Molecular characteristics of common allergens

The majority of allergens described are protein in nature with or without carbohydrate moieties (glycosylated), with a molecular weight ranging between 10-100 kDa. Most proteins in foods can be immunogenic and provoke production of specific antibody, mainly IgG, in individuals with or without an atopic tendency. Only a limited range of proteins is commonly associated with the production of IgE in the atopic individual, and is considered allergenic. Protein molecules that initiate immune responses are commonly over 7000 daltons in size (Roitt et al. 1998). No common molecular motif for allergens has been described, but they do have some properties in common. Allergens, particularly those that lead to persistent allergies, are thought to be resistant to digestion (Astwood et al. 1996, Becker 1997), the rationale being that this results in persistence in the body and stimulation of the immune system. There are certain fruit allergens, which may be unstable, even being degraded by enzymes released in the fruit by crushing (Bjorksten et al. 1980). Many allergens have enzymatic ability (Bufe 1998) so function in addition to stability may be related to allergenicity. Commonly a food will contain more than one allergenic protein, such as beta-lactoglobulin, lactoferrin and the caseins of cow's milk, and ovomucoid, ovalbumin and lysozyme of egg, indicating that the context as well as molecular structure must be important.

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