Allergy information for: Shrimp, black tiger shrimp (Penaeus monodon)

  • Name: Shrimp, black tiger shrimp
  • Scientific Name: Penaeus monodon
  • 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.

    Supplementary information on Shrimps and other crustaceans Allergy

    Crustaceans are among the most commonly consumed seafoods. Crustaceans belong to the Arthropod family. Crustaceans are divided into six major subgroups that include 44,000 species. Amongst these is a variety of commonly and less commonly eaten sea foods like langoustine, lobster, crayfish, and crab. Other sea foods like clams, mussels, oysters, scallops, abalone and squid are no crustaceans but molluscs or shell fish. Crustacean allergy is a so-called IgE-mediated food allergy. IgE (Immunoglobulin E) is the allergy antibody.

    Symptoms

    Reactions range from mild oral allergy syndrome (itching of the lips, mouth, or throat, and swelling of the lips, tongue, throat, and palate) to life-threatening systemic anaphylaxis (difficulty breathing, drop in blood pressure, and even death). Symptoms occur within one to one hour of ingestion (90% of cases). However, urticaria (hives) is the most frequent symptom. Others symptoms affecting the skin (itching, swelling), gastro-intestinal tract (nausea, cramping heartburn, and diarrhoea), respiratory symptoms (asthma, hayfever), and eyes (conjunctivitis) have been reported. Shellfish are frequently implicated in fatal anaphylactic reactions and are the third most important cause of anaphylaxis after peanuts and tree nuts (cashews, almonds, pecans, walnuts, etc.).

    Symptoms most often occur when the seafood is ingested (generally require higher doses to elicit a reaction), but can also appear when raw seafood is handled and even after inhaling steam while crustaceans such as shrimp are being cooked (may cause respiratory reactions). Cooking oil contaminated with seafood residues has also been reported to cause adverse reactions. Allergic reactions in workers at every stage of seafood processing also occur and are a serious public health problem in countries with major shellfish industries.

    Related foods (cross-reactions)

    It has been estimated that 75% of individuals who are allergic to one type of crustacean (shrimp, lobster, crawfish, or crab) are also allergic to another type. This is referred to as cross-reactivity. Cross-reactions between crustaceans and molluscs (oysters, squid, scallops) are also possible involving the same type of proteins in these foods. In fact, the molecules responsible for the cross-reactions can also cause cross-reactions between crustaceans, dust mites, cockroaches, and chironomid (used as fish food). However, no cross-reactions have been reported between crustaceans and fish such as Pollock, salmon, tuna, mackerel, trout, and anchovies.

    Who, when, how long and how often?

    Food allergies are most frequent in children, but adults are not exempt. Crustaceans, peanuts, fish, and tree nuts are the most common causes of food allergies among adults. Fish and shellfish allergies are estimated to affect approximately 1% of the general population. Countries where large amounts of crustaceans are consumed, such as the Scandinavian countries, have higher rates of crustacean allergies, although no species-specific studies have been conducted. Little is known about their persistence, but all evidence indicates that crustacean allergies are usually not outgrown.

    How much is too much?

    Symptoms most often occur when the seafood is ingested (generally require higher doses to elicit a reaction), but can also appear when raw seafood is handled and even after inhaling steam while crustaceans such as shrimp are being cooked (may cause respiratory reactions). Cooking oil contaminated with seafood residues has also been reported to cause adverse reactions. Allergic reactions in workers at every stage of seafood processing also occur and are a serious public health problem in countries with major shellfish industries.

    While one shrimp is often enough to induce an allergic reaction, some people react to even smaller amounts. Lowest threshold dosages remain to be elucidated.

    Diagnosis

    A detailed patient history is first taken. Skin and laboratory tests are then used to help eliminate allergic foods from the diet. In the case of crustaceans, a positive skin test combined with elevated antibody levels allow shrimp allergies, for example, to be diagnosed with 87% certainty. There is no established threshold value for crustacean specific IgE.

