Allergy information for: Shrimp, Neptune rose shrimp (Parapenaeus fissurus)

  • Name: Shrimp, Neptune rose shrimp
  • Scientific Name: Parapenaeus fissurus
  • Occurrence: Eaten as cooked shrimp or prawn, sometimes in batter as scampi, and also cooked in mixed seafood dishes such as paella and often in more general dishes such as Chinese special fried rice.
  • Allergy Information:

    Shrimp along with crayfish, crabs and lobsters are crustaceans. Food allergy to crustaceans is relatively common, symptoms ranging from mild oral allergy to severe symptoms such as anaphylaxis. Cooking does not remove the allergen. Crustacea are the third most important cause of food induced anaphylaxis after peanuts and tree nuts (cashews, almonds, pecans, walnuts, etc.). Thus crustacea and products thereof are listed in annex IIIa of the EU directive on labelling of foods and must be labelled when used as ingredients in pre-packaged food.

    Most allergy to crustacea seems to involve a muscles protein called tropomyosin, which is very similar in a wide range of crustacean foods. As a result someone with allergy to tropomyosin from one kind of crustacean is likely to react to others. Thus individuals with allergy to one kind of crustacean are usually advised to avoid all types of crustacean foods.

    In addition, some individuals with allergies to insects such as cockroach or moths can suffer food allergy to crustacean foods. Whilst most individuals with allergy to shrimps (crustacea) can tolerate molluscs, individuals with allergy to both types of shellfish have been reported. However, individuals allergic to finfish (such as cod or salmon) do not generally have allergies to shellfish.

  • Other Information:

    Crustacea and products thereof are listed in annex IIIa of the EU directive on labelling of foods. Crustacea include shrimps, crabs, crayfish, and lobsters.

  • Taxonomic Information:

    Parapenaeus fissurus ITIS 95743

    Publications on food allergy report data from several species of shrimp, sometimes simply remarking "fresh shrimp were purchased locally" without reporting species. Apart from the gammarus shrimps (ITIS 93773), which have only been reported as occupational allergens, all the shrimp species reported as allergenic are decapodes. The order decapoda contains shrimps, prawns, crawfish, lobsters and crabs. These are believed to have evolved from a Devonian shrimp-like ancestor and the penaeoid shrimps are not more closely related to shrimps such as pandalus than to crabs or lobsters.

    The main shrimp species used in publications on food allergy are:

    1. Metapenaeus ensis (NEWT 32278, ITIS 95814) has the English names greasyback shrimp, offshore greasyback shrimp or sand shrimp.

    2. Farfantepenaeus aztecus (NEWT 6690, ITIS 551570) was called Penaeus aztecus and has the English names brown shrimp, gulf shrimp, golden shrimp, northern brown shrimp, red shrimp or redtail shrimp.

    3. Penaeus monodon (NEWT 6703, ITIS 95638) has the English names tiger prawn, giant tiger prawn or black tiger shrimp.

    4. Fenneropenaeus indicus (NEWT 29960, ITIS 95626) was called Penaeus indicus and has the English names Indian prawn, Indian white prawn, tugela prawn or white prawn.

    5. Fenneropenaeus chinensis (ITIS 551578) was called Cancer chinensis, Penaeus chinensis or Penaeus orientalis and has the English name fleshy prawn. NEWT gives two species, Fenneropenaeus chinensis (NEWT 139456) or Fenneropenaeus orientalis (NEWT 70917).

    6. Parapenaeus fissurus (ITIS 95743) was called Penaeus fissurus and has the English name Neptune rose shrimp. This species and the rose shrimp Parapenaeus fissuroides (NEWT 228860, ITIS 551689) are closely related and sometimes treated as synonyms(

    7. Litopenaeus setiferus (NEWT 64468, ITIS 551680) was called Penaeus setiferus or Cancer setiferus (in some articles Penaeus setifecus) and has the English names white shrimp or northern white shrimp.

    8. Pandalus borealis (NEWT 6703, ITIS 96967) has been sometimes called Pandalus borelis or Pandalus boralis. This is a true rather than a penaeoid shrimp. The English names are northern shrimp, northern red shrimp, pink shrimp, coldwater shrimp or deepwater prawn. As this species is used in the Parmacia Diagnostics (Uppsala, Sweeden) ImmunoCAP system, it is often implied when the species is not named.

    A mixture of Penaeus monodon, Penaeus semisulcatus (ITIS 95644, NEWT 64467, green tiger prawn) and Metapenaeus affinis (ITIS 95784, NEWT 228858, jinga shrimp) is used in extracts from Torii Yakuhin (Kobe, Japan).

