BACKGROUND: Because of the frequent use of natural latex products, IgE-mediated reactions to latex proteins represent an important health threat in industrialized countries. Although several latex allergens have been characterized and IgE cross-reactivities with allergens present in plant-derived food have been described, limited information is available regarding the presence of common IgE-binding components in latex and plant pollen. METHODS: By using serum IgE from 56 individuals with latex allergy, the IgE-binding components in ammoniated latex milk and latex glove extracts were characterized by immunoblotting. The presence of cross-reactive IgE-binding components in the different latex extracts, extracts from mugwort, ragweed, timothy grass pollen, and recombinant birch pollen allergens (Bet v 1 and Bet v 2 [birch profilin]) was studied by immunoblot inhibitions and quantitative competition experiments. The involvement of carbohydrates in the constitution of cross-reactive IgE epitopes was studied by periodate treatment of extracts. RESULTS: Although sera from certain individuals with latex allergy showed IgE reactivity with protein bands of different molecular weights in Western-blotted latex milk and glove extracts, both extracts contained common IgE epitopes. Although preincubation with recombinant Bet v 1 and Bet v 2 did not significantly inhibit IgE binding to latex proteins, weed and, in particular, timothy grass pollen extract strongly inhibited IgE binding to latex allergens. The cross-reactive IgE epitopes were sensitive to periodate treatment. CONCLUSIONS: Mugwort, ragweed, and timothy grass pollen share IgE epitopes with glycoprotein latex allergens. The presence of common epitopes might in part explain clinical symptoms in patients allergic to pollen on contact with latex.
BACKGROUND: Because of the frequent use of natural latex products, IgE-mediated reactions to latex proteins represent an important health threat in industrialized countries. Although several latex allergens have been characterized and IgE cross-reactivities with allergens present in plant-derived food have been described, limited information is available regarding the presence of common IgE-binding components in latex and plant pollen. METHODS: By using serum IgE from 56 individuals with latexallergy, the IgE-binding components in ammoniated latex milk and latex glove extracts were characterized by immunoblotting. The presence of cross-reactive IgE-binding components in the different latex extracts, extracts from mugwort, ragweed, timothy grass pollen, and recombinant birch pollen allergens (Bet v 1 and Bet v 2 [birch profilin]) was studied by immunoblot inhibitions and quantitative competition experiments. The involvement of carbohydrates in the constitution of cross-reactive IgE epitopes was studied by periodate treatment of extracts. RESULTS: Although sera from certain individuals with latexallergy showed IgE reactivity with protein bands of different molecular weights in Western-blotted latex milk and glove extracts, both extracts contained common IgE epitopes. Although preincubation with recombinant Bet v 1 and Bet v 2 did not significantly inhibit IgE binding to latex proteins, weed and, in particular, timothy grass pollen extract strongly inhibited IgE binding to latex allergens. The cross-reactive IgE epitopes were sensitive to periodate treatment. CONCLUSIONS:Mugwort, ragweed, and timothy grass pollen share IgE epitopes with glycoprotein latex allergens. The presence of common epitopes might in part explain clinical symptoms in patientsallergic to pollen on contact with latex.