Detection of four distinct groups of hen egg allergens binding IgE in the sera of children with egg allergy

Walsh, Bradley J.; Hill, David; Macoun, P.; Cairns, Diane; Howden, M.E.H.

doi:10.1157/13077741

Cited by 38 publications

(34 citation statements)

References 19 publications

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“…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.…”

Section: Discussionsupporting

confidence: 86%

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

Everberg¹,

Brostedt²,

Öman³

et al. 2010

Int Arch Allergy Immunol

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Background: Egg is a common cause of food-allergic reactions, especially among young children. Some egg-allergic patients do, however, tolerate heated egg products and component-resolved diagnostics (CRD) may facilitate prediction of different disease manifestations. Commercially available preparations of the egg-white allergens, ovomucoid, ovalbumin, conalbumin and lysozyme, have been reported to contain impurities which interfere with accurate CRD. Methods: Commercial preparations of the 4 egg-white allergens were characterized using allergen-specific monoclonal chimeric human/mouse IgE antibodies in experimental ImmunoCAP® tests. Further purification of commercial ovomucoid, ovalbumin and conalbumin preparations was performed by chromatography based on affinity to monoclonal antibodies. Purity was monitored by size exclusion chromatography, SDS-PAGE, Western blotting and experimental ImmunoCAP tests using allergen-specific chimeric IgE antibodies. IgE reactivity to the highly purified egg components was analyzed in 83 samples from egg white-sensitized individuals. Results: Preparations of commercially available ovomucoid, ovalbumin and conalbumin were found to contain other egg allergens which were removed by chromatographic purification. No impurities were detected in the commercial lysozyme preparation. Previously unknown complexes between the target allergens and contaminating allergens were detected and removed by affinity chromatography. IgE reactivity to ovalbumin was most common in the analyzed samples (87%), followed by ovomucoid (72%), conalbumin (69%) and lysozyme (58%). Conclusions: In this study we demonstrate the advantage of using monoclonal antibodies for purification, and monoclonal chimeric IgE antibodies for characterization, of egg allergens intended for CRD. Our study also established that ovalbumin, ovomucoid, conalbumin and lysozyme are all major allergens.

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Section: Discussionsupporting

confidence: 86%

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

Everberg¹,

Brostedt²,

Öman³

et al. 2010

Int Arch Allergy Immunol

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“…Hen egg, which contains 1-3 g/l of LYS, is probably one of the main sources of LYS used to maintain the quality of food and pharmaceutical products. However, hen eggs are also the second most frequent cause of food allergy in infants, with LYS being one of its main allergens (Gal d 4) responsible for a sensitization frequency of more than 35% in patients with clinically observed egg hypersensitivity [2,3]. …”

Section: Introductionmentioning

confidence: 99%

Anaphylaxis Induced by a Drug Containing Lysozyme and Papain: Influence of Papain on the IgE Response

Benedé

Pérez-Rangel

Lozano‐Ojalvo

et al. 2014

Int Arch Allergy Immunol

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Background: This paper reports the case of an egg-allergic pediatric patient who, once desensitized to egg following a successful rush oral immunotherapy protocol, could also tolerate Lizipaina®, a drug containing lysozyme (LYS) and papain, which had previously caused him a severe allergic reaction. Because the LYS amount that elicited the anaphylactic reaction (5 mg) was much lower than that tolerated during a double-blind placebo-controlled food challenge (corresponding to approximately 60 mg of LYS), the possibility that the presence of papain could increase the allergenic potential of LYS was investigated. Methods: Lizipaina, LYS and LYS hydrolyzed with papain were analyzed by SDS-PAGE under reducing and nonreducing conditions, and Western blotting of sera from egg-allergic patients was performed in order to detect IgE-binding fragments. Finally, sequence identification of the IgE-reactive bands was carried out by MALDI-TOF/TOF. Results: The SDS-PAGE pattern of LYS treated with papain under nonreducing conditions showed the presence of intact LYS that partially disappeared following reduction with β-mercaptoethanol, releasing IgE-reactive fragments as determined by Western blotting. MALDI-TOF/TOF revealed that papain degraded LYS, giving rise to three IgE-binding fragments: LYS (22-129), LYS (34-96) and LYS (62-128) that likely remained linked through the disulfide bonds present in the LYS molecule. Conclusion: The combined administration of LYS with proteolytic enzymes such as papain may have developed a severe allergic reaction in the patient studied, underlining the importance of considering all the components and their interactions when drugs are to be consumed by allergic persons.

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“…It contains both conformational and sequential epitopes [4][5][6][7]. Allergic reactions exclusively to lysozyme were reported by Pérez-Calderón et al [8], Malmheden [9], Frémont et al [10], and Camp et al [11] at lower milligram dosages in a doubleblind placebo-controlled food challenge [10].…”

Section: Introductionmentioning

confidence: 99%

Lysozyme in wine: A risk evaluation for consumers allergic to hen's egg

Weber

Kratzin

Brockow

et al. 2009

Molecular Nutrition Food Res

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Lysozyme used in wine production could present a risk for consumers allergic to hen's egg. Thus, precautionary labeling of lysozyme on wines has been adopted within the European Community by updating Annex IIIa by Directive 2007/68/EC on November 27, 2007. Since no scientific data is known about the actual amounts and risks of lysozyme in wines, various in vitro efforts and skin prick tests were applied in this study to evaluate the presence of lysozyme in wines and the reactivity of those residues in allergic individuals and to fulfill the claim of updating Annex IIIa announced in Directive 2003/89/EC. Depending on the wine's color (red or white wine) and fining with bentonite, which is known as an important step to remove unstable proteins mainly from white wines, diverse results were obtained concerning the amounts of lysozyme in finished wines and their in vitro and in vivo reactivity in humans allergic to hen's egg.

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Detection of four distinct groups of hen egg allergens binding IgE in the sera of children with egg allergy

Cited by 38 publications

References 19 publications

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

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

Anaphylaxis Induced by a Drug Containing Lysozyme and Papain: Influence of Papain on the IgE Response

Lysozyme in wine: A risk evaluation for consumers allergic to hen's egg

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