Utility of Component-Resolved Diagnostics in Food Allergy

Current Allergy and Asthma Reports

Volumn 15, Issue 6, 2015, Pages

  Tuano, Karen S ^a   Davis, Carla M ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

Component testing; Diagnosis; Food allergen; Food allergies; Oral food challenge

Indexed keywords

FOOD ALLERGEN; IMMUNOGLOBULIN E; ALLERGEN;

ALLERGIC REACTION; CLINICAL PRACTICE; COMPONENT RESOLVED DIAGNOSTIC TESTING; CROSS REACTION; DIAGNOSTIC ACCURACY; DIFFERENTIAL DIAGNOSIS; DISEASE SEVERITY; EGG ALLERGY; FOOD ALLERGY; FOOD COMPOSITION; GEOGRAPHIC PATHOLOGY; HAZELNUT; HEALTH CARE UTILIZATION; HUMAN; IMMUNOLOGICAL PROCEDURES; METHODOLOGY; MILK ALLERGY; PEANUT ALLERGY; PREDICTIVE VALUE; REVIEW; RISK ASSESSMENT; RISK FACTOR; SENSITIVITY AND SPECIFICITY; SHRIMP; SOYBEAN; ANIMAL; FOOD HYPERSENSITIVITY; HYPERSENSITIVITY; IMMUNOLOGY; POLLEN;

ALLERGENS; ANIMALS; FOOD HYPERSENSITIVITY; HUMANS; HYPERSENSITIVITY; IMMUNOGLOBULIN E; POLLEN;

EID: 84937421689     PISSN: 15297322     EISSN: 15346315     Source Type: Journal    
DOI: 10.1007/s11882-015-0534-0     Document Type: Review

References (71)

