Allergy information for: Shrimp, greasyback shrimp (Metapenaeus ensis)

Name: Shrimp, greasyback shrimp
Scientific Name: Metapenaeus ensis
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:
Metapenaeus ensis NEWT 32278, ITIS 95814
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 19^thcentury 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:
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:
Commercial shrimp extracts have been used in most studies with shrimp. Pharmacia Diagnostics (Uppsala, Sweden) 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).
Protocol: (controls, definition of positive etc)The protocol of Arai et al. (1998) [1595] is available in Japanese.
Number of Patients:Arai et al. (1998) [1595] tested 3102 adult asthmatic patients with dust mite and cedar pollen allergens and 33 foods.
Summary of Results: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:Leung et al (1996) [1557] used recombinant Met e 1 and extracts made by taking approximatively 2 gm of muscle proteins from each of abalone (Haliotis diversicolor), whelk (Hemifusus ternatana), mussel (Perna viridis), pen shell (Pinna atropurpurea), clam (Lutraria philipinarum), cuttlefish (Sepia madokai), squid (Loligo edulis), octopus (Octopus luteus), shrimp (Metapenaeus ensis), mud crab (Scylla serrata), spiny lobster (Panulirus homarus), grasshoppers (Mecopoda elongata), oyster (Crassostrea gigas), and "alaskan scallop" (an unidentified species of the family Pectinidae). The muscle was boiled in deionized distilled water for 10 minutes. The boiled muscle was homogenized with either 100 mmol/L Tris, 10 mmol/L ehtylenediaminetetraacetic acid, 10 mmol/L 2-mercaptoethanol or phosphate-buffered saline (PBS) in a Polytron homogenizer (Brinkman) for 30 seconds and centrifuged at 14,000 rpm for 10 minutes. The supernatant was aliquoted and stored in -70° C. Cockroach (Periplaneta americana) and fruit fly (Drosophila melanogaster) were also extracted but as whole body extracts.
IgE protocol:Immunoblotting (see below).
Number of Patients:
Leung et al (1994) [1562] used sera from 8 shrimp allergic patients and 12 atopic controls.
Leung et al (1996) [1557] used sera from 9 shrimp allergic patients.
Summary of Results:
Immunobltting only.

Immunoblotting

Immunoblotting separation:Leung et al (1994) [1562] and Leung et al (1996) [1557] separated the extracts by SDS-PAGE in a 10% separating gel with a 5% stacking gel. Samples were boiled for 10 minutes in buffer with 4% SDS, 10% 2-mercaptoethanol before loading.
Immunoblotting detection method:Leung et al (1994) [1562] and Leung et al (1996) [1557] electrophoretically transferred proteins onto a nitrocellulose filter in a semi-dry transfer cell (Bio-Rad) at 15 V for 1 hour. Strips of the blot were blocked with 3% (w/v) nonfat dried milk in PBS for 30 minutes. Strips were incubated in the test serum (1:10 dilution) in PBS with 3% milk at 4°C overnight with shaking. The strip was washed in PBS-Tween (0.05% Tween-20 in PBS) at room temperature three times for 20 minutes each. The bound IgE on the strip was detected by incubation with ¹²⁵I-labeled anti-human IgE (Sanofi-Pasteur Diagnostics, Ohaska, Minn.) in PBS buffer with 3% milk at 4°C overnight. Nonspecific binding was removed by washing the strip with PBS-Tween at room temperature three times for 20 minutes. The strips were exposed to x-ray film with an intensifying screen from 24 hours to 1 week at -70°C.
Immunoblotting results:
Leung et al (1994) [1562] used immunoblotting to detect clones producing recombinant Met e 1.
Leung et al (1996) [1557] chose 9 sera which bound Met e 1 at 38 kDa. The 38 kDa band was found with 9/9 sera in the extracts of shrimp (Metapenaeus ensis), mud crab (Scylla serrata), spiny lobster (Panulirus homarus), grasshoppers (Mecopoda elongata), cockroach (Periplaneta americana), fruit fly (Drosophila melanogaster), abalone (Haliotis diversicolor), whelk (Hemifusus ternatana), mussel (Perna viridis), pen shell (Pinna atropurpurea), scallop, oyster (Crassostrea gigas), clam (Lutraria philipinarum), cuttlefish (Sepia madokai), squid (Loligo edulis), and octopus (Octopus luteus) but not with chicken or mouse. A 49 kDa band was seen with 8/9 sera with whelk (Hemifusus ternatana), with 7/9 sera with squid (Loligo edulis), with 4/9 sera with pen shell (Pinna atropurpurea) and with 2/9 sera with oyster (Crassostrea gigas). Pen shell, scallop, oyster, squid, and octopus also bound IgE from a single serum at 68-72 kDa. This serum also bound a 28 kDa band from octapus. Preabsorption of the tested sera with the recombinant shrimp tropomyosin, Met e 1, resulted in complete inhibition of their IgE reactivity to the 38 kDa protein present in all the tested mollusks.

