As patients almost always react to shrimps, crawfish, lobsters and crabs, there are no reports of reactions specifically after eating lobsters. Halmepuro et al (1987) [1802] describe the 23 patients who donated sera as having analphylactic, gasterointestinal or respiratory reactions to crustacea.
Skin Prick Test
Number of Studies:
1-5
Food/Type of allergen:
Halmepuro et al. (1987) [1802] made extracts from crawfish (Procambarus clarkii), spiny Lobster (panuliris argus), white shrimp (Litopenaeus setiferus) and blue crab (Callinectes sapidus) which were boiled for 15 minutes, peeled and homogenized in approximately 2 ml/g of phosphate buffered saline, pH 7.2 (PBS). After mixing overnight at 4°C, the extract was centrifuged at 16000 x g for 30 minutes at 4°C. Supernatants were concentated by ultrafiltration with an Amicon YM2 (cut-off 2 kda) and exhausively dialysed against PBS with a 3.5 kDa membrane. The extract was centrifuged at 66000 x g for 30 minutes at 4°C and the supernatant aliquoted and stored at -20°C. A maximum of 10 mg/ml extract was used.
Protocol:
(controls, definition of positive etc)
Halmepuro et al. (1987) [1802] defined a positive SPT as giving a wheal of 2 mm greater diameter than the negative control.
Number of Patients:
Halmepuro et al (1987) [1802] reported testing 23 patients.
Summary of Results:
Halmepuro et al (1987) [1802] reported that all 23 patients gave a positive skin prick with lobster and crawfish.
IgE assay (by RAST, CAP etc)
Number of Studies:
1-5
Food/Type of allergen:
Halmepuro et al. (1987) [1802] made extracts from crawfish (Procambarus clarkii), spiny Lobster (panuliris argus), white shrimp (Litopenaeus setiferus) and blue crab (Callinectes sapidus) which were boiled for 15 minutes, peeled and homogenized in approximately 2 ml/g of phosphate buffered saline, pH 7.2 (PBS). After mixing overnight at 4°C, the extract was centrifuged at 16000 x g for 30 minutes at 4°C. Supernatants were concentated by ultrafiltration with an Amicon YM2 (cut-off 2 kda) and exhausively dialysed against PBS with a 3.5 kDa membrane. The extract was centrifuged at 66000 x g for 30 minutes at 4°C and the supernatant aliquoted and stored at -20°C. Lehrer & McCants (1987) [1575] made similar extracts including oyster with the a final centrifugation at 78000 x g.
IgE protocol:
Halmepuro et al. (1987) [1802] used RAST and crossed-immune electrophoresis (CRIE).
Lehrer & McCants (1987) [1575] used RAST and RAST inhibition.
Leung et al. (1996) [1557] and Leung et al (1998) [1555] used immunoblotting.
Leung et al. (1996) [1557] used sera from 9 shrimp allergic subjects.
Leung et al (1998) [1555] used sera from 10 crustacea allergic subjects.
Summary of Results:
Halmepuro et al. (1987) [1802] reported that all 23 sera were positive by RAST (>18% of added radioactivity) with lobster and crawfish. CRIE suggested that the allergens of shrimp, crawfish and lobster were similar.
Lehrer & McCants (1987) [1575] reported a strong correlation between RAST results for oyster and crustacea (0.82 for lobster). Raw and cooked oyster were inhibited to 85% and 89% by lobster extract (see oyster for further information).
Immunoblotting
Immunoblotting separation:
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 (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. (1996) [1557] reported that 9/9 sera from shrimp allergic patients bound to an allergen from Panuliris homarus at 38 kDa (see greasybacked shrimp entry).
Leung et al (1998) [1555] reported that the recombinant Hom a 1, rPan s 1 and rMet e 1 ran as 60 kDa GST-fusion proteins and bound IgE from sera from 10 crustacea allergic subjects.
Oral provocation
Number of Studies:
0
Food used and oral provocation
vehicle
Blind?
Number of Patients?
Dose response
Symptoms
No challenges with lobster reported
IgE cross-reactivity and Polysensitisation
Leung et al. (1996) [1557], Leung et al (1998) [1555], Leung et al (1998) [1554] and DeWitt et al. (2004) [1536] report details of the similar tropomyosin allergens from shrimps, lobsters and crabs together with IgE cross-reactivity between both extracts and recombinant allergens. Several molluscs are also shown to have cross-reactive tropomyosins.
Halmepuro et al. (1987) [1802] had earlier reported IgE cross-reactivity between extracts from crustacea and Lehrer & McCants (1987) [1575] extended this to oysters.
Other Clinical information
Binder et al (2001) [1588] reported that immunoblots of an extract of lobster (H. gammarus) show IgE binding near 40 kDa using sera of individuals allergic to the indianmeal moth. This was inhibited by preincubation of the sera with recombinant indianmeal moth arginine kinase. Thus arginine kinase may also be a lobster allergen.
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]). Nephrops is relatively closely related to Homarus which may produce similar allergens. Contact determatis has also been reported (Aasmoe et al, 2005 [1766]; Scharer et al, 2002 [1612]).
Reviews (3)
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
PUBMED ID:
16261809
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
PUBMED ID:
15725289
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
PUBMED ID:
15891527
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
PUBMED ID:
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
PUBMED ID:
3734286
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
PUBMED ID:
7499677
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
PUBMED ID:
15672477
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
PUBMED ID:
11422159
Halmepuro L, Salvaggio JE, Lehrer SB.
Crawfish and lobster allergens: identification and structural similarities with other crustacea. Int Arch Allergy Appl Immunol. 1987;84(2):165-172. 1987
PUBMED ID:
3654002
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
PUBMED ID:
9597774
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
PUBMED ID:
8939159
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
PUBMED ID:
12000333
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