of APDH was higher in extracts of commercial nonfrozen fish, compared to pre rigor mortis , post rigor mortis and frozen commercial codfish. A high homology of codfish APDH was found with the corresponding human enzyme. A significant inhibition of APDH‐Sepharose by human and, to a lesser extent, by rabbit APDH was observed. Western blot of APDH codfish extract showed two bands at 41 and 36 kDa, respectively. Conclusions: We have characterized a new allergen from codfish, which had a high level of homology in different species. The p41 relative content of extracts from nonfrozen codfish was higher than in the other samples assessed.