Jimenez-Lopez, Jose CFoley, Rhonda CBrear, EllaClarke, Victoria CLima-Cabello, ElenaFlorido, Jose FSingh, Karam BAlché, Juan DSmith, Penelope M C2023-01-252023-01-252017-10-06http://hdl.handle.net/10668/11783β-conglutin has been identified as a major allergen for Lupinus angustifolius seeds. The aim of this study was to evaluate the binding of IgE to five recombinant β-conglutin isoforms (rβ) that we overexpressed and purified and to their natural counterparts in different lupin species and cultivars. Western blotting suggested β-conglutins were the main proteins responsible for the IgE reactivity of the lupin species and cultivars. Newly identified polypeptides from "sweet lupin" may constitute a potential new source of primary or cross-reactive sensitization to lupin, particularly to L. albus and L. angustifolius seed proteins. Several of them exhibited qualitative and quantitative differences in IgE-binding among these species and cultivars, mainly in sera from atopic patients that react to lupin rather than peanut. IgE-binding was more consistent to recombinant β2 than to any of the other isoforms, making this protein a potential candidate for diagnosis and immunotherapy.enConglutinsCross-allergenicityDiagnosisFood allergyIgE-binding activityImmunotherapyRecombinant allergenSeed storage proteinsSweet lupinVicilinAllergensArachisBlotting, WesternCross ReactionsFood HypersensitivityHumansImmunoglobulin ELupinusPlant ProteinsSeed Storage ProteinsSeedsresearch article29120805open access10.1016/j.foodchem.2017.10.0151873-7072https://openresearch-repository.anu.edu.au/bitstream/1885/139363/1/1-s2.0-S0308814617316448-main.pdf