    9. Crangon crangon (ITIS 97118) is called the common shrimp and also the brown shrimp or better the European brown shrimp. It is a true shrimp carrying its eggs on its legs.

    Note that several names such as "Atlantic shrimp" or "brown shrimp" are used for more than one species.

    Some articles mention the 19th century division of the crustacea into natantia (swimmers such as shrimps) and reptania (walkers such as crabs). The monophylly and subdivision of reptania has been discussed (Ahyong & O'Meally, 2004 [1653]; Dixon et al, 2003 [1654]; Morrison et al, 2002 [1652]) but natantia has found fewer defenders

  • Last modified: 18 October 2006

Reviews (0)

    References (0)

      Clinical History

      • Number of Studies:1-5
      • Number of Patients:>50
      • Symptoms:

        Clinical histories do not normally include the species of crustacean. Thus the symptoms below are for all types of shrimp.

        Hoffman et al. (1981) [1600] report symptoms from 11 patients as 3/11 eczema flair, 2/11 urticaria, 1/11 angioedema, 1/11 angioedema and urticaria, 1/11 rash, 1/11 eosinophilic granuloma and 2/11 anaphylaxis.

        To avoid double counting of patients, we quote the summary of Besler et al. (2001) [1598] of the symptoms reported by the New Orleans group in 4 articles, noting that laryngeal symptoms, oral allergy and swelling of lips were counted as gastrointestinal symptoms and that wheeze was the main respiratory symptom. White shrimps and brown shrimps were consumed in the area.

        1. Waring et al. (1985) [1613] reported symptoms from 14 patients as 14% fainting, 57% angioedema, 86% urticaria , 43% gastrointestinal and 29% respiratory symptoms.

        2. Daul et al. 1987 [1574] reported symptoms from 33 patients as 21% anaphylaxis, 6% pruritus, 85% urticaria/angioedema, 40% gastrointestinal and 27% respiratory symptoms.

        3. Daul et al. 1988 [1573] reported symptoms from 9 patients as 33% angioedema, 100% pruritus, 11% urticaria , 44% gastrointestinal and 44% respiratory symptoms.

        4. Morgan et al. 1989 [1571] reported symptoms from 36 patients as 72% angioedema, 75% pruritus, 56% urticaria , 42% gastrointestinal and 39% respiratory symptoms.

        Steensma (2003) [1541] reports a case of anaphylaxis (lip angioedema, throat swelling, diffuse flushing, urticaria, abdominal cramps, nausea, wheezing, severe dyspnea, and hypotension with noninvasive blood pressure level of 80/50 mm Hg) following a kiss from someone who had eaten shrimps. Colas des Francs et al (1991) [1615] also report anaphylaxis at low dose.

        There are several reports of shrimp in articles surveying food induced anaphylaxis such as Strickler et al (1986) [522] or Moneret-Vautrin et al. (2003) [1016].

        Harada et al. (2000) [1593] surveyed the Japanese literature and reported that shrimp and wheat are the two most common allergens involved in food dependent exercise induced anaphylaxis, FDEIA, in Japan. Tokunaga et al. (1995) [1596] and Watanabe et al. (1990) [1597] report individual cases of FDEIA to shrimp and Harada et al. (2001) [767] report a case where both aspirin and exercise were required to cause FDEIA after eating shrimp. The first report of FDEIA with crustacea may have been Maulitz et al. (1979) [1705]. Mathelier-Fusade et al. (2002) [880] and McNeil & Strauss (1988) [1614] also reported cases of FDEIA with shrimp.

        Asthma is often the most important symptom of occupational allergy to shrimps. Asero et al. (2002) [1546] describe a case of allergy to aerosols from cooking shrimps with severe asthma and rhinoconjunctivitis associated with eyelid angioedema in a patient who could tolerate eating shrimps.

        Lin et al. (1993) [1565] did not describe symptoms on consumption of the Neptune rose shrimp, Parapenaeus fissurus.

      Skin Prick Test

      • Number of Studies:1-5
      • Food/Type of allergen:Not described
      • Protocol: (controls, definition of positive etc)Not described
      • Number of Patients:Lin et al. (1993) [1565] report tests on 10 patients.
      • Summary of Results:Lin et al. (1993) [1565] report that the 10 patients showed a positive skin test to shrimp without further details.

