Abstract
Background: Shrimp allergy is a leading cause of anaphylaxis in patients with food allergies and the most common cause of food allergy in adults. There are known conserved B-cell allergen IgE binding epitopes that would predict cross-reactivity of shellfish allergens, but patient shrimp specific IgE binding has not been assessed in different shrimp species.
Objective: This study examines the IgE binding pattern to major shrimp proteins in two different shrimp species among US shrimp allergic patients.
Methods: Patients with a physician-diagnosed shrimp allergy were recruited for this analysis. Skin prick testing to raw shrimp, cooked shrimp, shrimp extract, Dermatophagoides pteronyssinus (Der p1) , Dermatophagoides farinae (Der f1) , cockroach, codfish, crab, lobster, and oyster extracts were performed in all patients. Serum collected from US shrimp allergic patients were analyzed by Western Blot to assess the IgE binding patterns for major shrimp allergens in two different shrimp species, Penaeus aztecus (Brown shrimp) andPenaeus monodon (Black tiger shrimp).
Results : Specific IgE (sIgE) binding to the major and minor shrimp allergens including tropomyosin, arginine kinase, myosin light chain, hemocyanin and sarcoplasmic calcium binding protein was evaluated. The sIgE binding pattern in US shrimp allergic patients for the major heat-stable shrimp allergens tropomyosin, myosin light chain and sarcoplasmic protein were similar for different shrimp speciesPenaeus aztecus (Brown shrimp; Gulf of Mexico) and Penaeus monodon (Black tiger shrimp; Southeast Asia), suggesting conservation of epitopes between species.
Conclusion : Given similar sIgE binding patterns for the major shrimp proteins in the two different shrimp species, shared epitopes are observed between shrimp species. This knowledge may help with the diagnosis of shrimp allergy and cross-reactivity, as it could lend itself to the development of a component-resolved diagnostic assay to identify sIgE to epitopes in different shrimp species.