Lupine allergy: Not simply cross-reactivity with peanut or soy

• Published in: Journal of allergy and clinical immunology 2007-09, Vol.120 (3), p.647-653
• Main Authors: Peeters, Kim A.B.M., MD, Nordlee, Julie A., MS, Penninks, André H., PhD, Chen, Lingyun, PhD, Goodman, Richard E., PhD, Bruijnzeel-Koomen, Carla A.F.M., MD, PhD, Hefle, Sue L., PhD, Taylor, Steve L., PhD, Knulst, André C., MD, PhD
• Format: Article
• Language: English
• Subjects: Adult; allergens; Allergies; Allergy and Immunology; amino acid sequencing; Arachis - immunology; Arachis hypogaea; Asthma; Biological and medical sciences; Cross Reactions; cross-reactivity; double-blind; eliciting dose; Female; Food; Food allergies; Food Hypersensitivity - etiology; Food Hypersensitivity - immunology; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Glycerol; Glycine max - immunology; Humans; IgE immunoblotting; Immunoblotting; Immunopathology; Laboratories; Legumes; Lupine allergy; Lupinus - immunology; Male; Medical sciences; Middle Aged; Molecular weight; Patients; peanut; placebo-controlled food challenge; Plant Extracts - immunology; Proteins; Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis; skin prick tests; Skin Tests
• ISSN: 0091-6749; 1097-6825
• DOI: 10.1016/j.jaci.2007.05.032

Background Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized. Objectives We sought to identify allergens associated with lupine allergy, evaluate potential cross-reactivity with peanut, and determine eliciting doses (EDs) for lupine allergy by using double-blind, placebo-controlled food challenges. Methods Six patients with a history of allergic reactions to lupine flour were evaluated by using skin prick tests, CAP tests, and double-blind, placebo-controlled food challenges. Three of these patients were also allergic to peanut. Lupine allergens were characterized by means of IgE immunoblotting and peptide sequencing. Results In all 6 patients the ED for lupine flour was 3 mg or less for subjective symptoms and 300 mg or more for objective symptoms. The low ED and moderate-to-severe historical symptoms indicate significant allergenicity of lupine flour. Two patients allergic to lupine but not to peanut displayed IgE binding predominantly to approximately 66-kd proteins and weak binding to 14- and 24-kd proteins, whereas patients with peanut allergy and lupine allergy showed weak binding to lupine proteins of about 14 to 21 or 66 kd. Inhibition of binding was primarily species specific. Conclusion Lupine allergy can occur either separately or together with peanut allergy, as demonstrated by 3 patients who are cosensitized to peanut and lupine. Clinical implications Lupine flour is allergenic and potentially cross-reactive with peanut allergen, thus posing some risk if used as a replacement for soy flour.