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Cyp c 1 is the major allergen found in the common carp (Cyprinus carpio) and serves as the prototype for the parvalbumin family of fish allergens (UniProt: P02618). It is a small, acidic protein (approximately 12 kDa) characterized by the presence of EF-hand motifs that coordinate calcium ions, which are essential for maintaining the protein's structural integrity and its potent IgE-binding epitopes (WHO/IUIS). In fish physiology, Cyp c 1 functions as a calcium buffer in fast-twitch muscle fibers to facilitate rapid relaxation. In humans, it is the primary trigger for fish allergy, recognized by specific IgE antibodies in over 90% of fish-allergic individuals, and its high stability allows it to resist denaturation during cooking and digestion (PMID: 15131215). As a therapeutic target, Cyp c 1 is the focus of allergen-specific immunotherapy (AIT) aimed at desensitizing patients and preventing life-threatening anaphylaxis. Current biotechnological efforts involve the development of recombinant or hypoallergenic variants of Cyp c 1 that retain T-cell reactivity while reducing IgE-mediated side effects to improve the safety and efficacy of treatment (PMID: 28641383).
Induction of immune tolerance by promoting T-regulatory (Treg) cell activity and the production of allergen-specific IgG4 antibodies, which act as blocking antibodies to prevent IgE-mediated mast cell degranulation (PMID: 22404457).
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