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.

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.

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.

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).

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

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

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. 

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.

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.

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).

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 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]).