Lupine Allergy: Not Simply Cross-Reactivity with Peanut or Soy

Authors

Kim A. B. M. Peeters, University Medical Center UtrechtFollow
Julie A. Nordlee, University of Nebraska-LincolnFollow
André H. Penninks, TNO Quality of Life, Zeist, Netherlands
Lingyun Chen, University of Nebraska-Lincoln
Richard E. Goodman, University of Nebraska-LincolnFollow
Carla A. F. M. Bruijnzeel-Koomen, University Medical Center Utrecht
Sue L. Hefle, University of Nebraska-Lincoln
Steve L. Taylor, University of Nebraska-LincolnFollow
André C. Knulst, University Medical Center Utrecht

Document Type

Article

Date of this Version

2007

Citation

Journal of Allergy and Clinical Immunology (2007) 120: 647–653

doi: 10.1016/j.jaci.2007 .05.032

Comments

Copyright © 2007, American Academy of Allergy, Asthma and Immunology. Published by Elsevier. Used by permission

Abstract

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.