Shrimp

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Code: f24
Latin name: Pandalus borealis, Penaeus monodon, Metapenaeopsis barbata, Metapenaus joyneri
Source material: Boiled, frozen Atlantic shrimp and raw, frozen prawns from the Indo-West-Pacific
Family: Pandalidae (Pandalus borealis) and Penaeidae (Penaeus monodon, Metapenaeopsis barbata, Metapenaus joyneri)
Shrimp is considered to be a highly allergenic food, causing severe reactions, such as anaphylaxis.

Allergen Exposure

Allergen description
Numerous shrimp species are consumed around the world, and due to the great popularity of Asian food, the consumption of both raw and boiled shrimp is increasing.

Pandalus borealis (deep-water shrimp, cold-water shrimp, northern shrimp, Alaskan pink shrimp, pink shrimp, northern red shrimp) is a very important food resource found in the cold parts of the Atlantic and the Pacific Oceans.

Penaeus monodon (giant tiger prawn, black tiger prawn, leader prawn, grass prawn) is the most important species of farmed crustacean worldwide. The natural distribution is in the Indo-West–Pacific region.
Metapenaeus joyneri (shiba shrimp) and Metapenaeopsis barbata (whiskered velvet shrimp, red rice shrimp, fired prawn) are also economically important shrimps distributed through out the Indo-West–Pacific. The shiba shrimp is particularly popular for making sushi.
 
Allergens
Tropomyosin has been demonstrated as a major allergen in shrimp in several studies (1-3). Argininkinase (mv 40 kD) and an unidentified component of 16.5 kD have also been discussed and might be additional cross-reacting allergens playing a role in allergy to crustaceans (8-9).

Of these allergens, a number have been characterized.
Met e1 (Metapenaeus ensis), Pen a1 (Penaeus aztecus), Pen i1 (Penaeus indicus) and Pen m1 (Penaeus monodon) from Tropomyosin.
Lit v2 (Litopenaeus vannamei) and Pen m2 (Penaeus monodon) from Argininkinase.
 

Potential Cross-Reactivity

Up to date almost 40 different shrimp species have been studied, but so far only a few IgE-binding proteins have been clearly identified. In the majority of these studies the identified allergen component has turned out to be the highly conserved muscle protein tropomyosin (mw 34-38 kD) which is present in all eukaryotic cells (1, 3, 6). Cross-reactivity due to tropomyosin has been shown between crustaceans, molluscs and non-edible arthropods such as insects (cockroach, chironomides) arachnids (house dust mite) and nematodes (2, 6-7,  10, 12).

Clinical Experience

Anaphylactic reactions, urticaria, gastro-intestinal and respiratory symptoms have been reported.

Food-dependent exercise-induced anaphylaxis after consumption of shrimp has occurred. Shrimp is also an occupational allergen connected to work in the food industry.

Seafood may contain high levels of histamine.

Hypersensitivity to crustacean food, such as shrimp, lobster, crayfish and crab is relatively common and symptoms following ingestion can include both local and more severe systematic reactions. Affected individuals typically display allergic reactivity to multiple crustacean species and IgE-sensitization shows association to a wide range of invertebrate foods, including mussels, oysters, squid, and octopus.

References

  1. Shanti K.N., Martin B.M., Nagal S., Metcalfe D.D:, Sabba-Rao P.V. Identification of tropomyosin as the major allergen and characterization ot its IgE-binding epitopes. J Allergy Clin Immunol 1993;151:5354-5363
  2. Leung P.S.C., Chu K.H., Chow W.K., Aftab A.,Bandea C.I., Kwan H.S., Nagy S.M., Gershwin M.E. Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen. J Allergy Clin Immunnol 1994;92:837-845
  3. Daul C.B., Slattery M., Reese G., Lehrer S.B. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. Int Arch Allergy Immunol 1994;105:49-55
  4. Leung P.S.C., Chow W.K., Duffey S., Kwan H.S., Gershwin M.E., Chu K.H. IgE reactivity against a cross-reactive allergen in crustacean and mollusca: evidence for tropomyosin as the common allergen  J Allergy Clin Immunol 1996;98:954-961
  5. Leung P.S.C, Chu K-H Molecular and immunological characterization of shellfish allergens. Frontiers of Bioscience 1998;3:306-312
  6. Reese G., Ayuso R., Lehrer S.B. Tropomyosin: an invertebrate pan allergen. Int Arch Allergy Immunol 1999;119:247-258
  7. Ayuso R., Reese G., Leong-Kee S., Plante M. Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins. Int Arch Allergy Immunol 2002;129:38-48
  8. Samson K.T.R, Chen F.H., Miura K., Odajima Y., Rivas M.N., Minoguchi K. IgE-binding to raw and boiled shrimp proteins in atopic and nonatopic patients with adverse reactions to shrimp. Int Arch Allergy Immunol. 2004; 133:225-232
  9. Yu C-J. Lin Y-F. Chiang B-L., Chow L-P. Proteomics and Immunological analysis of a novel shrimp allergen, Pen m2. J of Immunol 2003;170:445-453
  10. Marknell-Dewitt Å., Mattsson L., Reese G., Lidholm J. Recombinant tropomyosin from Penaeus aztecus (rPen a 1) for measurement of specific immunoglobulin E antibodies relevant in food allergy to crustaceans and other invertebrates. Mol Nutr Food Res 2004;48:370-379
  11. Östlund A, Norén M., Tanaka A., Dahlström J., Borgå Å. IgE antibody patterns to boiled an raw Pandalus borealis, Penaeus monodon, Metapenaeopsis barbata and Metapenaeus joyneri in patient samples from Europe, US and Japan. XXV Congress of EAACI, Vienna, Austria, Abstract Book p.150, 2006
  12. Zhang Y., Matsuo H., Morita E. Cross-reactivity among shrimp, crab and scallops in a patient with seafood allergy. J of Dermatology 2006;3:174-177

 

As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.