      IgE assay (by RAST, CAP etc)

      • Number of Studies:0
      • Food/Type of allergen:Lin et al. (1993) [1565] removed the edible portions of shrimp (Parapenaeus fissurus), crab (Portunus trituberculotus), cuttlefish (Sepia esculenta), oyster (Crassostrea gigas) and pomfret (Pampus argenteus) and homogenized these in 1:100 w/v PBS (137 mM NaCl, 2.7 mM KCl, 8 mM Na2HPO4, 14.7 mM KH2PO4, pH 7.4) for 3 minutes in a blender. The suspension was extracted for 16 hours at 4° C and then centrifuged. Ammonium sulfate was added slowly to the supernatant to produce 100% saturation. The precipitate was collected by centrifugation at 12,000 g for 30 min. at 4° C and was disolved in deionized water and dialysed against water for 24 hours at 4° C.  The dialysate was then sterilized by filtration (0.45 µm pore size) and stored.
      • IgE protocol:RAST
      • Number of Patients:Lin et al. (1993) [1565] used sera from 10 shrimp allergic patients aged 14 to 33 years for immunoblotting.
      • Summary of Results:Lin et al. (1993) [1565] reported that the sera from the 10 shrimp allergic patients were all RAST positive for shrimp extract.


      • Immunoblotting separation:

        Lin et al. (1993) [1565] used 1D- or 2D-electrophoresis by the method of Shen et al. (1991) [1617].

      • Immunoblotting detection method:Lin et al. (1993) [1565] electrophoretically transferred proteins to a polyvinylidene difluoride membrane, which was blocked and incubated with diluted sera for 16 hours at room temperature. The blots were washed and incubated with 125I labelled monoclonal anti-human IgE antibodies which was revealed by autoradiography.
      • Immunoblotting results:Lin et al. (1993) [1565] found that IgE from 2/10 sera bound to a band at 86 kDa in shrimp extract, 4/10 to a band at 74 kDa, 1/10 to a band at 50 kDa, 2/10 to a band at 47 kDa, 1/10 to a band at 41 kDa and 7/10 to a band at 39 kDa. The 39 kDa allergen was purified from shrimp and crab by SDS-PAGE and both showed 6 isoforms from pI 5.1 to 5.6 for shrimp and 5.2 to 5.9 for crab by protein staining. Sequences of peptides after digestion of both allergens with the endopeptidase Lys-C showed that the allergens were arginine kinases. The absense of any bands due to tropomyosins is surprising. Protein staining of the extract shows a band near 36 kDa but the extract has not been shown to contain tropomyosin.

      Oral provocation

      • Number of Studies:0
      • Food used and oral provocation vehicle:

        Oral provocation is described for white shrimps (Litopenaeus setiferus) especially the article of Daul et al. (1988) [1572].

        Several articles report oral challenge to "shrimp" in studies of allergy to a range of allergenic foods without giving details of the shrimp species or the food preparations (Rance et al. (2005) [1647]; Osterballe et al (2005) [1764]; Rance & Dutau, 1997[481]; Stricker et al, 1986 [522]; Atkins et al, 1985 [1704]).

      • Blind:Not described for Parapenaeus fissurus.
      • Number of Patients:Not described for Parapenaeus fissurus.
      • Dose response:Not described for Parapenaeus fissurus.
      • Symptoms:Not described for Parapenaeus fissurus.

      IgE cross-reactivity and Polysensitisation

      There is strong IgE cross-reactivity between all the crustacea. The most important allergen in these species is tropomyosin and DeWitt et al. (2004) [1536] reported that recombinant Pen a 1 bound 94% of the IgE from the 6 crustacea specific sera. As tropomyosin is strongly conserved in sequence with more than 99% identity amongst penaeoid shrimps and 92% identity between more distantly related crustacea such as a penaeoid shrimp (Farfantepenaeus aztecus) and a crab (Charybdis feriatus), allergy to crustacea is generally treated as a single allergy.

      Lehrer et al. (1985) [1706] used crossed immunoelectrophoresis to show that of the 7 allergens detected from white shrimp, 5 cross-reacted with crayfish, 3 with lobster and 1 with crab extract. Two precipitins appear to be common crustacea allergens and were present in shrimp, crayfish, lobster and crab.

      Chiou et al. (2003) [1689] studied cross-reactivity of 67 sera IgE with 36 Pharmacia allergens. There was a significant correlation of reactivity between F23 from crab, Cancer pagus, and F24 from shrimp, Pandalus borealis. 27 sera bound F23 and 28 bound F24 and 20 sera bound both allergens. Inhibition studies on 15 sera showed that 3 showed an inhibition of >50% between shrimp and cockroach reactive sera, 11 showed a inhibition of >50% between shrimp and crab reactive sera, and 4 showed a inhibition of >50% between crab and cockroach reactive sera.

