IgE-antibodies of fish allergic patients cross-react with frog parvalbumin

C. Hilger*, L. Thill, F. Grigioni, C. Lehners, P. Falagiani, A. Ferrara, C. Romano, W. Stevens, F. Hentges

*Corresponding author for this work

    Research output: Contribution to journalArticleResearchpeer-review

    79 Citations (Scopus)

    Abstract

    Background: The major allergens in fish are parvalbumins. Important immunoglobulin (Ig)E cross-recognition of parvalbumins from different fish species has been shown. Recently frog parvalbumin α has been found to be responsible for a case of IgE-mediated anaphylaxis triggered by the ingestion of frog meat. The aim of this study was to investigate whether IgE antibodies of fish allergic persons cross-react with frog parvalbumin and to appreciate its clinical relevance. Methods: The sera of 15 fish allergic patients and one fish and frog allergic patient were tested by IgE-immunoblotting against frog muscle extract. Sera were tested against recombinant parvalbumin α and β from Rana esculenta. Skin prick tests were performed in selected patients with recombinant frog parvalbumin. Ca2+ depletion experiments and inhibition studies with purified cod and frog recombinant parvalbumin were done to characterize the cross-reactive pattern. Results: Fourteen of the sera tested had IgE antibodies recognizing low molecular weight components in frog muscle extract. Calcium depletion experiments or inhibition of patient sera with purified cod parvalbumin led to a significant or complete decrease in IgE binding. When tested against recombinant parvalbumins, three of 13 sera reacted with α parvalbumin and 11 of 12 reacted with β parvalbumin from R. esculenta. Skin prick tests performed with recombinant frog parvalbumin were positive in fish allergic patients. Inhibition studies showed that a fish and frog allergic patient was primarily sensitized to fish parvalbumin. Conclusion: Cod parvalbumin, a major cross-reactive allergen among different fish species, shares IgE binding epitopes with frog parvalbumin. This in vitro cross-reactivity seems to be also clinically relevant. Parvalbumins probably represent a new family of cross-reactive allergens.

    Original languageEnglish
    Pages (from-to)653-660
    Number of pages8
    JournalAllergy: European Journal of Allergy and Clinical Immunology
    Volume59
    Issue number6
    DOIs
    Publication statusPublished - Jun 2004

    Keywords

    • Allergen
    • Fish
    • Food allergy
    • Frog
    • Parvalbumin
    • Rana esculenta

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