    However, food challenges (giving increasing amounts of potentially allergic food in graduated steps to patients to determine whether they will have an allergic reaction) are the most effective way of determining whether a person is truly allergic to a certain food. Initial food challenges are always conducted as double-blind, placebo controlled tests. In the case of crustaceans, for example, food challenges involve double-blind, placebo-controlled tests using increasing doses of the boiled crustacean in vanilla ice cream containing grape flavouring. If the double-blind placebo-controlled food challenge is negative, an open food challenge is generally performed. Food challenges should only be performed in a hospital setting with highly trained personnel used to dealing with anaphylactic reactions. Patients with a recent history of severe reactions should not be challenged. In addition, patients that are allergic to one type of crustacean should be tested for allergies reactions to all the other crustaceans because of the potential for cross-reactions.

    Where do I find crustacean?

    Crustaceans or crustacean residues may be present in certain processed foods. It is thus very important that people with allergies to crustaceans develop the habit of carefully reading ingredient labels and be aware of the words, terms, and indicators used on labels that indicate the presence of crustaceans or crustacean residues. Food products can contain hidden allergens.

    Non-food products

    Crustaceans are used in few non-food products such as creams. Contact with these products can induce allergic reactions.

    Avoidance

    For patients diagnosed with a crustacean allergy, avoidance of crustaceans is the only proven therapy, especially since adverse reactions to very small amounts of crustaceans are not uncommon. It is thus very important that people with allergies to crustaceans develop the habit of carefully reading ingredient labels and that they are aware of words, terms, and indicators used on labels that indicate the presence of crustaceans or crustacean residues. Food products can contain hidden allergens. Eating out especially in restaurants with South-East Asian cuisine is a risk factor for unexpected contact with crustaceans. Annex IIIa of the new EU labelling directive makes the listing of crustaceans and crustacean products on labels mandatory.

  • 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:

    Penaeus monodon  NEWT 6703, ITIS 95638

    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 (3)

    • Morrison CL, Harvey AW, Lavery S, Tieu K, Huang Y, Cunningham CW.
      Mitochondrial gene rearrangements confirm the parallel evolution of the crab-like form.
      Proc Biol Sci. 269(1489):345-350.\r\n. 2002
      PUBMEDID: 11886621
    • Ahyong, ST; O'Meally, D.
      Phylogeny of the Decapoda reptantia: Resolution using three molecular loci and morphology
      RAFFLES BULLETIN OF ZOOLOGY, 52 (2): 673-693\r\n. 2004
      PUBMEDID:
    • Dixon, CJ; Ahyong, ST; Schram, FR.
      A new hypothesis of decapod phylogeny
      CRUSTACEANA, 76: (8) 935-975\r\n. 2003
      PUBMEDID:

    Clinical History

    • Number of Studies:>20
    • Number of Patients:>50
    • Symptoms:

      Yu et al. (2003) [1542] report that the 18 shrimp-allergic patients who had IgE detectable by immunoblotting with P. monodon crude extract had a history of atopic disease, with 70% having a history of asthma, 65% of allergic rhinitis, and 25% of atopic dermatitis.

      Samson et al. (2004) [1292] divided their 16 shrimp allergic patients into two groups with 9 described as "atopic" and 7 as "non-atopic". The symptoms of the both groups of patients were similar with generalized pruritis (5/9 and 4/7), urticaria (8/9 and 6/7), conjunctivitis (3/9 and 3/7), angioedema (3/9 and 2/7), gasterointestinal (1/7), upper respiratory (3/9 and 3/7), lower respiratory (2/9 and 4/7) and anaphylaxis (2/9).

      Many clinical histories do not include the species of crustacean generally simply specifying "shrimp". The symptoms described in these reports are listed below.

      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 are consumed in this region of the USA.