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 Metapenaeus ensis.
Number of Patients:Not described for Metapenaeus ensis.
Dose response:Not described for Metapenaeus ensis.
Symptoms:Not described for Metapenaeus ensis.

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.

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

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 (7^th 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.
Seafood allergy and allergens: a review.
Mar Biotechnol (NY). 5(4):339-348.. 2003
PUBMEDID: 14719162
Lehrer SB, Ayuso R, Reese G.
Current understanding of food allergens
Ann N Y Acad Sci. 964:69-85.. 2002
PUBMEDID: 12023195
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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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
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[A study of food-dependent exercise-induced anaphylaxis by analyzing the Japanese cases reported in the literature]
Arerugi. 49(11):1066-1073.. 2000
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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
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Arai Y, Sano Y, Ito K, Iwasaki E, Mukouyama T, Baba M.
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Rance F, & Dutau G
Labial food challenge in children with food allergy.
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Stricker WE, Anorve-Lopez E, Reed CE,
Food skin testing in patients with idiopathic anaphylaxis.
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Tokunaga H, Kokubu F, Okamoto M, Miyamoto M, Hanyuuda M, Adachi M.
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Watanabe T, Sakamoto Y, Tomonaga H, Inuyama M, Sasayama H, Hara K, Imamura Y, Asai S.
[A case of food-dependent exercise-induced anaphylaxis]
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Leung PS, Chen YC, Mykles DL, Chow WK, Li CP, Chu KH.
Molecular identification of the lobster muscle protein tropomyosin as a seafood allergen.
Mol Mar Biol Biotechnol. 7(1):12-20.. 1998
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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
Leung PS, Chu KH, Chow WK, Ansari A, Bandea CI, Kwan HS, Nagy SM, Gershwin ME.
Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen.
J Allergy Clin Immunol. 94(5):882-890.. 1994
PUBMEDID: 7963157
Mathelier-Fusade P, Vermeulen C, Leynadier F.
[Responsibility of food in exercise-induced anaphylaxis: 7 cases]
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Biochemical Information for Met e 1

