Allergy information for: Shrimp, Indian prawn (Fenneropenaeus indicus)

  • Name: Shrimp, Indian prawn
  • Scientific Name: Fenneropenaeus indicus
  • 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:

    Fenneropenaeus indicus NEWT 29960, ITIS 95626

    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(http://www.fa.gov.tw/tfb10/e/f3/a52b.htm).

    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 http://tolweb.org/tree?group=Decapoda.
  • 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.

      Skin Prick Test

      • Number of Studies:1-5
      • Food/Type of allergen:An extract of Fenneropenaeus indicus was reported (Nagpal et al. 1987) [1711] but its use for SPT was not mentioned and commercial extract may have been used.
      • Protocol: (controls, definition of positive etc)Not reported
      • Number of Patients:Shanti et al. (1993) [1576] report SPT from 4 patients.
      • Summary of Results:Shanti et al. (1993) [1576] report that the 4 patients whose sera were used gave positive skin tests.

      IgE assay (by RAST, CAP etc)

      • Number of Studies:0
      • Food/Type of allergen:Shanti et al. (1993) [1576] extracted tropomyosin from uncooked shrimp and purified it by ethanol precipitation, ammonium sulfate fractionation and isoelectric precipitation. Nagpal et al. (1989) [1572] and Shanti et al. (1993) [1576] purified the allergen Pen i 1 (SA-II) from boiled shrimp by ion exchange chromatography on DEAE-Sephacel and size exclusion chromatography.
      • IgE protocol:Shanti et al. (1993) [1576] used ELISA
      • Number of Patients:Shanti et al. (1993) [1576] tested sera from 4 patients.
      • Summary of Results:Shanti et al. (1993) [1576] report IgE binding to Pen i 1 (tropomyosin) in ELISA and IgE binding to tryptic peptides of Pen i 1 in ELISA and dot-blot immunoassay.

      Immunoblotting

      • Immunoblotting separation:Shanti et al. (1993) [1576] used 15% SDS PAGE by the method of Laemmli (1970) [948].
      • Immunoblotting detection method:Shanti et al. (1993) [1576] transferred proteins to nitrocellulose by the method of Towbin et al. (1979) [1069].
      • Immunoblotting results:Shanti et al. (1993) [1576] showed that the allergen Pen i 1 and purified tropomysosin both bound human IgE as a band at approximately 34 kDa. Both also ran at 50 kDa in 6 M urea (with staining for protein).

      Oral provocation

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

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

        Nagpal et al. (1987) [1711] do not give details of their recipe for DBPCFC.

        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:

        Daul et al. (1988) [1572] used DBPCFC and open challenge.

        Nagpal et al. (1987) [1711] used DBPCFC

      • Number of Patients:Nagpal et al. (1987) [1711] tested one patient.
      • Dose response:Not reported
      • Symptoms:Nagpal et al. (1987) [1711] report that one of two patients whose sera was used reacted to a DBPCFC to cooked shrimp without further details.

      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.

      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.

      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

      Nagpal et al. (1987) [1711] identified shrimp tRNA as an allergen. However, Besler et al (2001) [1598] comment "existence of tRNA allergen not confirmed by other investigators".

      Rajagopal et al. (2000) [1549] compared the allergenicity and antigenicity in mice of tropomyosin and maleylated tropomyosin from Fenneropenaeus indicus. Maleylated tropomyosin was shown not to bind human IgE and to show reduced antigenicity. However, it showed a similar T-cell response to native tropomyosin.

      As the allergens are likely to be similar, data on other shrimps is relevant to this entry. In particular, much of the early research is listed in the entry for white shrimp. 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 (5)

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        Allergen Data Collection: Shrimps (Natantia)
        Internet Symposium on Food Allergens 3(1): 37-53. 2001
        PUBMEDID:
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      • Wild LG, Lehrer SB.
        Fish and shellfish allergy.
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      • 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 Pen i 1

      • Allergen Name:Pen i 1
      • Alternatve Allergen Names:Tropomyosin, Sa-II 
      • Allergen Designation:None
      • Protein Family:Pfam PF00261; Tropomyosin family
      • Sequence Known?:Only 9 peptides were sequenced.
      • Allergen accession No.s:N/A
      • 3D Structure Accession No.:N/A
      • Calculated Masses:N/A
      • Experimental Masses:34 kDa
      • Oligomeric Masses:Tropomyosins form dimers.
      • Allergen epitopes:

        Shanti et al. (1993) [1576] digested Sa-II and tropomyosin with trypsin. Two peptides, FLAEEADRKYDEVAR and MQQLENDLDQVQESLLKANIQLVEK corresponding to residues approximately 153-160 and 50-66 of tropomyosin individually blocked up to 50% of IgE binding to tropomyosin at 100 pmol/ml. A 1:1 mixture also blocked to 50% without any additive effect. 4 other peptides inhibited up to 20% of IgE binding.

