Allergy information for: Salmon (Salmo salar)

  • Name: Salmon
  • Scientific Name: Salmo salar
  • Occurrence: Salmon from both recreational catches and commercial landings is eaten after cooking from fresh fish. Smoked salmon is likely to have allergenic properties similar to ordinary fish. Canned salmon may have reduced allergenicity as is found with tuna.
  • Allergy Information:

    Allergy to fin fish is relatively common (0.4% of adults in the USA according to one telephone survey), and can be associated with severe symptoms such as anaphylactic shock. Symptoms can also occur after ingestion of only a small quantity of fish with one reported reaction in an individual after receiving a kiss from someone who had recently eaten fish. Allergy to fish is not to be confused with a toxic reaction to histamine in spoiled fish (scombroid fish poisoning).

    Almost all fish allergy seems to involve the protein parvalbumin, which is found in the muscle of most fish. As the parvalbumins are similar in all fish species, individuals allergic to one fish are likely to react to a range of different fish species. Thus after a diagnosis of allergy to one fish species, patients are normally advised to avoid all fin fish. Some individuals also react to frog. Although fin fish and shellfish allergies are not linked, individuals can be allergic to both foods.

    Parvalbumin remains able to cause a reaction after cooking. Thus fish remains allergenic after cooking and other treatments. Fish can be a "hidden" allergen in, for example, pizza toppings. Consequently, the EU labelling regulations require foods containing fish and products thereof to be labelled.

    Supplementary information on Fish Allergy

    Fish and fish products play an important role in human nutrition. Fish is a valuable source of proteins and contains large amounts of healthy fats (so called polyunsaturated fatty acids) and fat-soluble vitamins. However, it also is one of the most common causes of food allergy. Fish allergy is a so-called IgE-mediated food allergy. IgE (Immunoglobulin E) is the allergy antibody.

    Allergy to fish is caused by a reaction to protein in fish meat (muscle). The dominating allergen is a muscle protein called parvalbumin. In professional literature this allergen is often referred to as “Gad c 1” from the Latin name for cod fish Gadus callarias. This major allergen is extremely stable to heat, which means that boiling or frying of fish does not destroy the allergen. Other proteins in fish have been described as allergens, but most reactions to cod (and other fish; see under Related foods) are most likely caused by this one allergen

    Symptoms

    Reactions can be severe and even life-threatening. The severity of symptoms may vary according to the amount ingested and the sensitivity of the person. Often the first symptom is irritation and itching in mouth and throat appearing few minutes after the intake. It can be followed by other allergic reactions such as nausea, vomiting, stomach ache, diarrhoea, hives (also called urticaria or nettle rash), swelling under the skin (also called angioedema), itching and reddening of the skin, worsening of eczema, asthma (wheezing, breathlessness, coughing), hay fever (itchy nose and eyes, sneezing/runny nose), swelling of the airways, and sometimes fatal episodes of allergic shock. Usually a combination of several symptoms is seen.

    Spoiled fish can contain a substance called histamine. This is the same substance that is produced by cells of an allergic patient during an allergic reaction. It is involved in the induction of symptoms. Spoiled fish can elicit symptoms in every person having eaten it. The reaction is similar to an allergic reaction, i.e. swelling, hives, wheezing etc., but it is poisoning.

    Related foods (cross-reactions)

    Most information on fish allergy is gathered on codfish. The variety of fish eaten around the world is immense. Despite this, fish species known to cause allergy belong to a few closely related orders: codfish and hake (Gadiformes), mackerel, tuna and perch (Perciformes), salmon and trout (Salmoniformes), plaice and sole (Pleuronectiformes), herring, anchovy and sardine (Clupeiformes), carp and catfish (Cypriniformes), and eel (Anguilliformes). Patients with allergy to codfish are often allergic to the other fish species as well. This can be explained by similarity of the allergen parvalbumin in all fish species. Allergic reactions based on such similarity are called cross-reactions. The cross-reactivity between fish species is certainly not complete. Some patients are allergic to one and tolerate other species.

    Allergy to fish does not mean that other seafood like shellfish is not tolerated. Cross-reactivity is irrelevant between fish and shellfish. Of course, patients can develop allergy to both independently. Fish roe (or caviar) has been reported to cause food allergy but there is no relation to allergy to the fish from which the eggs originate.

