Allergenic cross-reactivity of egg-white and egg-yolk proteins: an in vitro study

B. J. Walsh, C. Elliott, R. S. Baker, D. Barnett, R. W. Burley, D. J. Hill, M. E. H. Howden

    Research output: Contribution to journalArticlepeer-review

    26 Citations (Scopus)

    Abstract

    The radioallergosorbent test (RAST) and RAST inhibition test were used to examine cross-allergenicity amongst the major hen’s egg-white and egg-yolk proteins. Using ovalbumin as a reference allergen to compare cross-reactivity, it was apparent that the proteins conalbumin, ovomucoid and lysozyme substantially inhibited binding to ovalbumin discs of IgE in the sera of patients clinically hypersensitive to egg. The converse situation with conalbumin, ovomucoid and lysozyme on the discs and ovalbumin as the inhibitor also resulted in significantly decreased levels of IgE binding to the proteins on the discs. It was also demonstrated that cross-reactions occurred between ovalbumin and the yolk protein, apovitellenin I. Cross-reaction was also observed surprisingly when egg lysozyme was on the disc and the milk protein allergen alpha-lactalbumin was used as the inhibitor. The demonstration of cross-reaction between all of these proteins may signify that there are a number of common allergenic determinants on these egg proteins, thus providing a molecular basis for the phenomenon of cross-reactivity.

    Original languageEnglish
    Pages (from-to)228-232
    Number of pages5
    JournalInternational Archives of Allergy and Immunology
    Volume84
    Issue number3
    DOIs
    Publication statusPublished - 1987

    Fingerprint

    Dive into the research topics of 'Allergenic cross-reactivity of egg-white and egg-yolk proteins: an in vitro study'. Together they form a unique fingerprint.

    Cite this