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.