    Finally, it has been reported that parvalbumin in frogs legs can in some cases also cause allergy in fish allergic patients. This again is cause by cross reactivity.

    Who, when, how long and how often?

    Food allergy to fish is seen both among children and adults (approximately 0.1-0.2%). Varieties in food habits according to country influence the frequency patterns of fish allergy, with the number of fish allergics being higher in those countries where fish is a major component of the local diet. In general, fish allergy is not outgrown but it persists through life.

    How much is too much?

    Care has to be taken since very small amounts (few mg, in other words a tiny flake) of fish can elicit a reaction in very sensitive persons. A dose of only 5 mg of cod has been described to cause reaction. Furthermore, some fish allergic persons can get allergic symptoms due to the steam (airborne allergens) from cooking fish. Fish allergy is therefore sometimes a problem in the fish industry and among restaurant cooks, where handling and inhalation might cause eczema and asthma. Finally, even a kiss of somebody that has eaten fish can induce a reaction in a fish allergic person.

    Diagnosis

    An indication for IgE-mediated fish allergy can be obtained from skin prick testing and from serum IgE testing. The presence of a positive skin prick test or of fish protein-specific IgE-antibody in serum is indicative of an IgE-mediated fish allergy, but both tests may be false-positive or false-negative. Therefore, a definitive diagnosis has to be based on strict, well-defined elimination and re-introduction protocols or on controlled fish challenge procedures. Fish allergy is confirmed if symptoms disappear after elimination and re-appear upon re-introduction or if a so-called double-blind placebo controlled food challenge gives a positive result. During such a challenge both doctor and patient do not know which challenge meal contains fish and which does not. Such challenge procedures are also helpful in determining the threshold dose of reactivity, and to verify if a person has outgrown the food allergy, although this is rarely seen with fish allergy.

    Where do I find fish?

    It is important to study the labels on processed foods since various products can contain fish: surimi (fish product imitating crabmeat), fish meal, animal fat, liver pâté, some sausages, crab salad, sushi, oyster sauce, Worcestershire sauce, Caesar salad, tapenade, and pizza toppings. Fish oils/animal oil can also contain fish proteins, depending on the degree of refining of the oil. Fish gelatine made from skin and bones and used in food products is not considered to present a risk to fish allergic persons at the doses typically used.

    Non-food products

    Fish gelatine is applied in pharmaceutical products like vaccines, but it is not considered a risk to fish allergic persons.

    Avoidance

    If suffering from fish allergy, strict avoidance of fish in any form and food containing fish-derived ingredients is the only way to prevent a reaction. This can sometimes be difficult because they can be hidden in food products. According to the new EU labelling directive (2003/89/EC) and the list of the Codex Alimentarius Commission, any fish-derived ingredient has to be listed on the label. Even if labels are carefully read, unintentionally and accidentally consumption of fish may happen. Fish allergic individuals should especially be cautious when eating away from home. When ordering a “non-fish meal” at a restaurant it may be contaminated with fish proteins from utensils, cooking oil or a grill exposed to fish.

  • Other Information:
  • Taxonomic Information:

    The Atlantic salmon, Salmo salar, NEWT 8030, is the salmon species in most publications on food allergy.

    Several other related species of pacific salmon or trout are also eaten in large quantities such as
    Chinook salmon, Oncorhynchus tschawytscha, NEWT 74940
    Chum salmon, Oncorhynchus keta, NEWT 8018
    Coho salmon, Oncorhynchus kisutch, NEWT 8019
    Pink salmon, Oncorhynchus gorbuscha, NEWT 8017
    Sockeye salmon, Oncorhynchus nerka, NEWT 8023
    Rainbow trout or steelhead salmon, Oncorhynchus mykiss, NEWT 8022.

    However, there are also unrelated fish called salmon such as the Western Australian salmon, Arripis truttacea, ITIS 645562.
  • Last modified: 18 October 2006

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    References (0)

      Clinical History

      • Number of Studies:1-5
      • Number of Patients:11-20
      • Symptoms:

        Most articles mentioning allergy to salmon describe allergy to fish in general without attributing symptoms specifically to salmon. For example, Helbling et al. (1996) [1727] describe the symptoms of 39 patients as pruritus (27/39), hives (27/39), asthma and wheezing (21/39), angioedema (20/39), dyspepsia and cramps (7/39), vomiting (3/39), shock (3/39) and fainting (2/39). 13/39 patients had a history of allergic reaction following ingestion of salmon, 16/39 had a positive SPT and 13/24 a positive RAST to salmon.