        Also see data for the very similar allergen Pen a 1.

      • Allergen stability:
        Process, chemical, enzymatic:

        Shimakura et al. (2005) [1578] report that partially proteolytically digested shrimp tropomyosin can bind IgE from sera of allergic patients when tested by ELISA inhibition rather than immunoblotting or ELISA. Similarly Reese et al. (1996) [1560] report that Pen a 1 cleaved by CNBr or digested by endoproteinases Lys-C, Glu-C, trypsin, Arg-C or chymotrypsin continued to bind IgE from allergic sera. Naqpal et al 1989 [1572] describe a naturally occuring 8 kDa allergen from Fenneropenaeus indicus which corresponded to a proteolytic fragment of the tropomyosin. Fu et al. (2002) [1833] showed that shrimp tropomyosin (probably Pen a 1) was rapidly degraded by simulated gastric fluid.

        Allergenicity can survive cooking, possibly because tropomyosin have a very simple helical structure which can rapidly refold after denaturation. Extracts from boiled shrimp are frequently used in allergen purification and for extract preparation.

      • Nature of main cross-reacting proteins:

        IgE cross-reactivity is likely with many invertebrate tropomyosins. See data for the similar allergens Pen a 1 and Met e 1.

      • Allergen properties & biological function:Tropomyosins bind to actin in muscle increasing thin filament stability and rigidity. Depolymerization from the pointed end is inhibited, without affecting elongation (Broschat, 1990 [1589]). As tropomyosin prevents the binding of myosin, it may play an important role with troponin in controlling muscle contraction. The sequence exhibits a prominent seven-residues periodicity and this is reflected in the interactions of the 2 polypeptide chains which form a coiled coil structure of two alpha-helices as originally proposed by Crick in 1952 (see the porcine structure 1C1G). Some tropomyosins are N-acetylated modifying the structure of the N terminal region and increasing the affinity for the thin filaments (Greenfield & Fowler, 2002 [1590]).
      • Allergen purification:

        Naqpal et al (1989) [1572] purified two heat-stable allergens, designated as Sa-I and Sa-II, from boiled shrimp (Fenneropenaeus indicus) extracts. Sa-I was isolated by ultrafiltration, Sephadex G-25, and diethylaminoethyl-Sephacel chromatography and gave a single band on SDS-PAGE at 8.2 kDa. Sa-II was purified by successive chromatography on diethylaminoethyl-Sephacel, Bio-Gel P-200, and Sepharose 4B columns. It gave a singe band at 34 kDa on SDS-PAGE.

        Shanti et al. (1993) [1576] used competitive ELISA inhibition to show that Sa-II bound IgE identically to tropomysosin purified from raw shrimp (Fenneropenaeus indicus). Sa-II also ran similarly on SDS-PAGE and HPLC of tryptic digests were superimposable. They also showed that Sa-I was a fragment of Sa-II.

      • Other biochemical information:The sequences AEKSEEAVHELQK, RMQQLENDLDQVQESLLKANIQLVEK,
        DKALSNAEGEVAALNRRIQLLEEDLER, LAEASQAADESER, FLAEEADRKYDEVAR,
        EERAETGESKIVELEEELRVVGNNLK, SNQREEEYKNQIK, AEFAER, DELVNEKEKYKQ were reported by Shanti et al. (1993) [1576]. These sequences differ in 4/150 amino acids from Met e 1 after alignment (Leung et al, 1994 [1562]).

      References (7)

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        Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus).
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        Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes.
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        Allergenicity of crustacean extractives and its reduction by protease digestion
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        IgE and monoclonal antibody reactivities to the major shrimp allergen Pen a 1 (tropomyosin) and vertebrate tropomyosins.
        Adv Exp Med Biol. 409:225-230.. 1996
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        Tropomyosin prevents depolymerization of actin filaments from the pointed end.
        J Biol Chem. 265(34):21323-21329.. 1990
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        Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin.
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