Structural analyses of IgE-binding proteins originated from plant foodstuffs

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Patients allergic to plant foodstuffs are known to increase yearly. We have investigated the allergenic proteins in plant foodstuffs using patient's sera and revealed that patient's IgE are cross-reactive among many homlogous proteins which are widely distributed in paint kingdom. Some of the IgE-binding proteins derived from different foodstuffs are glycoproteins and react with antibody raised against horse radish peroxidase (anti HRP). This antiHRP is known to recognize a asparagine-conjugated and high mannose type sugar moiety on peroxidase. The binding activity of patient's IgE against plant's allergens was reduced remarkedly by the pre-treatment of allergenic proteins with antiHRP, suggesting that the epitopes of these allergens are homologous and to be high mannose type sugar moieties. If these sugar moieties are common epitopes of plant allergens, patient's IgE antibodies could react with many homologous proteins which have similar sugar moiety in plant foodstuffs and patients present allergic symptons against many plants beyond there classification, such as species, genus, and families. We investigate one of the plant allergen which has asparagine-conjugated high mannose type sugar moiety, Gly m Bd 28K and potato's allergen, patatin. Both the allergenic proteins found to have a common epitope against patient's IgE antibodies. Furthermore, we revealed that many other plant proteins might share the common epitopes against patient's sera.