Latin name: Cyprinus carpio
Carp allergen components
There are no allergens from Cyprinus carpio listed by International Union of Immunological Societies (IUIS) January 2008.
The Carp is a native of Asia, but extensive introductions have helped to make it the world’s most widely distributed freshwater fish.
The Carp is recognised by its small eyes, thick lips with two barbels at each corner of the mouth, large scales and strongly serrated spines in the dorsal and anal fins. The colour is variable, but often olive green to silvery grey dorsally, fading to silvery yellow on the belly. Small Carp could be confused with Goldfish, Carassius auratus. The latter, however, have no barbels on the corners of the mouth.
Carp are reported to grow to over a metre in length and 60 kg in weight, but 4-5 kg is more usual. They are omnivorous, sucking and straining mud from the bottom, and insects and plants from the surface.
The common Carp has been introduced as a food and ornamental fish into temperate freshwaters throughout the world.
The following allergen has been characterised:
Cyp c 1, a parvalbumin (1).
f355 rCyp c 1
Recombinant non-glycosylated protein produced in an E. coli strain carrying a cloned cDNA encoding Cyprinus carpio allergen Cyp c 1
Common names: Parvalbumin
Biological function: Calcium binding and muscle functioning protein
Mw: 12 kDa
Cyp c 1 is a major fish protein, a parvalbumin (1-3). Parvalbumins are small, acidic calcium-binding buffer proteins found in fast muscle of lower and higher vertebrates. They are thought to be involved in the relaxation process in fast-twitch muscle. They have been identified as the major fish allergens (3). This is the basis for the use of recombinant Carp parvalbumin as a tool for in vitro and in vivo diagnosis of fish allergy. Carp parvalbumin is a 3 EF-hand calcium-binding protein. It has remarkable stability, which explains why, despite cooking and exposure to the gastrointestinal tract, it (along with other paralbumins) can sensitise patients.
Recombinant Carp parvalbumin was found to contain 70 % of the IgE epitopes present in natural extract of Cod, Tuna and Salmon. This suggested that the substance would make a valid tool in the diagnosis of patients with fish allergy (4). In a study aimed at characterising cross-reactive IgE-binding components in 6 different fish species (Cod, Tuna, Salmon, Perch, Carp, and Eel), sera from 30 patients allergic to fish found IgE reactivity to a common allergen in all. This allergen was identified as a parvalbumin and shown to have cross-reactive IgE epitopes (5).
Two Carp parvalbumin isoforms (Cyp c 1.01 and Cyp c 1.02) with comparable IgE binding capacities have been isolated. rCyp c 1.01 reacted with IgE antibodies from all 60 fish-allergic patients tested, induced specific and dose-dependent basophil histamine release, and contained most of the IgE epitopes (70%) present in natural allergen extracts from Cod, Tuna, and Salmon, thus demonstrating the value of recombinant Carp parvalbumin as a diagnostic tool (2).
Parvalbumin has been shown to be a major allergen in other fish. Parvalbumin from Alaska Pollack, a globally important commercial fish species belonging to the Gadidae family (which includes Atlantic cod), was shown to be as potent in antibody binding as Cod Gad c 1 (which has been thoroughly studied and considered as a reference for sensitisation in fish allergy) (6).
Purified Carp parvalbumin has been shown to react with IgE antibodies of more than 95% of individuals allergic to fish, and to contain around 83% of the IgE epitopes present in other fish species(1). Although cross-reactivity may extend to other fish containing parvalbumin, the degree of cross-reactivity would depend on the degree of homology. For instance, a study used sera from 10 patients allergic to fish to evaluate the cross-reactivity among 9 commonly edible fish: Cod, Salmon, Pollack, Mackerel, Tuna, Herring, Wolffish, Halibut, and Flounder: Cod (Gad c 1), Salmon (Sal s 1), Pollack (The c 1), Herring, and Wolffish were shown to share antigenic and allergenic determinants, whereas Halibut, Flounder, Tuna, and Mackerel displayed the lowest level of cross-reactivity. The highest mean IgE ELISA inhibition was obtained by Gad c 1, followed by The c 1, Herring, Sal s 1, Wolffish, Halibut, Flounder, Tuna, and finally Mackerel with the least. Nine of the 10 patients showed positive skin test to Cod, Salmon, and Pollack; 8 patients reacted to recombinant Sal s 1. Positive skin-reactivity to rGad c 1 and rThe c 1 was demonstrated in 1 patient (7).