      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:

      Commercial shrimp extracts have been used in most studies with shrimp. Parmacia Diagnostics (Uppsala, Sweeden) extract Pandalus borealis, Torii Yakuhin (Kobe, Japan) extract a mixture of Penaeus monodon, Penaeus semisulcatus and Metapenaeus affinis while Bencard (Munich, Germany) only specify an extract of cooked shrimp, fit for human consumption (Elizabeth Urban, personal communication).

      Samson et al. (2004) [1292] used the Torii Yakuhin extract.

    • Protocol: (controls, definition of positive etc)Samson et al. (2004) [1292] considered an immediate wheal 3 mm in diameter as positive. All patients had wheal and flare reaction to histamine but not to saline.
    • Number of Patients:

      Samson et al. (2004) [1292] tested 16 patients with a history of adverse reactions to shrimp.

      Arai et al. (1998) [1595] tested 3102 adult asthmatic patients with dust mite and cedar pollen allergens and 33 foods.

    • Summary of Results:

      Samson et al. (2004) [1292] report that 13/16 patients gave positive SPT reactions with shrimp extract. The atopic and non-atopic patients were similar with 7/9 and 6/7 reacting.

      Arai et al. (1998) [1595] report that 625/3102 patients had a positive skin test for one or more food allergens. 27.7% of the patients with a positive test reacted to shrimp which was the most frequently found allergenic food.  

    IgE assay (by RAST, CAP etc)

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

      Samson et al. (2004) [1292] used raw, heated (60°C for 20 min.) or boiled (20 min. in deionized water) black tiger shrimp (Penaeus monodon) muscle which was homogenized in 0.086 M NaCl and 0.033 M NaHCO3 and then stirred overnight at 4°C. After centrifugation at 12000g, the supernatant was dialysed against PBS, aliquoted and stored at -20°C.

      Yu et al. (2003) [1542] ground the shrimp (Penaeus monodon) muscle in a mortar filled with liquid nitrogen, then extracted it for 16 h at 4°C with constant stirring with 50 mM PBS, pH 7.0, containing 0.2 mM DTT and 1 mM PMSF. After centrifugation at 12,000 x g for 10 min at 4°C, the supernatant was dialyzed for 48 h at 4°C against 10 mM sodium phosphate buffer, pH 7.0, then lyophilized to yield the crude extract.

    • IgE protocol:Samson et al. (2004) [1292] used CAP-FEIA-RAST. 0.35 UA/ml of specific IgE was taken as positive.
    • Number of Patients:Samson et al. (2004) [1292] tested sera from 16 patients with a history of adverse reactions to shrimp and 13 controls.
    • Summary of Results:Samson et al. (2004) [1292] detected specific IgE in sera from 89% of the 9 atopic patients with a history of adverse reactions to shrimp but in sera from only 43% of the 7 non-atopic patients with a history of adverse reactions to shrimp. Those with postive SPT also had higher levels of specific IgE.

    Immunoblotting

    • Immunoblotting separation:

      Samson et al. (2004) [1292] separated proteins in a 4-20% gradient gel by SDS-PAGE with 2-mercaptoethanol.

      Yu et al. (2003) [1542] applied 0.5 mg of P. monodon extract to an immobilized pH gradient gel strip containing pH range of 3-10 ampholytes, and isoelectric focusing was performed in a Multiphor II horizontal electrophoresis system (Amersham Pharmacia Biotech). After isoelectric focusing, the strip was subjected to SDS-PAGE on 12.5% gels.

    • Immunoblotting detection method:

      Samson et al. (2004) [1292] transfered proteins to PVDF membranes (Applied Biosystems, Foster, Calif., USA) which had been prewashed with methanol and tris-glycine buffer.The membranes were cut into strips and washed with PBS containing 0.1% Brij 35 (Sigma Diagnostics) and blocked with 0.1% human serum albumin in PBS/Brij for 2 hours at room temperature. Strips were washed and then incubated with sera (diluted 1:10 in PBS/Brij) at 4 °C overnight. After washing, IgE binding was revealed with alkaline phosphatase-conjugated goat anti-human IgE for 2 hours at  room temperature followed by NBT/BCIP solution.

