Molecular diagnosis of shrimp allergy: Efficiency of several allergens to predict clinical reactivity

Journal of Allergy and Clinical Immunology: In Practice

Volumn 3, Issue 4, 2015, Pages 521-529.e10

  Pascal, Mariona ^a,b   Grishina, Galina ^a   Yang, Ariana C ^c   Sánchez García, Silvia ^d,e   Lin, Jing ^a   Towle, David ^f   Ibañez, Maria Dolores ^d   Sastre, Joaquín ^e   Sampson, Hugh A ^a   Ayuso, Rosalia ^a,g  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF BARCELONA   (Spain)

^c UNIVERSITY OF SÃO PAULO   (Brazil)

^d HOSPITAL INFANTIL UNIVERSITARIO NIÑO JESÚS   (Spain)

^e Hospital UniversitarioFundación Jiménez Díaz   (Spain)

^f MOUNT DESERT ISLAND BIOLOGICAL LABORATORY   (United States)

^g Ear Nose and Throat Associates of New York PC   (United States)

Author keywords

Arginine kinase; Component resolved diagnosis; DBPCFC; Epitope; Fatty acid binding protein; Hemocyanin; Microarray; Myosin light chain; Sarcoplasmic calcium binding protein; Shellfish allergy; Tropomyosin; Troponin C

Indexed keywords

ALLERGEN; ARGININE KINASE; CALCIUM BINDING PROTEIN; EPITOPE; HEMOCYANIN; HOUSE DUST ALLERGEN; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G4; MYOSIN LIGHT CHAIN; SARCOPLASMIC CALCIUM BINDING PROTEIN; TROPOMYOSIN; UNCLASSIFIED DRUG; ARTHROPOD PROTEIN; IMMUNOGLOBULIN G; RECOMBINANT PROTEIN;

ADOLESCENT; ADULT; ANAPHYLAXIS; ANTIGEN DETECTION; ARTICLE; CHILD; CONTROLLED STUDY; FEMALE; FOOD ALLERGY; HOUSE DUST ALLERGY; HUMAN; IMMUNOREACTIVITY; MAJOR CLINICAL STUDY; MALE; PREDICTION; PRICK TEST; SHRIMP; SKIN TEST; ANIMAL; BLOOD; CONTROLLED CLINICAL TRIAL; FOOD HYPERSENSITIVITY; IMMUNOLOGY; PENAEIDAE; SHELLFISH;

ALLERGENS; ANIMALS; ARGININE KINASE; ARTHROPOD PROTEINS; CALCIUM-BINDING PROTEINS; EPITOPES; FOOD HYPERSENSITIVITY; HEMOCYANIN; HUMANS; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; PENAEIDAE; RECOMBINANT PROTEINS; SHELLFISH; SKIN TESTS; TROPOMYOSIN;

EID: 84943275667     PISSN: 22132198     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jaip.2015.02.001     Document Type: Article

References (48)

