Allergy information for: Shrimp, brown shrimp (Farfantepenaeus aztecus)

  • Name: Shrimp, brown shrimp
  • Scientific Name: Farfantepenaeus aztecus
  • 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:

    Farfantepenaeus aztecus NEWT 6690, ITIS 551570

    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:11-20
    • 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:Morgan et al. 1989 [1571] made water soluble shrimp extracts by separately boiling brown shrimps (Farfantepenaeus aztecus) or white shrimps (Litopenaeus setiferus) in deionized water for 15 minutes. Shrimp meat was removed from the shell, degutted and homogenized in PBS, pH 7.2 in a blender. The slurry was shaken overnight at 4°C and centrifuged at 27,500g. The supernatant was concentrated with an Amicon YM5 (cutoff >5000 Da), centrifuged at 105,000g and dialysed against PBS. Extracts were sterile filtered with a 0.45 µm membrane and were tested and found negative for hepatis B surface antigen.
    • Protocol: (controls, definition of positive etc)Morgan et al. 1989 [1571] defined a positive response to shrimp as a mean wheal diameter 3 mm greater than that from the PBS/glycerol (50% v/v) control with a maximum allergen concentration of 10 mg/ml.
    • Number of Patients:

      Morgan et al. (1989) [1571] tested 30 shrimp allergic patients with both white and brown shrimp extracts.

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

    • Summary of Results:

      Morgan et al. (1989) [1571] found that 6/30 were negative to both white and brown shrimp extracts, 23/30 were positive for both extracts and a single patient was positive only for brown shrimp.

      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:

      Morgan et al. 1989 [1571] used the extract of boiled brown or white shrimp described for SPT.

      DeWitt et al. (2004) [1536] used recombinant Pen a 1 and natural tropomyosin from Pandalus borealis. 

      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).

    • IgE protocol:

      Morgan et al. 1989 [1571] used RAST and RAST inhibition.

      DeWitt et al. (2004) [1536] used immunoCAP with IgE inhibition.

    • Number of Patients:

      Morgan et al. 1989 [1571] tested sera from 31 shrimp allergic patients and 13 atopic shrimp tolerant controls.

      DeWitt et al. (2004) [1536] tested sera from 9 shrimp sensitive subjects. 

    • Summary of Results:

      Morgan et al. 1989 [1571] reported that 16/31 patients had positive RAST to both brown and white shrimp, one was only positive to white shrimp and 2 only to brown shrimp extract. None of the sera from SPT negative patients gave a positive RAST. RAST Inhibition studies of 7 sera with high RASTs showed that 2 showed qualitatively different allergens between white and brown shrimp.

      DeWitt et al. (2004) [1536] also showed specific IgE binding to recombinant Pen a 1 and seven invertebrate extracts. 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. The natural and recombinant shrimp tropomyosin show similar binding despite the different species.

    Immunoblotting

    • Immunoblotting separation:

      Daul et al (1994) [1563] separated proteins in an SDS-PAGE gel with 15% total acrylamide and 2.7% cross-linker. The stacking gel was 4% acrylamide. Samples were boiled in 2% SDS and 1% 2-mercaptoethanol.

      Reese et al. (1996) [1560] separated proteins in an SDS-PAGE gel with 17.5% total acrylamide and 2.5% cross-linker. The stacking gel was 5% acrylamide.

    • Immunoblotting detection method:

      Daul et al (1994) [1563] transferred proteins onto nitrocellulose membranes (0.2 µm, BA-83, Scheicher and Schull, Dassel, Germany) using a Mini Transblot tank (BioRad). Membranes were washed with PBS, blocked with PBS containing 10% fetal calf serum and 1% bovine serum albumin, washed again with PBS containing 0.02% (v/v) Tween 20 and cut into strips. Strips were incubated overnight with sera diluted 1:2 with PBS, washed 3 times with PBS-Tween and incubated with 125I-labelled goat anti-human IgE. Strips were washed in PBS and autoradiograpged for 24-96 hours at -70°C.

      Reese et al. (1996) [1560] used a different method of detection with alkaline phosphatase-labelled monoclonal anti-human IgE in combination with the chemiluminescent substrate CSPD (Tropix).

