Primary respiratory and food allergy to mealworm

Sensitization profiles (specific IgE [sIgE], immunoblot, and the basophil activation test [BAT]), allergens involved (liquid chromatography-mass spectrometry) and the development of clinical allergy to shrimp (open food challenge) and mealworm (double-blind, placebo-controlled food challenger [DBPCFC]) were investigated (for details, see the Methods section in this article's Online Repository at www.jacionline.org). All subjects had a negative oral food challenge result for shrimp, and only subject 3 and 4 had positive DBPCFC results for mealworm. Because 3 of our subjects had higher sIgE levels to mealworm than to any other food or inhalant allergen, mealworm might be the primary sensitizer. Furthermore, immunoblots from patients with shrimp allergy1 showed different binding patterns compared with those from the 4 primary patients with mealworm allergy, and their basophil activation to mealworm was stronger than for shrimp (see Fig E1 in this article's Online Repository at www.jacionline.org). Because levels of sIgE to shrimp and HDM were low, inhibition studies were not feasible. [...]mealworm exposure can lead Tropomyosin-like(Tribolium castaneum) D6X4X3 85 38 12 23 32.3 Actin-87E (Drosophila melanogaster) P10981 60 22 9 14 41.8 TM-E1A = cuticular protein (Tenebrio molitor) Q9TXE4 32 27 3 9 23.2 Other known allergens identified Chitin-binding protein(Nasonia vitripennis) K7IX02 29 8 4 7 23.0 Myosin heavy-like(Tribolium castaneum) D6WVJ3 27 15 9 10 262.1 Troponin T-like(Tribolium castaneum) D6W953 17 14 5 6 45.7 Myosin light chain 2(Tribolium castaneum) D6WZU7 12 9 3 4 31.3 Arginine kinase (fragment[Lasippa tiga]) D1L9H9 11 19 2 2 12.0 Table E3IgE-binding proteins identified in 4 human subjectsProteins were...