Proteomic analysis of lupin seed proteins to identify conglutin Beta as an allergen, Lup an 1.
Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.
Goggin
Danica E
DE
School of Plant Biology, University of Western Australia, 35 Stirling Highway, Crawley, Western Australia 6009, Australia.
Mir
Gisela
G
Smith
William B
WB
Stuckey
Martin
M
Smith
Penelope M C
PM
D000485:Allergens / Q000032:analysis*; D000595:Amino Acid Sequence; D015153:Blotting, Western; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology; D007073:Immunoglobulin E / Q000097:blood; D031297:Lupinus / Q000737:chemistry*; D010940:Plant Proteins / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D055314:Seed Storage Proteins; D012639:Seeds / Q000737:chemistry*; D012882:Skin Tests
D000485:Allergens; D010940:Plant Proteins; D055314:Seed Storage Proteins; C042457:conglutin protein, Lupinus angustifolius; D007073:Immunoglobulin E