1. Pedrosa M, Boyano-Martínez T, García-Ara C, Quirce S. Shellfish allergy: a comprehensive review. Clin Rev Allergy Immunol May 29, 2014.
2. Leung NY, Wai C, Shangan S, Wang J, Kenny TP, Chu KH, et al. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review. Clin Rev Allergy Immunol 2014;46:180-97.
3. Sicherer SH. Epidemiology of food allergy. J Allergy Clin Immunol 2011;127:594-602.
4. Nwaru BI, Hickstein L, Panesar SS, Roberts G, Muraro A, Sheikh A. EAACI Food Allergy and Anaphylaxis Guidelines Group. Prevalence of common food allergies in Europe: a systematic review and meta-analysis. Allergy 2014;69:992-1007.
5. Clark S, Espinola J, Rudder SA, Banerji A, Camargo CA. Frequency of US emergency department visits for food-related acute allergic reactions. J Allergy Clin Immunol 2011;127(3):682-3.
6. Lieberman JA, Sicherer SH. Diagnosis of food allergy: epicutaneous skin tests, in vitro tests, and oral food challenge. Curr Allergy Asthma Rep 2011;11:58-64.
7. Lin J, Sampson HA. The role of immunoglobulin E-binding epitopes in the characterization of food allergy. Curr Opin Allergy Clin Immunol 2009;9:357-63.
8. Sastre J. Molecular diagnosis in allergy. Clin Exp Allergy 2010;40:1442-60.
9. Shanti KN, Martin BM, Nagpal S, Metcalfe DD, Rao PV. Identification of tropomyosin as the major shrimp allergen and characterization of its IgEbinding epitopes. J Immunol 1993;151:5354-63.
10. Yu CJ, Lin YF, Chiang BL, Chow LP. Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. J Immunol 2003;170:445-53.
11. García-Orozco KD, Aispuro-Herández E, Yepiz-Plascencia G, Calderón-de-la-Barca AM, Sotelo-Mundo RR. Molecular characterization of arginine kinase, an allergen from the shrimp Litopenaeus vannamei. Int Arch Allergy Immunol 2007;144:23-8.
12. Shen Y, Cao MJ, Cai QF, Su WJ, Yu HL, Ruan WW, et al. Purification, cloning, expression and immunological analysis of Scylla serrate arginine kinase, the crab allergen. J Sci Food Agric 2011;91:1326-35.
13. Ayuso R, Grishina G, Bardina L, Carrillo T, Blanco C, Ibañez MD, et al. Myosin light chain is a novel shrimp allergen, Lit v 3. J Allergy Clin Immunol 2008;122:795-802.
14. Shiomi K, Sato Y, Hamamoto S, Mita H, Shimakura K. Sarcoplasmic calciumbinding protein: identification as a new allergen of the black tiger shrimp Penaeus monodon. Int Arch Allergy Immunol 2008;146:91-8.
15. Ayuso R, Grishina G, Ibáñez MD, Blanco C, Carrillo T, Bencharitiwong R, et al. Sarcoplasmic calcium-binding protein is an EF-hand-type protein identified as a new shrimp allergen. J Allergy Clin Immunol 2009;124:114-20.
16. Piboonpocanun S, Jirapongsananuruk O, Tipayanon T, Boonchoo S, Goodman RE. Identification of hemocyanin as a novel non-crossreactive allergen from the giant freshwater shrimp Macrobrachium rosenbergii. Mol Nutr Food Res 2011;55:1492-8.
17. Ayuso R, Grishina G, Pascal M, Sanchez-Garcia S, Towle D, Smith C, et al. Hemocyanin, troponin C and fatty acid-binding protein (FABP) may be crossreactive allergens between crustaceans, cockroach and dust mites. J Allergy Clin Immunol 2011;127(Suppl):AB235.
18. Giuffrida MG, Villalta D, Mistrello G, Amato S, Asero R. Shrimp allergy beyond tropomyosin in Italy: clinical relevance of arginine kinase, sarcoplasmic calcium binding protein and hemocyanin. Eur Ann Allergy Clin Immunol 2014;46:172-7.
19. Bauermeister K, Wangorsch A, Garoffo LP, Reuter A, Conti A, Taylor SL, et al. Generation of a comprehensive panel of crustacean allergens from the North Sea shrimp Crangon crangon. Mol Immunol 2011;48:1983-92.
20. Gamez C, Paz-Zafra M, Boquete M, Sanz V, Mazzeo C, Ibánez MD, et al. New shrimp IgE binding proteins involved in mite-seafood cross-reactivity. Mol Nutr Food Res 2014;58:1915-25.
21. Yang AC, Arruda LK, Santos AB, Barbosa MC, Chapman MD, Galvão CE, et al. Measurement of IgE antibodies to shrimp tropomyosin is superior to skin prick testing with commercial extract and measurement of IgE to shrimp for predicting clinically relevant allergic reactions after shrimp ingestion. J Allergy Clin Immunol 2010;125:872-8.
22. Gámez C, Sánchez-García S, Ibáñez MD, López R, Aguado E, López E, et al. Tropomyosin IgE-positive results are a good predictor of shrimp allergy. Allergy 2011;66(10):1375-83.
23. 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 1996;98:954-61.
24. Ayuso R, Reese G, Leong-Kee S, Plante M, Lehrer SB. Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins. Int Arch Allergy Immunol 2002;129:38-48.
