Abstract
Allergic reactions to peanut (Arachis hypogaea, Ara h) are caused by immunoglobulin E (IgE)-mediated sensitizations to various proteins. The stability and relative proportion of these proteins in peanut determine the risk of hazardous reactions. Hazardous sensitization to seed storage proteins [S2 albumins (Ara h 2, 6 and 7) > other seed storage proteins (Ara 1 and 3) > oleosins (Ara h 10 and 11)] are distinct from sensitizations to lipid transfer protein (Ara h 9) with moderate risk or cross-sensitizations to Bet v 1-homologous PR-10 protein (Ara h 8) and to profilin (Ara h 5) with low risk. A specific IgE test, e.g. to Ara h 2 in the case of suspected systemic reaction, or where this should be ruled out, can facilitate easier risk assessment. Results, however, are only relevant in the presence of corresponding clinical symptoms. IgE sensitization to peanut extract without hazardous reactions is often caused in this part of the world by Bet v 1-related cross reactions (in birch pollen allergy sufferers), cross-reactive carbohydrate determinants (CCD) or profilin sensitizations. In the case of doubt, clinical relevance can only be established by means of oral challenge, particularly since not all peanut allergens (e. g., oleosins) are available as yet for diagnostic purposes.
Similar content being viewed by others
Abbreviations
- CCD:
-
cross-reactive carbohydrate determinants
- IgE:
-
Immunglobulin E
- nsLTP:
-
non-specific lipid transfer protein
References
Ahrens B, Niggemann B, Wahn U, Beyer K. Organ-specific symptoms during oral food challenge in children with food allergy. J Allergy Clin Immunol 2012;130:549–51
Koppelman SJ, Vlooswijk RA, Knippels LM, Hessing M, Knol EF, van Reijsen FC et al. Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world. Allergy 2001;56:132–7
Blom WM, Vlieg-Boerstra BJ, Kruizinga AG, van der Heide S, Houben GF, Dubois AE. Threshold dose distributions for 5 major allergenic foods in children. J Allergy Clin Immunol 2013;131:172–9
Nicolaou N, Custovic A. Molecular diagnosis of peanut and legume allergy. Curr Opin Allergy Clin Immunol 2011;11:22–8
Schmitz R, Ellert U, Kalcklösch M, Damm S, Thamm M. Patterns of sensitization to inhalant and food allergens - findings from the German Health Interview and Examination Survey for Children and Adolescents (KiGGS). Int Arch Allergy Immunol 2013;162:263–70
Vissers YM, Blanc F, Skov PS, Johnson PE, Rigby NM, Przybylski-Nicaise L et al. Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PLoS One 2011;6:e23998
Radauer C, Kleine-Tebbe J, Beyer K, Stabile pfanzliche Nahrungsmittelallergene: Speicherproteine. Allergo J 2012;21: 155–8
Bublin M, Kostadinova M, Radauer C, Hafner C, Szépfalusi Z, Varga EM et al. IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3. J Allergy Clin Immunol 2013;132:118–24
Vereda A, van Hage M, Ahlstedt S, Ibañez MD, Cuesta-Herranz J, van Odijk J et al. Peanut allergy: Clinical and immunologic differences among patients from 3 different geographic regions. J Allergy Clin Immunol 2011; 127:603–7
Codreanu F, Collignon O, Roitel O, Thouvenot B, Sauvage C, Vilain AC et al. A novel immunoassay using recombinant allergens simplifies peanut allergy diagnosis. Int Arch Allergy Immunol 2011;154:216–26
Cabanos C, Katayama H, Tanaka A, Utsumi S, Maruyama N. Expression and Purification of Peanut Oleosins in Insect Cells. Protein J 2011;30:457–63
Aalberse JA, Meijer Y, Derksen N, van der Palen-Merkus T, Knol E, Aalberse RC. Moving from peanut extract to peanut components: towards validation of component-resolved IgE tests. Allergy 2013;68:748–56
Petersen A, Scheurer S. Stabile pflanzliche Nahrungsmittelallergene: Lipid-Transfer-Proteine. Allergo J 2011;20:384–6
Asarnoj A, Movérare R, Ostblom E, Poorafshar M, Lilja G, Hedlin G et al. IgE to peanut allergen components: relation to peanut symptoms and pollen sensitization in 8-year-olds. Allergy 2010;65:1189–95
Asarnoj A, Nilsson C, Lidholm J, Glaumann S, Östblom E, Hedlin G et al. Peanut component Ara h 8 sensitization and tolerance to peanut. J Allergy Clin Immunol 2012;130:468–72
Nicolaou N, Murray C, Belgrave D, Poorafshar M, Simpson A, Custovic. Quantification of specific IgE to whole peanut extract and peanut components in prediction of peanut allergy. J Allergy Clin Immunol 2011; 127:684–5
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 componentresolved diagnostics. J Allergy Clin Immunol 2010; 125:191–7
Dang TD, Tang M, Choo S, Licciardi PV, Koplin JJ, Martin PE et al. HealthNuts study. Increasing the accuracy of peanut allergy diagnosis by using Ara h 2. J Allergy Clin Immunol 2012;129:1056–63
Eller E, Bindslev-Jensen C. Clinical value of component-resolved diagnostics in peanut-allergic patients. Allergy 2013;68:190–4
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
Asarnoj A, Glaumann S, Elfström L, Lilja G, Lidholm J, Nilsson C et al. Anaphylaxis to peanut in a patient predominantly sensitized to Ara h 6. Int Arch Allergy Immunol 2012;159:209–12
Krause S, Reese G, Randow S, Zennaro D, Quaratino D, Palazzo P et al. Lipid transfer protein (Ara h 9) as a new peanut allergen relevant for a Mediterranean allergic population. J Allergy Clin Immunol 2009;124:771–8
Lopes de Oliveira LC, Aderholz M, Brill M, Schulz G, Rolinck-Werninghaus C, Mills ENC 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
Author information
Authors and Affiliations
Corresponding author
Additional information
Conflict of interest
The authors declare that no conflicts of interests exist.
Acknowledgements
We would like to thank Bodo Niggemann (Pediatric, Pneumology and Immunology, Charité University Medicine, Berlin) for his valuable advice in the preparation of the flow diagrams.
Cite this as Lange L, Beyer K, Kleine-Tebbe J. Benefits and limitations of molecular diagnostics in peanut allergy. Allergo J Int 2014;23:158–63 DOI: 10.1007/s40629-014-0019-z
Rights and permissions
About this article
Cite this article
Lange, L., Beyer, K. & Kleine-Tebbe, J. Benefits and limitations of molecular diagnostics in peanut allergy. Allergo J Int 23, 158–163 (2014). https://doi.org/10.1007/s40629-014-0019-z
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s40629-014-0019-z