Quantitative IgE inhibition experiments with purified recombinant allergens indicate pollen-derived allergens as the sensitizing agents responsible for.

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Presentation transcript:

Quantitative IgE inhibition experiments with purified recombinant allergens indicate pollen-derived allergens as the sensitizing agents responsible for many forms of plant food allergy Lili Kazemi-Shirazi, MDa,b, Gabrielle Pauli, MDd, Ashok Purohit, MDd, Susanne Spitzauer, MDc, Renate Fröschlc, Karin Hoffmann- Sommergruber, PhDa, Heimo Breiteneder, PhDa, Otto Scheiner, PhDa, Dietrich Kraft, MDa, Rudolf Valenta, MDa Journal of Allergy and Clinical Immunology Volume 105, Issue 1, Pages 116-125 (January 2000) DOI: 10.1016/S0091-6749(00)90186-6 Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 1 Inhibition of serum IgE reactivity to nitrocellulose-blotted plant food extracts by preadsorption of sera with recombinant or natural pollen allergens. Nitrocellulose-blotted extracts from apple (A) , carrot (B) , celery (C) , hazelnut (D) , kiwi (E) , and peach (F) were probed with sera from 21 patients with OAS (panels 1-21) and with serum from a nonallergic individual (panel N) . Sera were preadsorbed with an unrelated control protein (lanes A, BSA), with a combination of rBet v 1 and rBet v 2 (lanes B) , or with natural timothy grass pollen allergens (lanes C) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 10 to 11 and 19 to N (hazelnut) and 9 to 11 and 18 to N (peach), molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 1 Inhibition of serum IgE reactivity to nitrocellulose-blotted plant food extracts by preadsorption of sera with recombinant or natural pollen allergens. Nitrocellulose-blotted extracts from apple (A) , carrot (B) , celery (C) , hazelnut (D) , kiwi (E) , and peach (F) were probed with sera from 21 patients with OAS (panels 1-21) and with serum from a nonallergic individual (panel N) . Sera were preadsorbed with an unrelated control protein (lanes A, BSA), with a combination of rBet v 1 and rBet v 2 (lanes B) , or with natural timothy grass pollen allergens (lanes C) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 10 to 11 and 19 to N (hazelnut) and 9 to 11 and 18 to N (peach), molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 1 Inhibition of serum IgE reactivity to nitrocellulose-blotted plant food extracts by preadsorption of sera with recombinant or natural pollen allergens. Nitrocellulose-blotted extracts from apple (A) , carrot (B) , celery (C) , hazelnut (D) , kiwi (E) , and peach (F) were probed with sera from 21 patients with OAS (panels 1-21) and with serum from a nonallergic individual (panel N) . Sera were preadsorbed with an unrelated control protein (lanes A, BSA), with a combination of rBet v 1 and rBet v 2 (lanes B) , or with natural timothy grass pollen allergens (lanes C) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 10 to 11 and 19 to N (hazelnut) and 9 to 11 and 18 to N (peach), molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 1 Inhibition of serum IgE reactivity to nitrocellulose-blotted plant food extracts by preadsorption of sera with recombinant or natural pollen allergens. Nitrocellulose-blotted extracts from apple (A) , carrot (B) , celery (C) , hazelnut (D) , kiwi (E) , and peach (F) were probed with sera from 21 patients with OAS (panels 1-21) and with serum from a nonallergic individual (panel N) . Sera were preadsorbed with an unrelated control protein (lanes A, BSA), with a combination of rBet v 1 and rBet v 2 (lanes B) , or with natural timothy grass pollen allergens (lanes C) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 10 to 11 and 19 to N (hazelnut) and 9 to 11 and 18 to N (peach), molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 1 Inhibition of serum IgE reactivity to nitrocellulose-blotted plant food extracts by preadsorption of sera with recombinant or natural pollen allergens. Nitrocellulose-blotted extracts from apple (A) , carrot (B) , celery (C) , hazelnut (D) , kiwi (E) , and peach (F) were probed with sera from 21 patients with OAS (panels 1-21) and with serum from a nonallergic individual (panel N) . Sera were preadsorbed with an unrelated control protein (lanes A, BSA), with a combination of rBet v 1 and rBet v 2 (lanes B) , or with natural timothy grass pollen allergens (lanes C) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 10 to 11 and 19 to N (hazelnut) and 9 to 11 and 18 to N (peach), molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 1 Inhibition of serum IgE reactivity to nitrocellulose-blotted plant food extracts by preadsorption of sera with recombinant or natural pollen allergens. Nitrocellulose-blotted extracts from apple (A) , carrot (B) , celery (C) , hazelnut (D) , kiwi (E) , and peach (F) were probed with sera from 21 patients with OAS (panels 1-21) and with serum from a nonallergic individual (panel N) . Sera were preadsorbed with an unrelated control protein (lanes A, BSA), with a combination of rBet v 1 and rBet v 2 (lanes B) , or with natural timothy grass pollen allergens (lanes C) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 10 to 11 and 19 to N (hazelnut) and 9 to 11 and 18 to N (peach), molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions

Fig. 2 Inhibition of serum IgE reactivity to nitrocellulose-blotted natural birch pollen extract by preadsorption of sera with recombinant Bet v 1 and recombinant plant food allergens. Nitrocellulose-blotted birch pollen extract was probed with sera from 5 patients with OAS (panels 1-5) and with serum from a nonallergic individual (panel 6) . Serum samples were preadsorbed with rBet v 1 (lanes A) , BSA as a control protein (lanes B) , rApi g 1 (lanes C) , rMal d 1 (lanes D), or rDau c 1 (lanes E) . Bound IgE antibodies were detected with iodine 125–labeled anti-human IgE antibodies and visualized by autoradiography. Molecular weights are displayed in kilodaltons on the left margins. For panels 4 to 6 , molecular weights are displayed on the right side. Journal of Allergy and Clinical Immunology 2000 105, 116-125DOI: (10.1016/S0091-6749(00)90186-6) Copyright © 2000 Mosby, Inc. Terms and Conditions