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Component testing for pollen-related, plant-derived food allergies

Author
Julie Wang, MD
Section Editor
Scott H Sicherer, MD, FAAAAI
Deputy Editor
Elizabeth TePas, MD, MS

INTRODUCTION

Advances in the identification of clinically relevant allergens and the development of recombinant proteins allow for assessment of immunoglobulin E (IgE) binding to individual proteins within an allergenic food. This type of testing is known as component-resolved diagnosis (CRD). Increased sensitivity and specificity can be achieved by assessing IgE binding to separate proteins, either purified native or recombinant, thereby providing improved diagnostic accuracy for predicting clinical reactivity. CRD may also provide additional prognostic information regarding the severity or persistence of food allergies.

CRD testing for pollen-related, plant-derived food allergies is reviewed here. Component testing for animal-derived food allergies is discussed separately. An overview of testing for food allergies is also presented separately. (See "Component testing for animal-derived food allergies" and "Diagnostic evaluation of food allergy".)

OVERVIEW

Allergies to plant-derived foods may occur in pollen-sensitized individuals due to pollen allergens that cross-react with food allergens, such as profilins or pathogenesis-related class 10 (PR-10) proteins that are homologues of the major white birch pollen antigen (Betula verrucosa 1 [Bet v 1]). This type of allergy is associated with symptoms that are generally limited to the oropharyngeal area (oral allergy syndrome/pollen-food allergy syndrome). In the absence of sensitization to pollens, allergies to plant-derived foods are the result of sensitization to more stable proteins, such as the seed storage or lipid transfer proteins (LTPs). In these cases, reactions are more often systemic, and there is a higher risk for anaphylaxis [1]. (See "Pathogenesis of oral allergy syndrome (pollen-food allergy syndrome)" and "Clinical manifestations and diagnosis of oral allergy syndrome (pollen-food allergy syndrome)".)

Component-resolved diagnosis (CRD) entails measurement of specific immunoglobulin E (IgE) responses to individual allergens as opposed to measuring IgE responses to allergen extracts that contain a mixture of proteins, including ones that may have greater or less clinical relevance. The pattern of specific IgE reactivity to defined allergens can help determine which patients are at higher risk for allergic reactions versus those who are sensitized but clinically tolerant. It may also help distinguish between those who are at risk for more severe reactions versus those or who are likely to have milder symptoms.

The prime example of the utility of CRD in the management of food allergy is peanut allergy [2]. Several studies have noted that having detectable levels of specific IgE to the seed storage proteins are associated with more severe, persistent peanut allergy [3-7], whereas exclusive sensitization to a Bet v 1 homologue is more often associated with a low risk of reactivity to peanut [8,9]. (See "Peanut, tree nut, and seed allergy: Diagnosis" and 'Peanut' below.)

          