      Yu et al. (2003) [1542] blotted proteins onto PVDF membranes, and incubated with pooled sera from shrimp-allergic patients which showed high IgE binding to the 40-kDa allergen, then bound IgE was detected using alkaline phosphatase-conjugated monoclonal anti-human IgE Abs.

    • Immunoblotting results:

      Yu et al. (2003) [1542] report that immunoblots using sera from 18 out of 80 shrimp allergic patients (22.5%) showed IgE binding to protein bands with apparent molecular masses of 14 - 70 kDa with P. monodon crude extract. Allergens with molecular masses ranging from 30 - 40 kDa were detected by 94% (17 of 18) of these sera. Allergens with molecular masses of 32, 34, and 38 kDa were recognized by 56 - 67% of sera while the allergens with masses of 25, 27, and 40 kDa were bound by 33 - 39%. Other bands, such as 22, 17, and 14 kDa, were detected at frequencies of <30%. The proteins with molecular masses of 32, 34, and 38 kDa were tentatively identified as tropomyosin and were bound by 13/18 sera (72%). 2D-immunoblots with a pool of 6 sera identified the 40 kDa species as arginine kinase and the 32 and 38 kDa peaks as tropomyosin by MALDI mass spectrometry.

      Samson et al. (2004) [1292] reported that SDS-PAGE of raw shrimp meat revealed at least 14 bands from 6.5 to 129 kDa. Heated shrimp (60 °C) showed weaker bands except for the 20 and 70 kDa region. Boiled shrimp showed stronger bands at 16.5 and 20 kDa. IgE from 6/16 sera bound to the 16.5 kDa band both raw and boiled, 5/16 bound to raw and 4/16 to boiled at 40 kDa. IgE from 6/16 sera bound to other bands (20, 22, 54, 72, 129 and 140 kDa) but only with raw shrimp. They note that sera from one atopic and 2 non-atopic patients gave positive immunoblots but were CAP-FEIA-RAST negative. Two of these immunoblots showed IgE binding to the 16.5 kDa allergen.

    Oral provocation

    • Number of Studies:0
    • Food used and oral provocation vehicle:Oral provocation is described for white shrimps (Litopenaeus setiferus) (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 Penaeus monodon.
    • Number of Patients:Not described for Penaeus monodon.
    • Dose response:Not described for Penaeus monodon.
    • Symptoms:Not described for Penaeus monodon.

    IgE cross-reactivity and Polysensitisation

    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.

    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.

    Reese et al. (1996) [1560] report that the extracts from crawfish (Procambarus clarkii), crab (Callinectes sapidus) and lobster (Panulirus argus) showed similar binding to IgE to Pen a 1.

    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. 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 (Lehrer & McCants (1985) [1575]; 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

    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 (4)

    • Besler M, Daul CB, Leung PSC.
      Allergen Data Collection: Shrimps (Natantia)
      Internet Symposium on Food Allergens 3(1): 37-53. 2001
      PUBMEDID:
    • 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

    References (49)

