Marine molluscs are seafood consumed worldwide and could cause food allergies, while investigation on their sensitizing components and cross-reactivity seems to be rare. Furthermore, allergy to mites may result in anaphylaxis in mollusc-allergic individuals owing to their cross-reactivity. The aim of the study was to identify cross-reactive allergens and investigate the cross-reactivity between different mollusc groups and mite-mollusc. The extracted mollusc and dust mite proteins were separated by SDS-PAGE, and IgE-binding components were recognized by immunoblotting with sera from patients sensitized to mollusc and mite. Cross-reactivity of different mollusc groups and mite-mollusc was assessed using ELISA and inhibition ELISA. The results of the immune detection, ELISA, and inhibition ELISA indicated that different mollusc groups and mite-mollusc showed varying degrees of cross-reactivity. The most frequently recognized cross-reactive protein was paramyosin from different mollusc groups and dust mite, while cross-reactive allergen paramyosin in the mite extract was identified and evaluated by MS and Allermatch, respectively. Inhibition ELISA studies also revealed that paramyosin played an important role in molluscan and mite-molluscan cross-reactivity. These findings contribute to a better understanding of the cross-reactivity involving mollusc species and mite-mollusc, which can be used to assist in the diagnosis and treatment of mite- and mollusc-allergic disorders.

Besides tropomyosin (TM) that is widely recognized as a major allergen in molluscs, a 99-kDa novel allergen (Rap v 2) was recently found in the sea snail Rapana venosa and identified as paramyosin (PM). However, the allergenic epitopes of PM in any molluscs have not been identified yet. In the present study, seven allergenic epitopes of Rap v 2 were identified by immunoinformatics tools, dot-blot inhibition assay, and basophil degranulation assay. Based on the analysis of PM and allergenic epitope amino acids, it was found that highly hydrophobic and positively charged amino acid residues play an important role in the formation of Rap v 2 epitopes. In addition, three potential critical amino acids that may account for TM and PM cross-reactivity in molluscs were found by sequence- and structure-based methods. These findings could be of major importance for improving the understanding of relevant paramyosin epitopes and the prevention and therapy of mollusc allergy.

Seafood refers to several distinct groups of edible aquatic animals including fish, crustacean, and mollusc. The two invertebrate groups of crustacean and mollusc are, for culinary reasons, often combined as shellfish but belong to two very different phyla. The evolutionary and taxonomic diversity of the various consumed seafood species poses a challenge in the identification and characterisation of the major and minor allergens critical for reliable diagnostics and therapeutic treatments. Many allergenic proteins are very different between these groups; however, some pan-allergens, including parvalbumin, tropomyosin and arginine kinase, seem to induce immunological and clinical cross-reactivity. This extensive review details the advances in the bio-molecular characterisation of 20 allergenic proteins within the three distinct seafood groups; fish, crustacean and molluscs. Furthermore, the structural and biochemical properties of the major allergens are described to highlight the immunological and subsequent clinical cross-reactivities. A comprehensive list of purified and recombinant allergens is provided, and the applications of component-resolved diagnostics and current therapeutic developments are discussed.