1. Sicherer SH, Sampson HA. Food allergy: epidemiology, pathogenesis, diagnosis, and treatment. J Allergy Clin Immunol. 2014;133:291–307.
2. Boyce JA, Assa’ad A, Burks AW, Jones SM, Sampson HA, Wood RA, et al. Guidelines for the diagnosis and management of food allergy in the United States: report of the NIAID-sponsored expert panel. J Allergy Clin Immunol. 2010;126:S1–58. These guidelines describe the current consensus in the United States for the diagnosis and management of food allergic disease and practical advice is contained in the guidelines.
3. Sicherer SH, Sampson HA. Food allergy. J Allergy Clin Immunol. 2010;125:S116–25.
4. Sampson HA. Utility of food-specific IgE concentrations in predicting symptomatic food allergy. J Allergy Clin Immunonol. 2001;107:891–6.
5. Roberts G, Lack G. Diagnosing peanut allergy with skin prick and specific IgE testing. J Allergy Clin Immunol. 2005;115:1291–6.
6. Shreffler WG. Microarrayed recombinant allergens for diagnostic testing. J Allergy Clin Immunol. 2011;127:843–9. This review describes the strengths and weaknesses of molecularly defined allergy testing and the microarray platform.
7. Hamilton RG. Clinical laboratory assessment of immediate-type hypersensitivity. J Allergy Clin Immunol. 2010;125:S284–96.
8. Canonica GW, Ansotegui IJ, Pawankar R, Schmid-Grendelmeier P, van Hage M, Baena-Cagnani, et al. A WAO–ARIA–GA2LEN consensus document on molecular-based allergy diagnostics. World Allergy Organ J. 2013;6:1–17. A WAO document that describes how molecular diagnostics can be interpreted and used for relevant information in the allergists office.
9. Amoah AS, Obeng BB, Larbi IA, Versteeg SA, Aryeetey Y, Akkerdaas JH, et al. Peanut-specific IgE antibodies in asymptomatic Ghanaian children possibly caused by carbohydrate determinant cross-reactivity. J Allergy Clin Immunol. 2013;132:639–47.
10. Suratannon N, Ngamphaiboon J, Wongpiyabovorn J, Puripokai P, Chatchatee P. Component-resolved diagnostics for the evaluation of peanut allergy in a low-prevalence area. Pediatr Allergy Immunol. 2013;24:665–70.
11. Hochwallner H, Schulmeister U, Swoboda I, Balic N, Geller B, Nystrand M, et al. Microarray and allergenic activity assessment of milk allergens. Clin Exp Allergy. 2010;40:1809–18.
12. Bernard H, Créminon C, Yvon M, Wal JM. Specificity of the human IgE response to the different purified caseins in allergy to cow’s milk proteins. Int Arch Allergy Immunol. 1999;115:235–44.
13. D’Urbano LE, Pellegrino K, Artesani MC, Donnanno S, Luciano R, Riccardi C, et al. Performance of a component-based allergen-microarray in the diagnosis of cow’s milk and hen’s egg allergy. Clin Exp Allergy. 2010;40:1561–70.
14. Sicherer SH, Sampson HA. Cow’s milk protein-specific IgE concentrations in two age groups of milk-allergic children and in children achieving clinical tolerance. Clin Exp Allergy. 1999;29:507–12.
15. Chatchatee P, Järvinen KM, Bardina L, Vila L, Beyer K, Sampson HA. Identification of IgE and IgG binding epitopes on beta- and kappa-casein in cow’s milk allergic patients. Clin Exp Allergy. 2001;31:1256–62.
16. Järvinen KM, Beyer K, Vila L, Chatchatee P, Busse PJ, Sampson HA. B-cell epitopes as a screening instrument for persistent cow’s milk allergy. J Allergy Clin Immunol. 2002;110:293–7.
17. García-Ara MC, Boyano-Martínez MT, Díaz-Pena JM, Martín-Muñoz MF, Martín-Esteban M. Cow’s milk-specific immunoglobulin E levels as predictors of clinical reactivity in the follow-up of the cow’s milk allergy infants. Clin Exp Allergy. 2004;34:866–70.
18. Ott H, Baron JM, Heise R, Ocklenburg C, Stanzel S, Merk HF, et al. Clinical usefulness of microarray-based IgE detection in children with suspected food allergy. Allergy. 2008;63:1521–8.
19. Fung I, Kim JS, Spergel JM. Relating microarray component testing and reported food allergy and food-triggered atopic dermatitis: a real-world analysis. Ann Allergy Asthma Immunol. 2013;110:173–177.e1.
20. Dang TD, Mills CE, Allen KJ. Determination of the clinical egg allergy phenotypes using component-resolved diagnostics. Pediatr Allergy Immunol 2014. A complete review of component resolved diagnostic testing in egg allergy.
21. Rona RJ, Keil T, Summers C, et al. The prevalence of food allergy: a meta-analysis. J Allergy Clin Immunol. 2007;120:638–46.
22. Osborne NJ, Koplin JJ, Martin PE, et al. Prevalence of challenge-proven IgE mediated food allergy using population based sampling and predetermined challenge criteria in infants. J Allergy Clin Immunol. 2011;127:668–76.e2.
23. Venter C, Pereira B, Voigt K, et al. Prevalence and cumulative incidence of food hypersensitivity in the first 3 years of life. Allergy. 2008;63:354–9.
24. Boyano-Martınez T, Garcıa-Ara C, Dıaz- Pena JM, Martın-Esteban M. Prediction of tolerance on the basis of quantification of egg white-specific IgE antibodies in children with egg allergy. J Allergy Clin Immunol. 2002;110:304–9.