Allergen Name:Met e 1
Alternatve Allergen Names:Tropomyosin
Allergen Designation:Major
Protein Family:Pfam PF00261; Tropomyosin family
Sequence Known?:Yes
Allergen accession No.s:http://us.expasy.org/cgi-bin/niceprot.pl?Q25456
3D Structure Accession No.:N/A
Calculated Masses:31705 Da
Experimental Masses:34 - 38 kDa (by SDS-PAGE). Tropomyosins run near 50 kDa with 6M urea.
Oligomeric Masses:
Tropomyosins form dimers.
Allergen epitopes:
No data available for Met e 1.
However, Ayuso et al. (2002) [1545] used 46 overlapping synthetic 15 amino acid peptides with sera from 18 shrimp-allergic subjects to identify the IgE-binding regions of Pen a 1, the tropomyosin from Farfantepenaeus aztecus. 5 major IgE-binding regions were identified as residues 43-57, 85-105, 133-148, 187-202 and 247-284. In addition, 22 peptides as minor IgE-binding regions were identified.
Similarly, Shanti et al. (1993) [1576] digested Pen i 1 with trypsin and identified two peptides corresponding to residues approximately 153-160 and 50-66 as epitopes.
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:
Reese et al. (1997) [1577] determined the sequence of Pen a 1, the tropomyosin from Farfantepenaeus aztecus. They showed that the 30 DNA substitutions only resulted in a single amino acid substitution. The tryptic peptides reported by Shanti et al. (1993) [1576] from Fenneropenaeus indicus included 4 amino acid substitutions in 150 residues. Thus penaeoid shrimp tropomysins are likely to be immunologically almost identical.
DeWitt et al. (2004) [1536] report that the level of sequence identity of tropomyosins with Pen a 1 is 99% for lobster (Homarus americanus), 92% for crab (Charybdis feriatus), 78-82% for insects and dust mites, 71% for a nematode (Caenorhabditis elegans) and 57% for both blue muscle (Mytilus edulis) and human, suggesting that IgE cross-reactivity is very likely for the invertebrate tropomysosins. Leung et al (1998) [1554] had earlier reported similar levels of amino acid identity for crab Cha f 1, Met e 1, lobster Pan s 1 and Hom a 1 and Homarus americanus slow muscle, fruit fly and chicken tropomyosins.
DeWitt et al. (2004) [1536] also showed specific IgE binding to recombinant Pen a 1 and seven invertebrate extracts with 9 sera. 6 sera bound extracts from crustacea most strongly, 2 bound dust mite extract more strongly and one serum showed similar binding with both extracts. rPen a 1 bound 94% of the IgE from the 6 crustacea specific sera and gave 50% inhibition of the binding of extracts at about 0.1 µg/ml.
Ayuso et al. (2002) [1543] investigated the binding of IgE to the sequences from other invertebrates related to the epitopes identified by Ayuso et al. (2002) [1545]. The epitope sequences were >90% identical between crustaceans, mites and cockroach. These epitopes were also reported to be related to those found in Pen i 1 from Fenneropenaeus indicus (Shanti et al. 1993 [1576]). However, the epitopes identified from oyster (Ishiwara et al. 1998 [1584]) and horned turban (Ishiwara et al. 1998 [1582]) were different. Ayuso et al. (2002) [1543] suggest that, in general, 2 amino acid substitutions in an epitope removes IgE binding.
Leung et al (1996) [1557] used sera from 9 shrimp allergic patients and tested for cross-reactivity on immunoblots. As well as all arthropods (crustacea and insects), IgE binding was seen with all 9 sera to tropomyosins from gastropods: abalone (Haliotis diveriscolor) and whelk (Hemifusus ternatana), bivalves: mussel (Perna viridis), pen shell (Pinna atropupurea), scallop, oyster (Crassostrea gigas) and clam (Lutraria philipinarum) and cephalopods: cuttlefish (Sepia madokai), squid (Loligo edulis) and octopus ((Octopus luteus). None of the sera bound to either chicken or mouse tropomyosin. Reese et al. (1996) [1560] also reported that porcine, bovine and rabbit tropomyosins did not bind IgE.
Leung et al (1998) [1555] demonstrated that allergy to both spiny lobster and American lobster (Panulirus stimpsoni and Homarus americanus) was due to tropomyosins and that preincubation of sera with the recombinant shrimp tropomyosin Met e 1 removed their IgE reactivity to lobster muscle extracts.
As allergy to crustacea is dominated by reactions to the tropomysosins, clinical data on cross-reactivity and studies on IgE binding to extracts is also informative. Fernandez et al. (2003) [1539] demonstrated IgE binding and SPT reactivity in subjects sensitised by insect and mite allergens without prior exposure to shrimp.
In contrast to the extensive observed cross-reactivity in IgE binding, 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]).
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:
Leung et al (1998) [1555] report the production of recombinant Met e 1.
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] showed that Sa-II was a tropomysosin and Sa-I a fragment of Sa-II.
Other biochemical information:

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