      Skin Prick Test

      • Number of Studies:1-5
      • Food/Type of allergen:

        Helbling et al. (1996) [1727] made an extract of Alaska pollack and of 4 crustacean species. 16 commercial extracts of fish, including salmon, and 12 commercial extracts of inhalant allergens were also used .

        Bernhisel-Broadbent et al. (1992) [1397] added 10 g. of raw and cooked fish (catfish, bass, perch, mackerel, tuna, salmon, trout, codfish and flounder) to 40 ml. phosphate buffered saline in centrifuge tubes with a glass marble. The tubes were placed in a test tube rotator overnight at 4°C. Samples were centrifuged at 1250 x g for 15 min and then at 16000 x g for 15 min. Supernatants were lyophilized. Skin tests used 1:20 (w/v) saline diluted extracts of raw fish.

        de Martino et al (1990) [1681] used commercial extracts (Lofarma, Milan, Italy). The extracts were diluted 1:20 (w/v) in a glycerol solution.

      • Protocol: (controls, definition of positive etc)

        Helbling et al. (1996) [1727] defined a positive skin prick as producing a 3 mm diameter wheal in a patient who reacted to the positive control (1 mg/ml histamine diphosphate) and not to 50% (v/v) glycerol in PBS. Results were recorded after 15 minutes.

        Bernhisel-Broadbent et al. (1992) [1397] used 1 mg/ml histamine as a positive control and saline as a negative control. Wheal with diameters 3 mm greater than the negative control were considered positive.

        de Martino et al (1990) [1681] used histamine hydochloride, 1 mg/ml, as a positive control and a glycerol solution as a negative control. Diameters were read after 15 minutes and reactions half or more than the size of the positive control, read after 10 minutes, were considered positive. 

      • Number of Patients:

        Helbling et al. (1996) [1727] tested 39 fish allergic study subjects with salmon together with 18 atopic control subjects.

        Bernhisel-Broadbent et al. (1992) [1397] tested 11 patients with histories of fish allergy and 20 controls including 10 atopic patients with other food allergies.

        de Martino et al (1990) [1681] tested 20 cod allergic children and 40 children who had a positive SPT and RAST to a different food.

      • Summary of Results:

        Helbling et al. (1996) [1727] found that 16/39 fish allergic subjects gave a positive skin test to salmon. 

        Bernhisel-Broadbent et al. (1992) [1397] reported that 9 patients showed a positive SPT to salmon with 4-19 mm wheal diameters.  This similar to several other fishes and was a smaller response than to cod but greater than to sardine or tuna. 

        de Martino et al (1990) [1681] reported that 4/20 of the cod allergic children reacted to salmon extract. None of the cod negative children reacted.

      IgE assay (by RAST, CAP etc)

      • Number of Studies:0
      • Food/Type of allergen:

        Helbling et al. (1996) [1727] made an extract of salmon (and of Alaska pollack, anchovy, mackerel, rainbow trout, and tuna) by blending 500g of raw fish in 1L of 0.01M PBS, pH 7.2, in a Waring blender for 1-3 minutes at room temperature. The mixture was extracted overnight at 4°C and centrifuged (70,000 g). Supernatants were concentrated  with an Amicon YM1 filter (molecular weight cut-off 1 kDa) and recentrifuged (180,000 g).

        Bernhisel-Broadbent et al. (1992) [1319] used extracts as described for skin tests by Bernhisel-Broadbent et al. (1992) [1397] but also made extracts from fish which were cooked and lyophilized to mimic the DBPCFC conditions and from fish which were cooked.

      • IgE protocol:

        Helbling et al. (1996) [1727] used RAST and RAST inhibition. A positive RAST was ≥3% binding of the added radioactivity.

        Bernhisel-Broadbent et al. (1992) [1397] and Bernhisel-Broadbent et al. (1992) [1319] used immunoblotting and Bernhisel-Broadbent et al. (1992) [1397] used ELISA inhibition.
      • Number of Patients:

        Helbling et al. (1996) [1727] tested 24 sera from fish allergic patients with salmon.

        Bernhisel-Broadbent et al. (1992) [1397] tested 6 sera from fish allergic patients.

