Fish parvalbumin allergen (Parvalbumin)

Fish parvalbumin allergen is a highly stable, low-molecular-weight calcium-binding muscle protein (usually 10–12 kDa, 108–113 amino acids) prevalent in the white muscle of most bony fish species. Parvalbumins belong to the EF-hand protein family and exist as two phylogenetic lineages: alpha and beta; only the beta-type is considered a major food allergen in fish. Parvalbumin functions physiologically as a Ca2+ buffer involved in muscle relaxation, but pathologically, it is the primary allergen causing fish-induced food allergies via IgE-mediated immune responses. The allergen is characterized by its strong resistance to digestion and heat, as well as a high clinical cross-reactivity among fish species due to conserved IgE-binding epitopes. Clinical manifestations include oral allergy syndrome, abdominal pain, urticaria, asthma, and anaphylaxis in allergic individuals. Diagnostic tests often measure parvalbumin-specific IgE as a biomarker, and the molecule is a key focus in risk management for allergic consumers. Parvalbumin is not a therapeutic drug target but is important in allergy diagnosis, food safety, and forensic fish identification.

Other names

Fish parvalbuminsBeta-parvalbuminPVALBFish muscle parvalbuminEF-hand calcium-binding protein (family)Gad m 1 (Atlantic cod parvalbumin, example of species-specific allergen name)Sco j 1 (Pacific mackerel parvalbumin, species-specific)

None applicable for drugs. Parvalbumin as an allergen primarily acts by binding IgE antibodies in allergic individuals, leading to immune cell activation and allergy symptoms. If considered for immunotherapy, mechanism would be immune tolerance induction to parvalbumin.