      However, Morgan et al. (1989) [1571] report that 1/16 subjects reacted only to white shrimp (Litopenaeus setiferus) extracts and 2/16 subjects to brown shrimp (Farfantepenaeus aztecus) extract alone. Different allergens between the two species were also noted with the 2 sera tested by RAST inhibition, although the allergens might have included tropomyosin fragments. Greater differences might be predicted for less closely related crustacea.

      Crustacea are eaten after cooking so that the resistance of the allergenicity of tropomyosins to heat may cause these to be more dominant. Similarly, the use of extracts from boiled shrimp may favour the identification of the highly conserved tropomyosins. It is possible that less heat stable allergens are more species specific and that reaction to allergens such as arginine kinase (Yu et al. 2003 [1542]) is dependent on both cooking conditions and species. Lin et al. (1993) [1565] report that monoclonal antibodies to shrimp arginine kinase are relatively specific with only 1/2 showing cross-reactivity to a crab extract and with no binding to extracts from mollusca

      There is also IgE cross-reactivity between crustacea and insects, gastropods, bivalves and cephalopods (van Ree et al. 1996 [1609]; Leung et al 1999 [1557]; Goetz & Whisman, 2000 [1594]). This is believed to be due to allergenic tropomyosins. Fernandez et al. (2003) [1539] demonstrated IgE binding and SPT reactivity to shrimp in subjects sensitised by insect and mite allergens without prior exposure to shrimp.

      In contrast to the observed cross-reactivity in IgE binding between arthropods and mollusks, clinical cross-reactivity is less common and some but not all crustacea allergics can tolerate mollusks (Leung et al (1996) [1557]; Ishiwara et al. 1998 [1584]; Ishiwara et al. 1998 [1582]).

      Other Clinical information

      Lin et al. (1993) [1565] report data on the allergens from the shrimp Parapenaeus fissurus. As the allergens are likely to be similar, data on other shrimps is relevant to this entry. As the species is often unspecified, data on "shrimps" is often repeated in several entries.

      Rance et al. (2005) [1647] reported that 13 of 183 food allergic children were allergic to shrimp, showing that shrimp was responsible for 5.3% of food allergies in their population (7th most common). As 2716 questionaires had been returned from children at a number of schools, this implied a prevalence of 0.48%. Osterballe et al (2005) [1764] reported that 3 adults and no children were allergic to shrimp by DBPCFC from their population of 898 children and 936 adults. Thus the adult prevalence of allergy to shrimp was 0.3%.

      Morgan et al. (1989) [1570] reported SPT results with other foods for 36 patients with a history of shrimp allergy. The atopic patients with pulminary symptoms were also more likely to show other sensitizations.

      Morgan et al. (1990) [1567] determined the levels of different classes of IgG antibodies to white shrimp extract in the sera of 31 DBPCFC positive patients. IgG1, IgG2 and IgG4 antibodies levels were higher in shrimp allergic individuals than in controls (significantly for IgG2 and IgG4). However, the IgG levels did not give useful diagnostic information. 

      Sheah-Min & Choon-Kook (2001) [1547] similarly measured levels of IgE, IgG and IgG4 to shrimp and crab (using Bencard allergens) in allergic patients. The levels of these antibodies did not correspond with each other. High IgE or IgG4 levels were significantly associated with allergy. IgE levels were most predictive of allergy but were not a reliable test for allergy.

      Crustacea have been frequently reported as occupational allergens. Several species in addition to those mentioned in articles on food allergy have been reported as occupational allergens including snow crabs (Cartier et al, 1986 [1591]; Cartier et al, 2004 [1610]), Nephrops norvegicus or scampi (Griffin et al, 2001 [1611]) and gammarus shrimps (Fontan et al. 2005 [1765]; Baur et al. 2000 [1550]). Occupational allergy probably involves aerosols (Bang et al. 2005 [1767]; Goetz & Whisman, 2000 [1594]; Desjardins et al 1995 [1561]) and both the stability of tropomyosins in boiling water (Lehrer et al. 1990 [1607]) and their cross-reactivity may be significant. Other allergens such as the 97 kDa allergen of scampi are also stable as aerosols (Griffin et al, 2001 [1611]). However, contact determatis has also been reported (Aasmoe et al, 2005 [1766]; Scharer et al, 2002 [1612]).

      Shellfish can act as hidden allergens in fishcake made from finfish and Faeste et al. (2003) [1616] report a case of anaphylaxis with detection of IgE against shrimp tropomyosin and also detection of (invertebrate) tropomyosin in the fish cake.

      Apparent allergy to shellfish can arise from allergy to parasitic worms (Gonzalez-Galan et al. 2002 [1388]).

