Shellfish allergy is of increasing concern, as its prevalence has risen in recent years. Many advances have been made in allergen characterization. B cell epitopes in the major allergen tropomyosin have been characterized. In addition to tropomyosin, arginine kinase, sarcoplasmic calcium-binding protein, and myosin light chain have recently been reported in shellfish. All are proteins that play a role in muscular contraction. Additional allergens such as hemocyanin have also been described. The effect of processing methods on these allergens has been studied, revealing thermal stability and resistance to peptic digestion in some cases. Modifications after Maillard reactions have also been addressed, although in some cases with conflicting results. In recent years, new hypoallergenic molecules have been developed, which constitute a new therapeutic approach to allergic disorders. A recombinant hypoallergenic tropomyosin has been developed, which opens a new avenue in the treatment of shellfish allergy. Cross-reactivity with species that are not closely related is common in shellfish-allergic patients, as many of shellfish allergens are widely distributed panallergens in invertebrates. Cross-reactivity with house dust mites is well known, but other species can also be involved in this phenomenon.
Keywords: Arginine kinase; Myosin light chain; Sarcoplasmic calcium-binding protein; Shellfish allergy; Tropomyosin.