    • Samson KT, Chen FH, Miura K, Odajima Y, Iikura Y, Rivas MN, Minoguchi K, Adachi M.
      IgE binding to raw and boiled shrimp proteins in atopic and nonatopic patients with adverse reactions to shrimp.
      Int Arch Allergy Immunol. 133(3):225-232. 2004
      PUBMEDID: 14976390
    • 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
      PUBMEDID: 12496430
    • Steensma DP.
      The kiss of death: a severe allergic reaction to a shellfish induced by a good-night kiss.
      Mayo Clin Proc. 78(2):221-222.. 2003
      PUBMEDID: 12583533
    • Morgan JE, O'Neil CE, Daul CB, Lehrer SB.
      Species-specific shrimp allergens: RAST and RAST-inhibition studies.
      J Allergy Clin Immunol. 83(6):1112-1117. 1989
      PUBMEDID: 2732411
    • Daul CB, Morgan JE, Hughes J, Lehrer SB.
      Provocation-challenge studies in shrimp-sensitive individuals.
      J Allergy Clin Immunol. 81(6):1180-1186.. 1988
      PUBMEDID: 3379230
    • Daul CB, Morgan JE, Waring NP, McCants ML, Hughes J, Lehrer SB.
      Immunologic evaluation of shrimp-allergic individuals.
      J Allergy Clin Immunol. 80(5):716-722.. 1987
      PUBMEDID: 3680815
    • Waring NP, Daul CB, deShazo RD, McCants ML, Lehrer SB.
      Hypersensitivity reactions to ingested crustacea: clinical evaluation and diagnostic studies in shrimp-sensitive individuals.
      J Allergy Clin Immunol. 76(3):440-445.. 1985
      PUBMEDID: 4031316
    • Colas des Francs V, Kopferschmitt-Kubler MC, Kopferschmit J et al.
      Choc anaphylactique après projection oculaire de jus de crevette.
      Rev Fr Allergol 31: 49-51.. 1991
      PUBMEDID:
    • Arai Y, Sano Y, Ito K, Iwasaki E, Mukouyama T, Baba M.
      [Food and food additives hypersensitivity in adult asthmatics. I. Skin scratch test with food allergens and food challenge in adult asthmatics]
      Arerugi 47(7):658-666.. 1998
      PUBMEDID: 9780440
    • Hoffman DR, Day ED Jr, Miller JS.
      The major heat stable allergen of shrimp.
      Ann Allergy 47(1):17-22.. 1981
      PUBMEDID: 7258736
    • Stricker WE, Anorve-Lopez E, Reed CE,
      Food skin testing in patients with idiopathic anaphylaxis.
      J Allergy Clin Immunol 77: 516-519.. 1986
      PUBMEDID: 3950255
    • Moneret-Vautrin DA, Kanny G, Morisset M, Rance F, Fardeau MF, Beaudouin E.
      Severe food anaphylaxis: 107 cases registered in 2002 by the Allergy Vigilance Network.
      Allerg Immunol (Paris). 36(2):46-51.. 2004
      PUBMEDID: 15061394
    • Harada S, Horikawa T, Icihashi M.
      [A study of food-dependent exercise-induced anaphylaxis by analyzing the Japanese cases reported in the literature]
      Arerugi. 49(11):1066-1073.. 2000
      PUBMEDID: 11193458
    • Tokunaga H, Kokubu F, Okamoto M, Miyamoto M, Hanyuuda M, Adachi M.
      [A case of food-dependent exercise-induced anaphylaxis induced by shrimp]
      Arerugi 44(11):1297-1304.. 1995
      PUBMEDID: 8857109
    • Watanabe T, Sakamoto Y, Tomonaga H, Inuyama M, Sasayama H, Hara K, Imamura Y, Asai S.
      [A case of food-dependent exercise-induced anaphylaxis]
      Arerugi 39(11):1523-1528.. 1990
      PUBMEDID: 2288498
    • Harada S, Horikawa T, Ashida M, Kamo T, Nishioka E, Ichihashi M.
      Aspirin enhances the induction of type I allergic symptoms when compined with food and exercise in patients with food-dependent exercise-induced anaphylaxis
      British Journal of Dermatology 144: 336-339. 2001