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Literature review current through: Jun 2017. | This topic last updated: Nov 23, 2015.
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References
Top
  1. Pastorello EA, Robino AM. Clinical role of lipid transfer proteins in food allergy. Mol Nutr Food Res 2004; 48:356.
  2. Sampson HA, Aceves S, Bock SA, et al. Food allergy: a practice parameter update-2014. J Allergy Clin Immunol 2014; 134:1016.
  3. Nicolaou N, Poorafshar M, Murray C, et al. Allergy or tolerance in children sensitized to peanut: prevalence and differentiation using component-resolved diagnostics. J Allergy Clin Immunol 2010; 125:191.
  4. Eller E, Bindslev-Jensen C. Clinical value of component-resolved diagnostics in peanut-allergic patients. Allergy 2013; 68:190.
  5. Dang TD, Tang M, Choo S, et al. Increasing the accuracy of peanut allergy diagnosis by using Ara h 2. J Allergy Clin Immunol 2012; 129:1056.
  6. Lieberman JA, Glaumann S, Batelson S, et al. The utility of peanut components in the diagnosis of IgE-mediated peanut allergy among distinct populations. J Allergy Clin Immunol Pract 2013; 1:75.
  7. Klemans RJ, Broekman HC, Knol EF, et al. Ara h 2 is the best predictor for peanut allergy in adults. J Allergy Clin Immunol Pract 2013; 1:632.
  8. Asarnoj A, Nilsson C, Lidholm J, et al. Peanut component Ara h 8 sensitization and tolerance to peanut. J Allergy Clin Immunol 2012; 130:468.
  9. Keet CA, Johnson K, Savage JH, et al. Evaluation of Ara h2 IgE thresholds in the diagnosis of peanut allergy in a clinical population. J Allergy Clin Immunol Pract 2013; 1:101.
  10. Martínez-Aranguren R, Lizaso MT, Goikoetxea MJ, et al. Is the determination of specific IgE against components using ISAC 112 a reproducible technique? PLoS One 2014; 9:e88394.
  11. Gadisseur R, Chapelle JP, Cavalier E. A new tool in the field of in-vitro diagnosis of allergy: preliminary results in the comparison of ImmunoCAP© 250 with the ImmunoCAP© ISAC. Clin Chem Lab Med 2011; 49:277.
  12. Goikoetxea MJ, Sanz ML, García BE, et al. Recommendations for the use of in vitro methods to detect specific immunoglobulin E: are they comparable? J Investig Allergol Clin Immunol 2013; 23:448.
  13. Sicherer SH, Wood RA. Advances in diagnosing peanut allergy. J Allergy Clin Immunol Pract 2013; 1:1.
  14. Koppelman SJ, Wensing M, Ertmann M, et al. Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen. Clin Exp Allergy 2004; 34:583.
  15. Asarnoj A, Movérare R, Ostblom E, et al. IgE to peanut allergen components: relation to peanut symptoms and pollen sensitization in 8-year-olds. Allergy 2010; 65:1189.
  16. Krause S, Reese G, Randow S, et al. Lipid transfer protein (Ara h 9) as a new peanut allergen relevant for a Mediterranean allergic population. J Allergy Clin Immunol 2009; 124:771.
  17. Bublin M, Breiteneder H. Cross-reactivity of peanut allergens. Curr Allergy Asthma Rep 2014; 14:426.
  18. Petersen A, Kull S, Rennert S, et al. Peanut defensins: Novel allergens isolated from lipophilic peanut extract. J Allergy Clin Immunol 2015; 136:1295.
  19. Lopes de Oliveira LC, Aderhold M, Brill M, 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.
  20. Aalberse JA, Meijer Y, Derksen N, et al. Moving from peanut extract to peanut components: towards validation of component-resolved IgE tests. Allergy 2013; 68:748.
  21. Asarnoj A, Glaumann S, Elfström L, et al. Anaphylaxis to peanut in a patient predominantly sensitized to Ara h 6. Int Arch Allergy Immunol 2012; 159:209.
  22. Bégin P, Vitte J, Paradis L, et al. Long-term prognostic value of component-resolved diagnosis in infants and toddlers with peanut allergy. Pediatr Allergy Immunol 2014; 25:506.
  23. De Knop KJ, Verweij MM, Grimmelikhuijsen M, et al. Age-related sensitization profiles for hazelnut (Corylus avellana) in a birch-endemic region. Pediatr Allergy Immunol 2011; 22:e139.
  24. Hansen KS, Ballmer-Weber BK, Sastre J, et al. Component-resolved in vitro diagnosis of hazelnut allergy in Europe. J Allergy Clin Immunol 2009; 123:1134.
  25. Schocker F, Lüttkopf D, Scheurer S, et al. Recombinant lipid transfer protein Cor a 8 from hazelnut: a new tool for in vitro diagnosis of potentially severe hazelnut allergy. J Allergy Clin Immunol 2004; 113:141.
  26. Beyer K, Grishina G, Bardina L, et al. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J Allergy Clin Immunol 2002; 110:517.
  27. Masthoff LJ, Mattsson L, Zuidmeer-Jongejan L, et al. Sensitization to Cor a 9 and Cor a 14 is highly specific for a hazelnut allergy with objective symptoms in Dutch children and adults. J Allergy Clin Immunol 2013; 132:393.
  28. Baar A, Pahr S, Constantin C, et al. Specific IgE reactivity to Tri a 36 in children with wheat food allergy. J Allergy Clin Immunol 2014; 133:585.
  29. Ballmer-Weber BK, Vieths S. Soy allergy in perspective. Curr Opin Allergy Clin Immunol 2008; 8:270.
  30. Mittag D, Vieths S, Vogel L, et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 2004; 113:148.
  31. Ito K, Sjölander S, Sato S, et al. IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children. J Allergy Clin Immunol 2011; 128:673.
  32. Holzhauser T, Wackermann O, Ballmer-Weber BK, et al. Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. J Allergy Clin Immunol 2009; 123:452.
  33. Berneder M, Bublin M, Hoffmann-Sommergruber K, et al. 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.
  34. Ebisawa M, Brostedt P, Sjölander S, et al. Gly m 2S albumin is a major allergen with a high diagnostic value in soybean-allergic children. J Allergy Clin Immunol 2013; 132:976.
  35. Klemans RJ, Knol EF, Michelsen-Huisman A, et al. Components in soy allergy diagnostics: Gly m 2S albumin has the best diagnostic value in adults. Allergy 2013; 68:1396.
  36. Kattan JD, Sampson HA. Clinical reactivity to soy is best identified by component testing to Gly m 8. J Allergy Clin Immunol Pract 2015; 3:970.
  37. Bublin M, Pfister M, Radauer C, et al. Component-resolved diagnosis of kiwifruit allergy with purified natural and recombinant kiwifruit allergens. J Allergy Clin Immunol 2010; 125:687.
  38. Rossi RE, Monasterolo G, Canonica GW, Passalacqua G. Systemic reactions to peach are associated with high levels of specific IgE to Pru p 3. Allergy 2009; 64:1795.
  39. Gaier S, Oberhuber C, Hemmer W, et al. Pru p 3 as a marker for symptom severity for patients with peach allergy in a birch pollen environment. J Allergy Clin Immunol 2009; 124:166.
  40. Novembre E, Mori F, Contestabile S, et al. Correlation of anti-Pru p 3 IgE levels with severity of peach allergy reactions in children. Ann Allergy Asthma Immunol 2012; 108:271.