      • Summary of Results:

        Helbling et al. (1996) [1727] reported a positive RAST with salmon for 13/24 fish-sensitive subjects. The proportion of positive responses varied from 8/11 for cod and 8/12 for haddock to 4/29 for anchovy and 5/27 for tuna. It had been suggested that some positive SPTs with commercial fish extracts were due to histamine contamination and in this study 13/18 and 5/18 atopic controls reacted to anchovy and tuna respectively. However, the correlation for salmon between RAST and SPT results with 10.1% of radioactivity bound by sera from SPT positive subjects and 1.7% bound by sera from SPT negative subjects suggests that SPT results were not influenced by histamine. RAST inhibition of IgE binding to trout extract was greatest for salmon extract, 80%, with pollock giving 50% and tuna near 40% inhibition. Salmon extract gave 40% inhibition of mackerel RAST.

        Bernhisel-Broadbent et al. (1992) [1397] reported that binding of serum IgE from 2 salmon allergic patients could be inhibited by cooked salmon, trout and flounder extract but not by milk whey. This suggests that almost all salmon allergenicity is due heat stable conserved proteins such as parvalbumin.

      Immunoblotting

      • Immunoblotting separation:

        Bernhisel-Broadbent et al. (1992) [1397] and Bernhisel-Broadbent et al. (1992) [1319] separated proteins by SDS-PAGE by the method of Dreyfuss et al. (1984) [1799].

      • Immunoblotting detection method:Bernhisel-Broadbent et al. (1992) [1397] and Bernhisel-Broadbent et al. (1992) [1319] transferred proteins electrophoretically onto nitrocellulose membranes in Tris-glycine buffer (pH 9.1) containing 20% (v/v) methanol. These were blocked in PBS with 0.5% porcine gelatin and 0.05% (v/v) Tween 20. The membranes were probed with 1:25 (v/v) diluted sera from fish allergic patients. Bound IgE was revealed by biotinylated goat anti-human IgE, followed by reaction with an enzyme horseradish peroxidase-avidin-D solution (Vector Laboratories, Burlingame, CA). 
      • Immunoblotting results:

        Bernhisel-Broadbent et al. (1992) [1397] showed that IgE from the sera of a salmon allergic patient recognised a 13 kDa allergen in extracts of several raw and cooked fish (catfish, bass, perch, mackerel, tuna, salmon, trout, codfish and flounder extracts were tested).  Tuna and flounder did not show binding. Sera from a flounder allergic patient did not recognise salmon extract but showed the 13 kDa band with catfish, bass, perch and mackerel. Bernhisel-Broadbent et al. (1992) [1319] used sera from the same salmon allergic patient, who had only reacted to salmon by open challenge, and reported that 13 kDa protein in both the lyophilized and non-lyophilized salmon extract bound IgE similarly.

      Oral provocation

      • Number of Studies:1-5
      • Food used and oral provocation vehicle:

        Bernhisel-Broadbent et al. (1992) [1397] initially gave 2 challenges per day of 2 ounces (uncooked weight) of cooked and lyophilized fish (2 ounces = 57 g). The placebo was either Nutramigen (Bristol-Myers, Evansville, IND) or canned tuna (see Bernhisel-Broadbent et al. 1992 [1319]) in 100 mls of juice. After a negative DBPCFC, an open challenge of 4 ounces (114 g) was given. Later challenges used doses of 3 ounces (85 g) in 150 mls of juice. 

        Bernhisel-Broadbent et al. (1992) [1319] used canned salmon for open challenge.

      • Blind:

        Bernhisel-Broadbent et al. (1992) [1397] used blind challenges which if negative were followed by open challenges.

        Bernhisel-Broadbent et al. (1992) [1319] reported open challenges.

      • Number of Patients:

        Bernhisel-Broadbent et al. (1992) [1397] reported 50 oral challenges with 12 fish species to 11 patients. 6 individuals were challenged with salmon. 

        Bernhisel-Broadbent et al. (1992) [1319] reported 2 open challenges with canned salmon and 45 open challenges with canned tuna.

      • Dose response:No dose response reported.
      • Symptoms:

        Bernhisel-Broadbent et al. (1992) [1397] report that a patient reacted to salmon with oral pruritus and cutaneous symptoms. Another patient only reacted on open challenge with oral pruritus and gasterointestinal symptoms. 4 patients did not react to salmon although some of these did react to other fish. There were an unusually large number of false negative challenges over all the fish (7/33 or 21%) but Bernhisel-Broadbent et al. (1992) [1319] reported that the lyophilization for DBPCFC did not alter IgE binding (see immunoblotting above).

