Identification of IgE-Binding Egg White Proteins: Comparison of Results Obtained by Different Methods

Abstract

The binding of IgE to egg white proteins was investigated for 34 sera from adults with a positive case history and/or positive RAST towards egg, and the impact of experimental conditions on IgE binding in commonly used methods was studied. Radioimmunoblotting after SDS-PAGE of both reduced and unreduced egg white extracts showed complex reaction patterns. The results were confirmed by crossed radioimmunoelectrophoresis (CRIE). Radio dot immunobinding was used to investigate the effect of treatment of allergens for SDS-PAGE and to evaluate the other methods. As a conclusion, the use of combinations of at least two methods is recommended for the identification of IgE-binding egg white proteins. Of the 34 sera, 18 reacted with ovotransferrin, 13 with ovomucoid, 11 with ovalbumin and 5 with lysozyme. The amounts of IgE bound to ovalbumin and lysozyme were generally lower than the amounts bound to ovotransferrin and ovomucoid.

Affinity Purification of Egg-White Allergens for Improved Component-Resolved Diagnostics

“…The rather high prevalence of IgE reactivity to all egg-white allergens in this study is consistent with other studies showing also high prevalence of IgE reactivity to ovomucoid [12,23,26], conalbumin [27] and lysozyme [4]. Discrepancies between studies regarding which allergen is actually most important in egg white could be due to methodological differences, patient selection or use of impure allergen reagents.…”

Recognition of Native and/or Thermally Induced Denatured Forms of the Major Food Allergen, Ovomucoid, by Human IgE and Mouse Monoclonal IgG Antibodies

“…8,9) Ovomucoid (OM), a glycoprotein with a molecular weight of 28 kDa, is thought to be the major allergen in egg white, 10) despite the existance of a controversial report. 11) Since its high allergenicity is associated with its thermal stability, relationship between them has been immunologically discussed. [12][13][14][15] Uris et al have clinically indicated the predominance of OM as an allergen in egg white and the importance of the allergenicity of heat-treated OM by a double-blind, placebo-controlled food challenge.…”

Hen egg white lysozyme is less active against Gardnerella vaginalis biofilm than human lysozyme

“…However, while the lysozyme preparations did not exert cytotoxic effects on isolated vaginal epithelial cells, in vivo intravaginal administration of egg white lysozyme can generate inflammatory reactions (Pichler and Campi, 1992) against the egg lysozyme and/or other egg proteins. Egg lysozyme as food additive can also be unsuitable for consumption by persons who are allergic to eggs, accounting for 10 to 20% of egg allergy (Aabin et al, 1996). Inversely, human lysozyme is not expected to trigger allergic reactions.…”