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Four of these are in egg white: ovomucoid (Gal d 1), ovalbumin (Gal d 2), ovotransferrin (Gal d 3) and lysozyme (Gal d 4). Of these, ovomucoid is the dominant allergen, and one that is less likely to be outgrown as children get older. [2] Ingestion of under-cooked egg may trigger more severe clinical reactions than well-cooked egg.
Ovalbumin (abbreviated OVA [1]) is the main protein found in egg white, making up approximately 55% of the total protein. [2] Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor. [ 3 ]
Chicken ovomucoid, also known as Gal d 1, is a known allergen. It is the protein most often causing egg allergy. At least four IgE epitopes have been identified. [4] Three other egg white proteins are also identified as allergenic: ovalbumin (Gal d 2), ovotransferrin (Gal d 3) and lysozyme (Gal d 4). [5]
Ovomucoid is the major allergen from egg white and is a heat-resistant glycoprotein found to be a trypsin inhibitor. Lysozyme is a holoprotein which can lyse the wall of certain Gram-positive bacteria and is found at high levels in the chalaziferous layer and the chalazae which anchor the yolk towards the middle of the egg.
Ovotransferrin makes up approximately 13% of egg albumen (in contrast to ovalbumin, which comprises 54%). [2] As a member of the transferrin and metalloproteinase family, ovotransferrin has been found to possess antibacterial and antioxidant and immunomodulatory properties, arising primarily through its iron (Fe3+) binding capacity by locking ...
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Immunoglobulin E (IgE) is a type of antibody (or immunoglobulin (Ig) "isoform") that has been found only in mammals. IgE is synthesised by plasma cells. Monomers of IgE consist of two heavy chains (ε chain) and two light chains, with the ε chain containing four Ig-like constant domains (Cε1–Cε4). [1]
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