25. Fernandez-Caldas E, Puerta L, Caraballo L, Lockey RF. Mite allergens. Clin Allergy Immunol 2008;21:161-82.
26. Binder M, Mahler V, Hayek B, Sperr WR, Schöller M, Prozell S, et al. Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate panallergen. J Immunol 2001;167:5470-7.
27. Asero R, Mistrello G, Amato S, Ariano R, Colombo G, Conte ME, et al. Shrimp allergy in Italian adults: a multicenter study showing a high prevalence of sensitivity to novel highmolecular weight allergens. IntArchAllergy Immunol 2012;157:3-10.
28. Villalta D, Tonutti E, Visentini D, Bizzaro N, Roncarolo D, Amato S, et al. Detection of a novel 20 kDa shrimp allergen showing cross-reactivity to house dust mites. Eur Ann Allergy Clin Immunol 2010;42:20-4.
29. Ayuso R, Sánchez-Garcia S, Lin J, Fu Z, Ibáñez MD, Carrillo T, et al. Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimpsensitization decreaseswith age. J AllergyClin Immunol 2010;125:1286-93.
30. Ayuso R, Sánchez-Garcia S, Pascal M, Lin J, Grishina G, Fu Z, et al. Is epitope recognition of shrimp allergens useful to predict clinical reactivity? Clin Exp Allergy 2012;42:293-304.
31. EAACI Subcommittee on Skin Tests. Allergen standardization and skin tests. Allergy 1993;48:48-82.
32. Lin J, Bruni FM, Fu Z, Malone J, Bardina L, Boner A, et al. A bioinformatics approach to identify patients with symptomatic peanut allergy using peptide microarray immunoassay. J Allergy Clin Immunol 2012;129:1321-8.
33. Ji H, Wong WH. TileMap: create chromosomal map of tiling array hybridizations. Bioinformatics 2005;21:3629-36.
34. Arima S, Lin J, Pecora V, Tardella LA. Bayesian hierarchical model for identifying epitopes in peptide microarray data. Biostatistics 2012;13:101-12.
35. Guyatt G, Rennie D, Meade MO, Cook DJ. Users' Guides to the Medical Literature: A Manual for Evidence-Based Clinical Practice, 2nd ed. New York, NY, USA: McGraw-Hill Education; 2008.
36. 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 2003;33:956-61.
37. Wang J, Calatroni A, Visness CM, Sampson HA. Correlation of specific IgE to shrimp with cockroach and dust mite exposure and sensitization in an inner-city population. J Allergy Clin Immunol 2011;128:834-7.
38. Fernandez-Rivas M, Bolhaar S, Gonzalez-Mancebo E, Asero R, van Leeuwen A, Bohle B, et al. Apple allergy across Europe: how allergen sensitization profiles determine the clinical expression of allergies to plant foods. J Allergy Clin Immunol 2006;118:481-8.
39. Santos AB, Rocha GM, Oliver C, Ferriani VP, Lima RC, Palma MS, et al. Crossreactive IgE antibody responses to tropomyosins from Ascaris lumbricoides and cockroach. J Allergy Clin Immunol 2008;121:1040-6.
40. Valenta R, Vrtala S, Laffer S, Spitzauer S, Kraft D. Recombinant allergens. Allergy 1998;53:552-61.
41. Reese G, Schicktanz S, Lauer I, Randow S, Lüttkopf D, Vogel L, et al. Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of brown shrimp, Penaeus aztecus. Clin Exp Allergy 2006;36:517-24.
42. Mita H, Koketsu A, Ishizaki S, Shiomi K. Molecular cloning and functional expression of allergenic sarcoplasmic calcium-binding proteins from Penaeus shrimps. J Sci Food Agric 2013;93:1737-42.
43. Jirapongsananuruk O, Sripramong C, Pacharn P, Udompunturak S, Chinratanapisit S, Piboonpocanun S, et al. Specific allergy to Peneaeus monodon (seawater shrimp) or Macrobrachium rosenbergii (freshwater shrimp) in shrimp-allergic children. Clin Exp Allergy 2008;38:1038-47.
44. Wang J, Lin J, Bardina L, Goldis M, Nowak-Wegrzyn A, Shreffler WG, et al. Correlation of IgE/IgG4 milk epitopes and affinity of milk-specific IgE antibodies with different phenotypes of clinical milk allergy. J Allergy Clin Immunol 2010;125:695-702.
45. Flinterman AE, Knol EF, Lencer DA, Bardina L, den Hartog Jager CF, Lin J, et al. Peanut epitopes for IgE and IgG4 in peanut-sensitized children in relation to severity of peanut allergy. J Allergy Clin Immunol 2008;121:737-43.
46. Platts-Mills TA, Vaughan JW, Blumenthal K, Pollart Squillace S, Sporik RB. Serum IgG and IgG4 antibodies to Fel d 1 among children exposed to 20 microg Fel d 1 at home: relevance of a nonallergic modified Th2 response. Int Arch Allergy Immunol 2001;124:126-9.
47. Hussain R, Poindexter RW, Ottesen EA. Control of allergic reactivity in human filariasis. Predominant localization of blocking antibody to the IgG4 subclass. J Immunol 1992;148:2731-7.
48. Van Neerven RJ, Knol EF, Ejrnaes A, Wurtzen PA. IgE-mediated allergen presentation and blocking antibodies: regulation of T-cell activation in allergy. Int Arch Allergy Immunol 2006;141:119-29.