        Bernhisel-Broadbent et al. (1992) [1319] reported only negative challenges with canned salmon and tuna. They also note that fish allergic patients had been able to eat these canned fish normally for 2 years. This was attributed to the very long heat treatment of the canning process of approximately 14 hours.

      IgE cross-reactivity and Polysensitisation

      Van Do et al (2005) [1792] used SPT and ELISA inhibition with 12 patients and their sera to characterize the cross-reactivities of native and some recombinant parvalbumins from 9 species (cod, Gadus morhua, Atlantic salmon, Salmo salar, Atlantic mackerel, Scomber scombrus, tuna, Thunus albacares, herring, Clupea harengus, wolffish, Anarhichas sp., halibut, Hippoglossus hippoglossus,  flounder, Platichthys flesus, and Alaska pollack, Theragra chalcogramma). Cross-reactivity was generally observed although some parvalbumins and extracts were poor inhibitors of IgE binding to cod for some sera i.e. 2/10 sera did not show inhibition by salmon parvalbumin (although surprisingly recombinant salmon parvalbumin caused inhibition).

      Tanaka et al. (2000) [1385] used cross-reactions to cluster seafood allergens into 4 groups with salmon, sardine, horse mackerel and mackerel in a group apart from cod and tuna.

      Other Clinical information

      As histamine is the main mediator of IgE mediated allergic reactions, the symptoms of histamine poisoning are similar to allergy to fish (Ohnuma et al. 2001 [1321]; Attaran & Probst, 2002 [1320]). Although histamine toxicity is normally associated with scombroid fish (mackerel, tuna, marlin, swordfish, albacore, bonito, skipjack, and almost 100 other species) which have a high concentration of histidine as a pH buffer, similar reactions have also been reported from several other (non-scombroid) species of fish including salmon (Gessner et al 1996 [1794]; Smart 1992 [1795]).

      Aasmoe et al. (2005) [1766] report occupational allergy to salmon.

      Allergy to salmon caviar seems to be distinct from allergy to fish muscle. Flais et al. (2004) [1790] describe a patient who experienced anaphylactic shock on her initial ingestion of salmon caviar, although she had previously comsumed salmon flesh without symptoms. Makinen-Kiljunen et al (2003) [1376] report serious symptoms in 2 patients after consumption of rainbow trout and whitefish roe. Both patients could consume fish muscle without problems. Kondo et al. (2005) [1801] reported that there was no correlation between IgE binding determined by RAST to extracts of salmon muscle (Oncorhynchus kisutch) and of salmon roe (Oncorhynchus keta) using sera from 27 fish allergic patients. Kondo et al. (2005) [1801] also used sera from 2 patients who had anaphylaxis after consuming salmon roe and from a third who avoided both salmon and salmon roe because of high IgE levels with salmon, salmon roe and chicken egg white. ELISA inhibition with these three sera showed cross-reaction between salmon and herring roe. Weaker inhibition was seen with pollock roe and with salmon extract. No inhibition was seen with hen's egg. Immunoblotting showed IgE binding to salmon roe at 15 and 17 kDa with the sera from the patients who had reacted. The third patient's sera bound to a 21 kDa band. N-terminal sequences suggested that all the bands were fragments of vitellogenin. The 15 and 17 kDa bands were from the beta'-component while the 21 kDa band may have been lipovitellin. Untersmayr et al. (2002) [1793] report a single patient who experienced local symptoms (angioedema of the oral and laryngeal mucosa) and systemic symptoms (wheezing, hypotension and gastric cramps) within minutes after consuming beluga caviar on three occasions. This patient's serum contained IgE binding to bands at masses of 30, 84, 100, and 118 kDa from sturgeon caviar and less intense IgE binding to a 73-kDa band in lumpsucker and an 82-kDa band in trout and salmon caviars. These authors also suggest that the 118 kDa protein might be vitellogenin.