    • Immunoblotting results:

      Musmand et al (1993) [1707] report that IgE from sera from 13 shrimp allergic patients bound to a total of 9 bands. However, IgE from 12/13 sera bound to a band at 36-Kda.

      Daul et al (1994) [1563] report that a 36-kDa allergen, named Pen a 1, reacted with 28/34 (82%) sera from shrimp-sensitive, skin test and RAST-positive, individuals. The allergen was isolated and a 21 amino acid internal peptide was sequenced which showed homology with tropomyosin.

      Reese et al. (1996) [1560] report that cyanogen bromide and protease (Lys-C, Glu-C, trypsin, Arg-C and chymotrypsin) cleaved purified Pen a 1 bound IgE (and monoclonal antibodies). However, IgE was not bound by all the peptides. The IgE binding pattern was different from that of all the monoclonal antibodies. They suggest that IgE binding to Pen a 1 was localized on a limited part of the sequence.

      Reese et al. (1997) [1577] showed that natural and recombinant Pen a 1 (4 clones) showed similar IgE binding to a pool of human sera. Four IgE reactive peptides, three of 13 and one of 21 amino acids, were sequenced. All were from the C-terminal region of tropomyosin and one overlapped the sequence identified by Shanti et al. (1993) [1576] from Indian prawn.

    Oral provocation

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

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

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

    • Blind:Not described for Farfantepenaeus aztecus.
    • Number of Patients:Not described for Farfantepenaeus aztecus.
    • Dose response:Not described for Farfantepenaeus aztecus.
    • Symptoms:Not described for Farfantepenaeus aztecus.

    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.

    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.

    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. 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 (5)

    • Lehrer SB, Ayuso R, Reese G.
      Seafood allergy and allergens: a review.
      Mar Biotechnol (NY). 5(4):339-348.. 2003
      PUBMEDID: 14719162
    • 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
    • Wild LG, Lehrer SB.
      Fish and shellfish allergy.
      Curr Allergy Asthma Rep. 5(1):74-79.. 2005
      PUBMEDID: 15659268
    • 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 a 1

    • Allergen Name:Pen a 1
    • Alternatve Allergen Names:Tropomyosin
    • Allergen Designation:Major
    • Protein Family:Pfam PF00261; Tropomyosin family
    • Sequence Known?:Yes
    • Allergen accession No.s:http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&val=73532979
    • 3D Structure Accession No.:Not available
    • Calculated Masses:

      32718.29 or 31572.85 Da (after removing a methionine from one of two possible starts of translation) 

    • Experimental Masses:34 - 38 kDa (by SDS-PAGE). Tropomyosins run near 50 kDa with 6M urea.
    • Oligomeric Masses:

      Tropomyosins form dimers.

    • Allergen epitopes: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. 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.
    • 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:

      The nucleotide sequence of Pen a 1 shows 30 DNA substitutions compared to that of Met e 1, which only result in a single amino acid substitution (Reese et al, 1997 [1577]). 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:

      Daul et al (1994) [1563] purified Pen a 1 from brown shrimp by SDS-PAGE.

      De Witt et al. (2004) [1536] expressed recombinant Pen a 1 in E. coli. Hexahistidine-tagged rPen a 1 was purified by immobilized-metal affinity chromatography (IMAC), using nickel charged chelating Sepharose HP packed in a XK50/20 column (Amersham Biosciences) and size exclusion chromatography (SEC), using a Superdex 200 XK50/100 column (Amersham Biosciences).

      De Witt et al. (2004) [1536] also purified native tropomyosin from finely chopped tail muscle of Pandalus borealis boiled for 10 min in 1 mL of distilled water per gram of tissue. After clarification by centrifugation and sequential passage through 1.2 µm and 0.45 µm mixed cellulose ester filters, the resulting extract was subjected to ultrafiltration using a PM-10 membrane (molecular mass cut-off: 10000 Da; Millipore). The retentate after ultrafiltration was applied to a Q Sepharose FF ion exchange column (Amersham Biosciences), equilibrated with 20 mM Tris-HCl, pH 8.0 and eluted with a linear 0–0.5 M NaCl gradient in the same buffer. Fractions containing strong 38 kDa band by SDS-PAGE were pooled for further purification by SEC as described above.

      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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