      PUBMEDID: 11531805
    • Maulitz RM, Pratt DS, Schocket AL.
      Exercise-induced anaphylactic reaction to shellfish.
      J Allergy Clin Immunol. 63(6):433-434.. 1979
      PUBMEDID: 447945
    • Gonzalez Galan I, Garcia Menaya JM, Jimenez Ferrera G, Gonzalez Mateos G.
      Anaphylactic shock to oysters and white fish with generalized urticaria to prawns and white fish.
      Allergol Immunopathol (Madr). 30(5):300-303.. 2002
      PUBMEDID: 12396966
    • Faeste CK, Wiker HG, Lovik M, Egaas E.
      Hidden shellfish allergen in a fish cake.
      Allergy 58(11):1204-1205.. 2003
      PUBMEDID: 14616143
    • Scharer L, Hafner J, Wuthrich B, Bucher C.
      Occupational protein contact dermatitis from shrimps. A new presentation of the crustacean-mite syndrome.
      Contact Dermatitis. 46(3):181-182.. 2002
      PUBMEDID: 12000333
    • 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
    • Osterballe M, Hansen TK, Mortz CG, Host A, Bindslev-Jensen C.
      The prevalence of food hypersensitivity in an unselected population of children and adults.
      Pediatr Allergy Immunol. 16(7):567-573.. 2005
      PUBMEDID: 16238581
    • Fontan M, Anibarro B, Postigo I, Martinez J.
      Allergy to freshwater shrimp (Gammarus).
      J Investig Allergol Clin Immunol. 2005;15(2):150-2.. 2005
      PUBMEDID: 16047717
    • Bang B, Aasmoe L, Aamodt BH, Aardal L, Andorsen GS, Bolle R, Boe R, Van Do T, Evans R, Florvag E, Gram IT, Huser PO, Kramvik E, Lochen ML, Pedersen B, Rasmussen T.
      Exposure and airway effects of seafood industry workers in northern Norway.
      J Occup Environ Med. 2005 May;47(5):482-492.. 2005
      PUBMEDID: 15891527
    • Griffin P, Allan L, Gibson M, Elms J, Wiley K, Curran AD.
      Measurement of personal exposure to aerosols of Nephrops norvegicus (scampi) using a monoclonal-based assay.
      Clin Exp Allergy 31(6):928-933.. 2001
      PUBMEDID: 11422159
    • Lehrer SB, Ibanez MD, McCants ML, Daul CB, Morgan JE.
      Characterization of water-soluble shrimp allergens released during boiling.
      J Allergy Clin Immunol. 85(6):1005-1013.. 1990
      PUBMEDID: 2355151
    • Desjardins A, Malo JL, L'Archeveque J, Cartier A, McCants M, Lehrer SB.
      Occupational IgE-mediated sensitization and asthma caused by clam and shrimp.
      J Allergy Clin Immunol. 96(5 Pt 1):608-617.. 1995
      PUBMEDID: 7499677
    • Goetz DW, Whisman BA.
      Occupational asthma in a seafood restaurant worker: cross-reactivity of shrimp and scallops.
      Ann Allergy Asthma Immunol. 85(6 Pt 1):461-466.. 2000
      PUBMEDID: 11152166
    • Baur X, Huber H, Chen Z.
      Asthma to Gammarus shrimp.
      Allergy 55(1):96-97.. 2000
      PUBMEDID: 10696868
    • Cartier A, Lehrer SB, Horth-Susin L, Swanson M, Neis B, Howse D, Jong M.
      Prevalence of crab asthma in crab plant workers in Newfoundland and Labrador.
      Int J Circumpolar Health 63 Suppl 2:333-336.. 2004
      PUBMEDID: 15736679
    • Cartier A, Malo JL, Ghezzo H, McCants M, Lehrer SB.
      IgE sensitization in snow crab-processing workers.
      J Allergy Clin Immunol. 78(2):344-348. . 1986
      PUBMEDID: 3734286
    • Sheah-Min Y, Choon-Kook S.
      The relevance of specific serum IgG, IgG4 and IgE in the determination of shrimp and crab allergies in Malaysian allergic rhinitis patients.
      Asian Pac J Allergy Immunol. 19(1):7-10.. 2001
      PUBMEDID: 11495303
