Abstract
Background: Fish is one of the most common causes of IgE-mediated adverse reactions to food. Several allergens have been identified and characterized from different fish species, among them, parvalbumin, as a highly conserved protein, is the most common causative agent of fish-borne allergies. Although most fish-allergic patients are sensitive to various species, some patients only show hypersensitivity to certain species such as salmonids. In this study, we computationally identified and mapped mono-sensitivity-causing Epitopes of salmonid fish and their cross-reactive Epitopes using in silico methods.
Methods: Amino acid sequences of parvalbumins were retrieved from NCBI, and following alignment, the phylogenic tree was drawn and potential Epitopes were determined and their physicochemical properties analyzed.
Results: We found that fish-allergic patients are mostly sensitized to beta-1 isoform of parvalbumin and its epitope C region (65-109) in salmonids is probably the causative agent of monosensitivity, while in beta-2 isoforms it may justify cross-reactivity of parvalbumins.
Conclusion: Surely, any progresses in biochemical, immunological, and molecular mechanism of allergic reactions to fish allergens can improve accurate diagnosis of fish allergy and its' prevention and treatment in the future.
Keywords: Calcium-binding proteins, mono-sensitivity, cross-reactivity, parvalbumin, allergy, IgE.
Graphical Abstract
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