      Reviews (2)

      • Taylor, S. L., Kabourek, J. L., Hefle, S. L.
        Fish allergy: Fish and products thereof
        Journal of Food Science 69 (8) R175-R180.. 2004
        PUBMEDID:
      • Wild LG, Lehrer SB.
        Fish and shellfish allergy.
        Curr Allergy Asthma Rep. 5(1):74-79.. 2005
        PUBMEDID: 15659268

      References (18)

      • de Martino M, Novembre E, Galli L, de Marco A, Botarelli P, Marano E, Vierucci A.
        Allergy to different fish species in cod-allergic children: in vivo and in vitro studies.
        J Allergy Clin Immunol. 86(6 Pt 1):909-914.. 1990
        PUBMEDID: 2262645
      • 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. 101(1 Pt 1):67-74.. 1998
        PUBMEDID: 9449503
      • Aasmoe L, Bang B, Andorsen GS, Evans R, Gram IT, Lochen ML.
        Skin symptoms in the seafood-processing industry in north Norway.
        Contact Dermatitis 52(2):102-107.. 2005
        PUBMEDID: 15725289
      • Flais MJ, Kim SS, Harris KE, Greenberger PA.
        Salmon caviar-induced anaphylactic shock.
        Allergy Asthma Proc. 25(4):233-236.. 2004
        PUBMEDID: 15510582
      • Tanaka R, Ichikawa K, Hamano K.
        [Clinical characteristics of seafood allergy and classification of 10 seafood allergens by cluster analysis]
        Arerugi 49(6):479-486.. 2000
        PUBMEDID: 10916886
      • Lindstrom CD, van Do T, Hordvik I, Endresen C, Elsayed S.
        Cloning of two distinct cDNAs encoding parvalbumin, the major allergen of Atlantic salmon (Salmo salar).
        Scand J Immunol. 44(4):335-344.. 1996
        PUBMEDID: 8845026
      • Van Do T, Hordvik I, Endresen C, Elsayed S.
        Expression and analysis of recombinant salmon parvalbumin, the major allergen in Atlantic salmon (Salmo salar).
        Scand J Immunol. 50(6):619-625.. 1999
        PUBMEDID: 10607310
      • Hamada Y, Tanaka H, Sato A, Ishizaki S, Nagashima Y, Shiomi K.
        Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin.
        Allergology International 53(3), 271-278.. 2004
        PUBMEDID:
      • Makinen-Kiljunen S, Kiistala R, Varjonen E.
        Severe reactions from roe without concomitant fish allergy.
        Ann Allergy Asthma Immunol. 91(4):413-416.. 2003
        PUBMEDID: 14582823
      • Gessner BD, Hokama Y, Isto S.
        Scombrotoxicosis-like illness following the ingestion of smoked salmon that demonstrated low histamine levels and high toxicity on mouse bioassay.
        CLINICAL INFECTIOUS DISEASES 23 (6): 1316-1318. 1996
        PUBMEDID:
      • Smart DR.
        Scombroid poisoning. A report of seven cases involving the Western Australian salmon, Arripis truttaceus.
        Med J Aust. 157(11-12):748-751. . 1992
        PUBMEDID: 1453998
      • Attaran RR, Probst F.
        Histamine fish poisoning: a common but frequently misdiagnosed condition.
        Emerg Med J. 19(5):474-475.. 2002
        PUBMEDID: 12205017
      • Ohnuma S, Higa M, Hamanaka S, Matsushima K, Yamamuro W.
        An outbreak of allergy-like food poisoning.
        Intern Med. 40(8):833-835.. 2001
        PUBMEDID: 11518138
      • Bernhisel-Broadbent J, Strause D, Sampson HA.
        Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods.
        J Allergy Clin Immunol. 90(4 Pt 1):622-629.. 1992
        PUBMEDID: 1401644
      • Bernhisel-Broadbent J, Scanlon SM, Sampson HA.
        Fish hypersensitivity. I. In vitro and oral challenge results in fish-allergic patients.
        J Allergy Clin Immunol. 89(3):730-737.. 1992
        PUBMEDID: 1545094
      • Dreyfuss G, Choi YD, Adam SA.
        Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies.
        Mol Cell Biol. 4(6):1104-1114.. 1984
        PUBMEDID: 6204191
      • Kondo Y, Kakami M, Koyama H, Yasuda T, Nakajima Y, Kawamura M, Tokuda R, Tsuge I, Urisu A.
        IgE Cross-reactivity between Fish Roe (Salmon, Herring and Pollock) and Chicken Egg in Patients Anaphylactic to Salmon Roe
        Allergology International 54(2), 317-323 . 2005
        PUBMEDID:
      • Untersmayr E, Focke M, Kinaciyan T, Poulsen LK, Boltz-Nitulescu G, Scheiner O, Jensen-Jarolim E.
        Anaphylaxis to Russian Beluga caviar.
        J Allergy Clin Immunol. 109(6):1034-1035.. 2002
        PUBMEDID: 12063537

