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IgE-binding and cross-reactivity of a new 41 kDa allergen of codfish
S Das Dores1, C Chopin, A Romano
1Laboratoire de Pathologie Cellulaire et Moléculaire en Nutrition, EMI-INSERM 0014, URM IFREMER no. 20, Faculté de Médecine de Nancy, Université Henri Poincare, Vandouevre-lès-Nancy, France.
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.