25. Wood RA. The natural history of food allergy. Pediatrics. 2003;111:1631–7.
26. Everberg H, Brostedt P, Oman H, Bohman S, Moverare R. Affinity purification of egg white allergens for improved component resolved diagnostics. Int Arch Allergy Immunol. 2011;154:33–41.
27. Cooke SK, Sampson HA. Allergenic properties of ovomucoid in man. J Immunol. 1997;159:2026–32.
28. Holen E, Elsayed S. Characterization of four major allergens of hen egg-white by IEF/SDS-PAGE combined with electrophoretic transfer and IgE-immunoautoradiography. Int Arch Allergy Immunol. 1990;91:136–41.
29. Lemon-Mule H, Sampson HA, Sicherer SH, Shreffler WG, Noone S, Nowak-Wegrzyn A. Immunologic changes in children with egg allergy ingesting extensively heated egg. J Allergy Clin Immunol. 2008;122:977–83.e1.
30. Bartnikas LM, Sheehan WJ, Larabee KS, Petty C, Schneider LC, Phipatanakul W. Ovomucoid is not superior to egg white testing in predicting tolerance to baked egg. J Allergy Clin Immunol. 2013;1:354–60.e2.
31. Ando H, Moverare R, Kondo Y, et al. Utility of ovomucoid-specific IgE concentrations in predicting symptomatic egg allergy. J Allergy Clin Immunol. 2008;122:583–8.
32. Haneda Y, Kando N, Yasui M, et al. Ovomucoids IgE is a better marker than egg white-specific IgE to diagnose boiled egg allergy. J Allergy Clin Immunol. 2012;129:1681–2.
33. Sicherer SH, Wood RA. Advances in diagnosing peanut allergy. J Allergy Clin Immunol: Pract. 2013;1:1–13. A practical guide in diagnosing peanut allergy in the office.
34. Arbes SJ Ur, Gergen PJ, Elliott L, Zeldin DC. Prevalence of positive skin test responses to 10 common allergens in the US population: results from the third National Health and Nutrition Examination Survey.
35. Liu AH, Jaramillo R, Sicherer SH, Wood RA, Bock SA, Burks AW, et al. National prevalence and risk factors for food allergy and relationship to asthma: results from the National Health and Nutrition Examination Survey 2005–2006. J Allergy Clin Immunol. 2010;126:798–806.
36. Nicolaou N, Poorafshar M, Murray C, Simpson A, Winell H, Kerry G, et al. Allergy or tolerance in children sensitized to peanut: prevalence and differentiation using component-resolved diagnostics. J Allergy Clin Immunol. 2010;125:191–7.
37. Nicolaou N, Murray C, Belgrave D, Poporafshar M, Simpson A, Custovic A. Quantification of specific IgE to whole peanut extract and peanut components in prediction of peanut allergy. J Allergy Clin Immunol. 2011;127:684–5.
38. Dang TC, Tang M, Choo S, Licciardi PV, Koplin JJ, Martin PE, et al. Increasing the accuracy of peanut allergy diagnosis by using Ara h 2. J Allergy Clin Immunol. 2012;129:1056–63.
39. Lieberman JA, Glaumann S, Batelson S, Borres MP, Sampson HA, Nilsson C. The utility of peanut components in the diagnosis of IgE-mediated peanut allergy among distinct populations. J Allergy Clin Immunol: Pract. 2013;1:75–82. This study gives a stepwise approach to testing may provide clinicians with a way to minimize the need for peanut challenges.
40. Beyer K, Grabenhenrich L, Beder A, Kalb B, Ziegert M, Finger A, et al. Predictive values of component-specific IgE for the outcome of peanut and hazelnut food challenges in children. Allergy. 2015;70:90–8. This is the first study to determine receiver operating characteristic curves predicting positive challenge outcome for peanut (Ara h 1,2,3 and 8) and hazelnut (Cor a 1,8,9,and 14).
41. Klemans RJB, Liu X, Knulst AC, Knol MJ, Gmelig-Meyling F, Borst E, et al. IgE binding to peanut components by four different techniques: Ara h 2 is the most relevant in peanut allergic children and adults. Clin Exp Allergy. 2013;43:967–74.
42. Keet CA, Johnson K, Savage JH, Hamilton RG, Wood RA. Evaluation of Ara h 2 IgE thresholds in the diagnosis of peanut allergy in a clinical population. J Allergy Clin Immunol Pract. 2013;1:101–3.
43. Klemans RJ, van Os-Medendorp H, Blankestijn M, Bruijnzeel-Koomen CA, Knol EF, Knulst AC. Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review. Clin Exp Allergy. 2014. A systematic review summarizing recent literature to assess the diagnostic value of sIgE to peanut components in diagnosing peanut allergy.
44. Ebisawa M, Movérare R, Sato S, Maruyama N, Borres MP, Komata T. Measurement of Ara h 1-, 2-, and 3-specific IgE antibodies is useful in diagnosis of peanut allergy in Japanese children. Pediatr Allergy Immunol. 2012;23:573–81.
45. Eller E, Bindslev-Jensen C. Clinical value of component-resolved diagnostics in peanut-allergic patients. Allergy. 2013;68:190–4.
46. Glaumann S, Nopp A, Johansson SG, Rudengren M, Borres MP, Nilsson C. Basophil allergen threshold sensitivity, CD-sens, IgE-sensitization and DBPCFC in peanut-sensitized children. Allergy. 2012;67:242–7.