      Reviews (4)

      • Besler M, Daul CB, Leung PSC.
        Allergen Data Collection: Shrimps (Natantia)
        Internet Symposium on Food Allergens 3(1): 37-53. 2001
      • Lehrer SB, Ayuso R, Reese G.
        Current understanding of food allergens
        Ann N Y Acad Sci. 964:69-85.. 2002
        PUBMEDID: 12023195
      • Lehrer SB, Ayuso R, Reese G.
        Seafood allergy and allergens: a review.
        Mar Biotechnol (NY). 5(4):339-348.. 2003
        PUBMEDID: 14719162
      • Chu KH, Tang CY, Wu A, Leung PS.
        Seafood allergy: lessons from clinical symptoms, immunological mechanisms and molecular biology.
        Adv Biochem Eng Biotechnol. 97:205-235.. 2005
        PUBMEDID: 16261809

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      Biochemical Information for Arginine kinase

      • Allergen Name:Arginine kinase
      • Alternatve Allergen Names:39 kD allergen
      • Allergen Designation:Major
      • Protein Family:Arginine and creatine kinases. Pfam domains PF00217 and PF02807.
      • Sequence Known?:Only peptide sequences
      • Allergen accession No.s:N/A
      • 3D Structure Accession No.:N/A
      • Calculated Masses:N/A
      • Experimental Masses:39 kDa
      • Oligomeric Masses:Probably a monomer (France et al, 1997) [1623]
      • Allergen epitopes:Not known
      • Allergen stability:
        Process, chemical, enzymatic:
        Not known but likely to be less stable than tropomyosin.
      • Nature of main cross-reacting proteins:

        Other arthropod arginine kinases are more than 77% identical in amino acid sequence and identity is more than 90% within the decapoda. Thus extensive IgE cross-reactivity is highly likely between arthropods. However, the closest vertebrate homologues are the creatine kinases which are approximately 45% identical in sequence and are not expected to cross-react.

        Thus, Yu et al. (2003) [1542] used sera from 13 Pen m 2 allergic individuals and found IgE binding with 13/13 sera to sand shrimp (Metapenaeus ensis), 12/13 sera to lobster (Homarus gammarus), 11/13 sera to crawfish (Metanephrops thomsoni), and 11/13 sera to crab (Scylla serrata).

        Binder et al. (2001) [1588] report IgE cross-reactivity between arginine kinases from moth, dust mite, cockroach, king prawn, lobster, and mussel.

        Neither Lin et al. (1993) [1565] using two anti-arginine kinase monoclonal IgGs with pomfret nor Binder et al. (2001) [1588] using IgE with cod observed any cross-reaction with vertebrate muscle.

      • Allergen properties & biological function:Arginine kinase catalyses the reversible production of high-energy phosphoarginine from ATP. Phosphoarginine is used as a buffer for ATP and stores energy in the high energy N-P bond. This function is replaced by phosphocreatine in vertebrates.
      • Allergen purification:Lin et al. (1993) [1565] purified the 39 kDa allergen on 1D SDS-PAGE. The protein was extracted in 0.5% SDS for 6 days, dialysed and lyophilized.
      • Other biochemical information:

        The peptide sequences of the 39 kDa allergen of Lin et al. (1993) [1565] show that it is closely related to Pen m 2 from Penaeus monodon. A crab allergen also showed similar sequences. The 39 kDa thermolabile allergen of Asero et al. (2002) [1546] may also be related. The peptide sequences reported from Parapenaeus fissurus were


        A 3-dimensional structure of a transition-state analog complex of horseshoe crab (Limulus) arginine kinase is available 1BG0.

      References (5)

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        A case of allergy to airborne, heat-labile shrimp allergens.
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      • Lin RY, Shen HD, Han SH.
        Identification and characterization of a 39 kd major allergen from Parapenaeus fissurus.
        J Allergy Clin Immunol. 92(6):837-845. . 1993
        PUBMEDID: 8258618
      • Yu CJ, Lin YF, Chiang BL, Chow LP.
        Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2.
        J Immunol. 170(1):445-453.. 2003
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      • France RM, Sellers DS, Grossman SH.
        Purification, characterization, and hydrodynamic properties of arginine kinase from gulf shrimp (Penaeus aztecus).
        Arch Biochem Biophys. 345(1):73-78.. 1997
        PUBMEDID: 9281313
      • Binder M, Mahler V, Hayek B, Sperr WR, Scholler M, Prozell S, Wiedermann G, Valent P, Valenta R, Duchene M.
        Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen.
        J Immunol. 167(9):5470-5477.. 2001
        PUBMEDID: 11673567