Abstract
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.
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