47. Bernard H, Paty E, Mondoulet L, Burks AW, Bannon GA, Wal JM, et al. Serological characteristics of peanut allergy in children. Allergy. 2003;58:1285–92.
48. de Oliveira LC L, Aderhold M, Brill M, Schulz G, Rolinck-Werninghaus C, Clare Mills EN, et al. The value of specific IgE to peanut and its component Ara h 2 in the diagnosis of peanut allergy. J Allergy Clin Immunol Pract. 2013;1:394–8.
49. Asarnoj A, Nilsson C, Lidholm J, Glaumann S, Ostblom E, Hedlin G, et al. Peanut component Ara h8 sensitization and tolerance to peanut. J Allergy Clin Immunol. 2012;130:468–72.
50. Ebo DG, Bridts CH, Verweij MM, De Knop KJ, Hagendorens MM, De Clerck LS, et al. Sensitization profiles in birch pollen-allergic patients with and without oral allergy syndrome to apple: lessons from multiplexed component-resolved allergy diagnosis. Clin Exp Allergy. 2010;6:339–47.
51. Nicolaou N, Custovic A. Molecular diagnosis of peanut and legume allergy. Curr Opin Allergy Clin Immunol. 2011;6:222–8.
52. Glaumann S, Nopp A, Johansson SG, Rudengren M, Borres MP, Nilsson C. Basophil allergen threshold sensitivity, CD-sens, IgE-sensitization and DBPCFC in peanut-sensitized children. Allergy. 2012;6:242–7.
53. Sastre J. Molecular diagnosis in allergy. Clin Exp Allergy. 2010;6:1442–60.
54. Movérare R, Ahlstedt S, Bengtsson U, Borres MP, van Hage M, Poorafshar M, et al. Evaluation of IgE antibodies to recombinant peanut allergens in patients with reported reactions to peanut. Int Arch Allergy Immunol. 2011;156:282–90.
55. Tolkki L, Alanko K, Petman L, Skydtsgaard MB, Milvang PG, Seppälä U, et al. Clinical characterization and IgE profiling of birch (Betula verrucosa)-allergic individuals suffering from allergic reactions to raw fruits and vegetables. J Allergy Clin Immunol Pract. 2013;1:623–31.
56. De Knop KJ, Verweij MM, Grimmelikhuijsen M, Philipse E, Hagendorens MM, Bridts C, et al. Age-related sensitization profiles for hazelnut (Corylus avellana) in a birch-endemic region. Pediatr Allergy Immunol. 2011;22:e139–49.
57. Masthoff LJN, Mattsson L, Zuidmeer-Jongejan L, Lidholm J, Andersson K, Akkerdaas JH, et al. Sensitization to Cor a 9 and Cor a 14 is highly specific for hazelnut allergy with objective symptoms in Dutch children and adults. J Allergy Clin Immunol. 2013;132:393–9.
58. Hansen KS, Ballmer-Weber BK, Sastre J, Lidholm J, Andersson K, Oberhofer H, et al. Component-resolved in vitro diagnosis of hazelnut allergy in Europe. J Allergy Clin Immunol. 2009;123:1134–41.
59. Kattan JD, Sicherer SH, Sampson HA. Clinical reactivity to hazelnut may be better identified by component testing than traditional testing methods. J Allergy Clin Immunol Pract. 2014;2:633–4.
60. Faber MA, De Graag M, Van Der Heijden C, Sabato V, Hagendorens MM, Bridts CH, et al. Cor a 14: missing link in the molecular diagnosis of hazelnut allergy? Int Arch Allergy Immunol. 2014;164:200–6.
61. Masthoff LJ, Pasmans SG, van Hoffen E, Knol MJ, Bruijnzeel-Koomen CA, Flinterman AE, et al. Diagnostic value of hazelnut allergy tests including rCor a 1 spiking in double-blind challenged children. Allergy. 2012;67:521–7.
62. Leung NYH, Wai CYY, Shu S, Wang J, Kenny TP, Chu KH, et al. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review. Clinic Rev Allerg Immunol. 2014;46:180–97. A review of the molecular identification of seafood allergens, allergenic epitopes, cross reactivity and factors affecting allergenicity of seafood.
63. 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.
64. 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.
65. Gamez C, Sanchez-Garcia S, Ibanez MD, Lopez R, Aguado E, Lopez E, et al. Tropomyosin IgE-positive results are a good predictor of shrimp allergy. Allergy. 2011;66:1375–83.
66. Yang AC, Arruda K, Santos ABR, Barbosa MCR, Chapman MD, Galvao CES, 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.
67. Holzhauser T, Wackermann O, Ballmer-Weber BK, Bindslev-Jensen C, Scibilia J, Perono-Garoffo L, et al. Soybean (Glycine max) allergy in Europe: Gly m 5 (B-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. J Allergy Clin Immunol. 2009;123:452–8.
68. Ito K, Sjolander S, Sato S, Moverare R, Tanaka A, Soderstrom L, et. al. IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children.
69. Vissers YM, Jansen APH, Ruinemans-Koerts, Wichers HJ, Savelkoul HFJ. IgE component-resolved allergen profile and clinical symptoms in soy and peanut allergic patients. Allergy. 2011;66:1125–6.
70. Berneder M, Bublin M, Hoffman-Sommergruber K, Hawranek T, Lang R. Allergen chip diagnosis for soy-allergic patients: Gly m 4 as a marker for severe food-allergic reactions to soy. Int Arch Allergy Immunol. 2013;161:229–33.
71. Kosma P, Sjolander S, Landgren E, Borres MP, Hedlin G. Severe reactions after the intake of soy drink in birch pollen-allergic children sensitized to Gly m 4. Acta Paediatr. 2011;6:305–6.