      Biochemical Information for Sal s 1

      • Allergen Name:Sal s 1
      • Alternatve Allergen Names:Parvalbumin, Sal s 1.01, Sal s 1.02
      • Allergen Designation:Major
      • Protein Family:EF hand calcium binding proteins, Pfam PF00036; efhand.
      • Sequence Known?:Yes
      • Allergen accession No.s:

        http://us.expasy.org/cgi-bin/niceprot.pl?Q91482

        http://us.expasy.org/cgi-bin/niceprot.pl?Q91483

      • 3D Structure Accession No.:N/A
      • Calculated Masses:11889 Da (Q91482)
      • Experimental Masses:12 and 14 kDa
      • Oligomeric Masses:Not known
      • Allergen epitopes:Bugajska-Schretter et al. (1998) [1318] show that IgE binding to carp beta-parvalbumin is very much stronger in the presense of calcium, when the protein is in its native folded form, suggesting that the epitopes are primarily conformational.
      • Allergen stability:
        Process, chemical, enzymatic:        Most parvalbumins quickly refold in the presence of calcium and thus allergenicity survives cooking.
      • Nature of main cross-reacting proteins:

        Lindstrom et al. (1996) [1374] report IgE cross reactivity between cod and salmon parvalbumins. Bugajska-Schretter et al. (1998) [1318] reported inhibition of IgE binding to salmon extract after preadsorption of 4 sera with cod extract was 52%, 96%, 74% and 87% for salmon. 

        Bugajska-Schretter et al. 2000 [1314] report that preabsorbtion of sera from 11 fish allergic patients by carp parvalbumin caused mean inhibition of IgE binding of 78% to salmon extract (55%-93%).

        Van Do et al (2005) [1792] used SPT and ELISA inhibition with 12 patients and their sera to characterize the cross-reactivities of native and some recombinant parvalbumins from 9 species with cod. For most sera, both native and recombinant salmon parvalbumins caused significant inhibition of IgE binding to cod parvalbumin. However,  for 2/10 sera, native salmon parvalbumin did not cause inhibition, although surprisingly recombinant salmon parvalbumin caused inhibition, and with 2 further sera inhibition was weak with both native and recombinant salmon parvalbumin.

      • Allergen properties & biological function:

        Parvalbumins control the flow of calcium from troponin C back to membrane bound pumps after a muscle contraction. Each parvalbumin can bind two calcium or (with lower affinity) magnesium ions.

        Most fish beta-parvalbumins are acetylated at the N-terminus and Lingstrom et al (1996) [1374] reported that the N-terminus of salmon parvalbumin was blocked.

      • Allergen purification:

        Lindstrom et al. (1996) [1374] report purification of two parvalbumins by anion exchange chromatography, gel filtration chromatography and high-performance liquid chromatography of salmon muscle extracts.

        Van Do et al (1999) [1396] report production and purification of both parvalbumins as recombinant His-tag fusion proteins using an Escherichia coli expression vector (pET-19b). The His-tag could be partially removed by digestion with enterokinase. The proteins without the His tag showed a MW similar to that of the native protein. Longer digestion or a larger enterokinase concentration led to further degradation of the proteins.

      • Other biochemical information:

        There are two families of beta-parvalbumin sequences in several fishes. One group includes Q90YK7 (Alaska pollack), Q91482 (salmon) and Q90YK9 (cod) and the other Q90YK8 (Alaska pollack), Q91483 (salmon) and Q90YL0 (cod). Each groups shares approximately 75% sequence identity and each sequence has 65-67% sequence identity with members of the other group.  Q91482 and Q91483 are 65-67% identical.

        3-D structures are available of beta-parvalbumins from carp, Cyprinus carpio, 4CPV, whiting, Merlangius merlangus, 1A75, silver hake, Merluccius Bilinearis, 1BU3, and pike, Esox lucius, 1PAL.

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