BACKGROUND: Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins. OBJECTIVE: To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut. METHODS: We investigated IgE cross-reactivity between lupine alpha-, beta-, gamma-, and delta-conglutins and the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 using enzyme-linked immunosorbent assay with sera from patients with coexisting peanut and lupine allergy. RESULTS: Peanut proteins inhibited IgE binding towards alpha- conglutins, delta-conglutins, and, to a lesser degree, beta-conglutins, while no IgE cross-reaction with delta-conglutin was observed. Ara h 2 most potently inhibited IgE binding to lupine and delta-conglutins, while Ara h 1 most potently cross-reacted with beta-conglutin. Ara h 3 was apparently not involved in these mechanisms. CONCLUSIONS: The present study reveals IgE cross-reactivity between the 2S albumins Ara h 2 and delta-conglutin, and the 7S vicilin-like Ara h 1 and beta-conglutin, which are possibly based on homologies between phylogenetically related proteins. Ara h 2 was the most potent inhibitor of IgE binding to lupine conglutins.
BACKGROUND: Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergicpatients is believed to occur as a result of cross-reactivity between lupine and peanut proteins. OBJECTIVE: To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut. METHODS: We investigated IgE cross-reactivity between lupine alpha-, beta-, gamma-, and delta-conglutins and the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 using enzyme-linked immunosorbent assay with sera from patients with coexisting peanut and lupine allergy. RESULTS:Peanut proteins inhibited IgE binding towards alpha- conglutins, delta-conglutins, and, to a lesser degree, beta-conglutins, while no IgE cross-reaction with delta-conglutin was observed. Ara h 2 most potently inhibited IgE binding to lupine and delta-conglutins, while Ara h 1 most potently cross-reacted with beta-conglutin. Ara h 3 was apparently not involved in these mechanisms. CONCLUSIONS: The present study reveals IgE cross-reactivity between the 2S albumins Ara h 2 and delta-conglutin, and the 7S vicilin-like Ara h 1 and beta-conglutin, which are possibly based on homologies between phylogenetically related proteins. Ara h 2 was the most potent inhibitor of IgE binding to lupine conglutins.
Authors: Maksymilian Chruszcz; Soheila J Maleki; Karolina A Majorek; Matthew Demas; Merima Bublin; Robert Solberg; Barry K Hurlburt; Sanbao Ruan; Christopher P Mattison; Christopher P Mattisohn; Heimo Breiteneder; Wladek Minor Journal: J Biol Chem Date: 2011-09-14 Impact factor: 5.157
Authors: Rhonda C Foley; Ling-Ling Gao; Andrew Spriggs; Lena Y C Soo; Danica E Goggin; Penelope M C Smith; Craig A Atkins; Karam B Singh Journal: BMC Plant Biol Date: 2011-04-04 Impact factor: 4.215