    • Morgan JE, Daul CB, Lehrer SB.
      The relationships among shrimp-specific IgG subclass antibodies and immediate adverse reactions to shrimp challenge.
      J Allergy Clin Immunol. 86(3 Pt 1):387-392.. 1990
      PUBMEDID: 2212410
    • Morgan JE, Daul CB, Hughes J, McCants M, Lehrer SB.
      Food specific skin-test reactivity in atopic subjects.
      Clin Exp Allergy 19(4):431-435.. 1989
      PUBMEDID: 2758357
    • Rance F, Grandmottet X, Grandjean H.
      Prevalence and main characteristics of schoolchildren diagnosed with food allergies in France.
      Clin Exp Allergy 35(2):167-172. . 2005
      PUBMEDID: 15725187
    • Ishikawa M; Ishida M; Shimakura K; Nagashima Y; Shiomi K.
      Purification and IgE-binding epitopes of a major allergen in the gastropod Turbo cornutus
      Biosci Biotechnol Biochem. 62(7):1337-1343 . 1998
      PUBMEDID: 9720216
    • Ishikawa M; Ishida M; Shimakura K; Nagashima Y; Shiomi K.
      Tropomyosin, the major oyster Crassostrea gigas allergen and its IgE-binding epitopes
      JOURNAL OF FOOD SCIENCE 63, Iss 1, 44-47 . 1998
      PUBMEDID:
    • Leung PS, Chow WK, Duffey S, Kwan HS, Gershwin ME, Chu KH.
      IgE reactivity against a cross-reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen.
      J Allergy Clin Immunol. 98(5 Pt 1):954-961.. 1996
      PUBMEDID: 8939159
    • Fernandes J, Reshef A, Patton L, Ayuso R, Reese G, Lehrer SB.
      Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews.
      Clin Exp Allergy. 33(7):956-961.. 2003
      PUBMEDID: 12859453
    • Lehrer SB, McCants ML.
      Reactivity of IgE antibodies with crustacea and oyster allergens: evidence for common antigenic structures.
      J Allergy Clin Immunol. 80(2):133-139.. 1987
      PUBMEDID: 2440933
    • Reese G, Tracey D, Daul CB, Lehrer SB.
      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
      PUBMEDID: 9095246
    • DeWitt AM, Mattsson L, Lauer I, 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. 48(5):370-379.. 2004
      PUBMEDID: 15672477
    • Lehrer SB, McCants ML, Salvaggio JE.
      Identification of crustacea allergens by crossed radioimmunoelectrophoresis.
      Int Arch Allergy Appl Immunol. 77(1-2):192-194.. 1985
      PUBMEDID: 4008073
    • Atkins FM, Steinberg SS, Metcalfe DD.
      Evaluation of immediate adverse reactions to foods in adult patients. II. A detailed analysis of reaction patterns during oral food challenge.
      J Allergy Clin Immunol. 75(3):356-363.. 1985
      PUBMEDID: 3973310
    • Rance F, & Dutau G
      Labial food challenge in children with food allergy.
      Pediat Allergy Immunol 8: 41-4.. 1997
      PUBMEDID: 9260218
    • Naqpal S, Rajappa L, Metcalfe DD, Subba Rao PV.
      Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus).
      J Allergy Clin Immunol. 83(1):26-36.. 1989
      PUBMEDID: 2913137
    • Asero R, Mistrello G, Roncarolo D, Amato S.
      A case of allergy to airborne, heat-labile shrimp allergens.
      J Allergy Clin Immunol. 109(2):371-372.. 2002
      PUBMEDID: 11842314
    • McNeil D, Strauss RH.
      Exercise-induced anaphylaxis related to food intake.
      Ann Allergy 61(6):440-442.. 1988
      PUBMEDID: 3202335
    • Mathelier-Fusade P, Vermeulen C, Leynadier F.
      [Responsibility of food in exercise-induced anaphylaxis: 7 cases]
      Ann Dermatol Venereol. 129(5 Pt 1):694-697.. 2002
      PUBMEDID: 12124510

