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Characterization of lupin major allergens ( Lupinus albus L.)
Author(s) -
Guillamón Eva,
Rodríguez Julia,
Burbano Carmen,
Muzquiz Mercedes,
Pedrosa Mercedes M.,
Cabanillas Beatriz,
Crespo Jesús F.,
Sancho Ana I.,
Mills E. N. Clare,
Cuadrado Carmen
Publication year - 2010
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200900452
Subject(s) - lupinus , vicilin , allergen , food allergy , cross reactivity , immunoglobulin e , biology , storage protein , hypoallergenic , allergy , lysine , food science , legumin , biochemistry , chemistry , amino acid , botany , immunology , cross reactions , antibody , gene
White lupin is considered to be a rich source of protein with a notable content of lysine and is being increasingly used in bakery, confectionery, snacks and pastry products due to its multifunctional properties, in addition to its potential hypocholesterolemic and hypoglycemic properties. However, lupin seed flour has been reported as a causative agent of allergic reactions, especially in patients with allergy to peanut since the risk of immunological cross‐reactivity between lupin and peanut is higher than with other legumes. Previously, we had identified two proteins as major lupin allergens (34.5 and 20 kDa) as determined by IgE immunoblotting using sera of 23 patients with lupin‐specific IgE. The aim of this study was to purify and characterize the two major lupin allergens. The results using in vitro IgE‐binding studies and MS analysis have shown that the 34.5 kDa allergen (Lup‐1) is a conglutin β (vicilin‐like protein) while the 20 kDa allergen (Lup‐2) corresponds to the conglutin α fraction (legumin‐like protein). The high level of amino acid sequence homology of Lup‐1 and Lup‐2 with the major allergens of some legumes explains the IgE cross‐reactivity and clinical cross‐reactivity of lupin and other legumes.