Parvalbumin has also been shown to be a major allergen in 3 species of Mackerel (Scomber japonicus, S. australasicus and S. scombrus) that are widely consumed and considered to be most frequently involved in incidents of IgE-mediated fish allergy in Japan. In a study in which parvalbumin was purified from the white muscle of 3 species of Mackerel, 4 of 5 sera from fish-allergic patients reacted to all the purified parvalbumins, demonstrating that parvalbumin is the major allergen in common among the various Mackerels (8).
Cod parvalbumin has been shown to also share IgE binding epitopes with frog parvalbumin. In a study investigating whether IgE antibodies of fish allergic persons cross-react with frog parvalbumin, sera of 15 fish-allergic patients and 1 fish- and frog-allergic patient were tested by IgE-immunoblotting against recombinant parvalbumin alpha and beta from frog muscle extract. Fourteen of the sera tested had IgE antibodies recognising low-molecular-weight components in frog muscle extract. Tested against recombinant parvalbumins, 3 of 13 sera reacted with alpha parvalbumin and 11 of 12 reacted with beta parvalbumin from frog. Skin prick tests performed in selected patients with recombinant frog parvalbumin were positive in fish-allergic patients. Inhibition studies showed that a fish- and frog-allergic patient was primarily sensitised to fish parvalbumin (9).
Bugajska-Schretter A, Grote M, Vangelista L, Valent P, Sperr WR, Rumpold H, Pastore A, Reichelt R, Valenta R, Spitzauer S. Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin. Gut 2000;46(5):661-9
Swoboda I, Bugajska-Schretter A, Verdino P, Keller W, Sperr WR, Valent P, Valenta R, Spitzauer S. Recombinant carp parvalbumin, the major cross-reactive fish allergen: a tool for diagnosis and therapy of fish allergy.
J Immunol 2002;168(9):4576-84
Swoboda I, Bugajska-Schretter A, Valenta R, Spitzauer S. Recombinant fish parvalbumins: Candidates for diagnosis and treatment of fish allergy. Allergy 2002;57 Suppl 72:94-6
Torres Borrego J, Martinez Cuevas JF, Tejero Garcia J. Cross reactivity between fish and shellfish. [Spanish] Allergol Immunopathol (Madr) 2003;31(3):146-51
Bugajska-Schretter A, Elfman L, Fuchs T, Kapiotis S, Rumpold H, Valenta R, Spitzauer S. Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion.
J Allergy Clin Immunol 1998;101(1 Pt 1):67-74.
Van DT, Hordvik I, Endresen C, Elsayed S. Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M.
Mol Immunol 2005;42(3):3-353
Van Do T, Elsayed S, Florvaag E, Hordvik I, Endresen C. Allergy to fish parvalbumins: studies on the cross-reactivity of allergens from 9 commonly consumed fish.
J Allergy Clin Immunol 2005;116(6):6-1320
Hamada Y, Tanaka H, Ishizaki S, Ishida M, Nagashima Y, Shiomi K. Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels. Food Chem Toxicol 2003;41(8):1149-56
Hilger C, Thill L, Grigioni F, Lehners C, Falagiani P, Ferrara A, Romano C, Stevens W, Hentges F. IgE antibodies of fish allergic patients cross-react with frog parvalbumin. Acta allergologica 2004;59(6):653-60