    Biochemical Information for Pen m 1

    • Allergen Name:Pen m 1
    • Alternatve Allergen Names:Tropomyosin
    • Allergen Designation:None
    • Protein Family:Pfam PF00261; Tropomyosin family
    • Sequence Known?:No
    • Allergen accession No.s:

      N/A

    • 3D Structure Accession No.:N/A
    • Calculated Masses:N/A
    • Experimental Masses:34 and 38 kDa, possibly representing two different glycosylated isoforms of the allergen (Yu et al. 2003)  [1542].
    • Oligomeric Masses:

      Tropomyosins form dimers.

    • Allergen epitopes:Not known
    • Allergen stability:
      Process, chemical, enzymatic:      Not known but probably similar to allergenic tropomyosins from other shrimp species, Pen a 1 or Met e 1.
    • Nature of main cross-reacting proteins:Not known but probably similar to allergenic tropomyosins from other shrimp species, Pen a 1 or 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:No purification has been published for Pen m 1. However, see Pen a 1 and Met e 1.
    • Other biochemical information:MALDI ToF mass spectroscopy identified two spots from the 2D separation using the sequence of tropomyosin from shrimp (M. ensis). The sequence coverage was 76% (16 of 21 peptides) and 63% (10 of 16 peptides), respectively.

    References (3)

    • Greenfield NJ, Fowler VM.
      Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin.
      Biophys J. 82(5):2580-2591.. 2002
      PUBMEDID: 11964245
    • 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
      PUBMEDID: 12496430
    • Broschat KO.
      Tropomyosin prevents depolymerization of actin filaments from the pointed end.
      J Biol Chem. 265(34):21323-21329.. 1990
      PUBMEDID: 2250026

    Biochemical Information for Pen m 2

    • Allergen Name:Pen m 2
    • Alternatve Allergen Names:Arginine kinase
    • Allergen Designation:None
    • Protein Family:Arginine and creatine kinases. Pfam domains PF00217 and PF02807.
    • Sequence Known?:Yes
    • Allergen accession No.s:http://us.expasy.org/cgi-bin/niceprot.pl?=Q8I9P7_PENMO
    • 3D Structure Accession No.:N/A
    • Calculated Masses:40112 Da
    • Experimental Masses:40 kDa
    • Oligomeric Masses: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:

      Yu et al. (2003) [1542] purified arginine kinase from Metapenaeus ensis (and also from Metanephrops thomsoni and Scylla serrata) by a modification of the procedure for the purification of the arginine kinase from Farfantepenaeus aztecus reported by France et al (1997) [1623].

      Lyophilized seafood (2.5 g) was peeled and ground in liquid nitrogen in a mortar and extracted for 16 h at 4°C with 25 ml of 0.1 M Tris-HCl, 10 mM 2-mercaptoethanol, 1 mM EDTA, 5 µM NaN3, and 25 µM PMSF, pH 8.0. The extract was centrifuged, a 70% - 90% ammonium sulfate fraction collected, which was then dissolved in 5 ml of 10 mM Tris-HCl, 10 mM 2-mercaptoethanol, and 0.1 mM EDTA, pH 8.0, and dialyzed against the same buffer. The supernatant was then applied to a HiTrap Q Sepharose Fast Flow column (Amersham Pharmacia Biotech) pre-equilibrated with the same buffer. Fractions with arginine kinase activity were eluted with a 25 ml linear gradient from 0 - 1M NaCl in the same buffer.

    • Other biochemical information:

      The 39 kDa allergen of Lin et al. (1993) [1565] from Parapenaeus fissurus is closely related as the peptide sequences match the sequence of Pen m 2.  The 39 kDa thermolabile allergen of Asero et al. (2002) [1546] may also be related.

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

    References (5)

    • 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
      PUBMEDID: 12496430
    • 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
    • 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
    • Asero R, Mistrello G, Roncarolo D, Amato S.
      A case of allergy to airborne, heat-labile shrimp allergens.
      J Allergy Clin Immunol. 109(2):371-372.. 2002
      PUBMEDID: 11842314
    • 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