Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6: The necessity of degranulation assays

Y. M. Vissers, M. Iwan, K. Adel-Patient, P. Stahl Skov, N. M. Rigby, P. E. Johnson, P. Mandrup Müller, L. Przybylski-Nicaise, M. Schaap, J. Ruinemans-Koerts, A. P.H. Jansen, E. N.C. Mills, H. F.J. Savelkoul, H. J. Wichers

Research output: Contribution to journalArticle

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Abstract

Background Peanuts are often consumed after roasting, a process that alters the three-dimensional structure of allergens and leads to Maillard modification. Such changes are likely to affect their allergenicity. Objective We aimed to establish the effect of thermal treatment mimicking the roasting process on the allergenicity of Ara h 1 and a mix of 2S albumins from peanut (Ara h 2/6). Methods Ara h 1 and Ara h 2/6 were purified from raw peanuts and heated in a dry form for 20min at 145°C in the presence (R+g) or absence (R-g) of glucose, and soluble proteins were then extracted. Sera obtained from 12 well-characterized peanut-allergic patients were used to assess the IgE binding and degranulation capacities of the allergens. Results Extensive heating at low moisture resulted in the hydrolysis of both Ara h 1 and Ara h 2/6. However, in contrast to Ara h 2/6, soluble R+g Ara h 1 formed large aggregates. Although the IgE-binding capacity of R+g and R-g Ara h 1 was decreased 9000- and 3.6-fold, respectively, compared with native Ara h 1, their capacity to elicit mediator release was increased. Conversely, both the IgE-binding capacity and the degranulation capacity of R-g Ara h 2/6 were 600-700-fold lower compared with the native form, although the presence of glucose during heating significantly moderated these losses. Conclusions and Clinical Relevance Extensive heating reduced the degranulation capacity of Ara h 2/6 but significantly increased the degranulation capacity of Ara h 1. This observation can have important ramifications for component-resolved approaches for diagnosis and demonstrates the importance of investigating the degranulation capacity in addition to IgE reactivity when assessing the effects of food processing on the allergenicity of proteins.

Original languageEnglish (US)
Pages (from-to)1631-1642
Number of pages12
JournalClinical and Experimental Allergy
Volume41
Issue number11
DOIs
StatePublished - Nov 1 2011

Fingerprint

Immunoglobulin E
Heating
Allergens
Glucose
Food Handling
Albumins
Proteins
Hydrolysis
Hot Temperature
Arachis hypogaea Ara h 1 protein
Arachis
Serum
Therapeutics

Keywords

  • Allergenicity
  • Ara h 1
  • Ara h 2/6
  • Glycation
  • Histamine release
  • IgE binding
  • Peanut allergy
  • RBL
  • Roasting
  • Thermal processing

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6 : The necessity of degranulation assays. / Vissers, Y. M.; Iwan, M.; Adel-Patient, K.; Stahl Skov, P.; Rigby, N. M.; Johnson, P. E.; Mandrup Müller, P.; Przybylski-Nicaise, L.; Schaap, M.; Ruinemans-Koerts, J.; Jansen, A. P.H.; Mills, E. N.C.; Savelkoul, H. F.J.; Wichers, H. J.

In: Clinical and Experimental Allergy, Vol. 41, No. 11, 01.11.2011, p. 1631-1642.

Research output: Contribution to journalArticle

Vissers, YM, Iwan, M, Adel-Patient, K, Stahl Skov, P, Rigby, NM, Johnson, PE, Mandrup Müller, P, Przybylski-Nicaise, L, Schaap, M, Ruinemans-Koerts, J, Jansen, APH, Mills, ENC, Savelkoul, HFJ & Wichers, HJ 2011, 'Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6: The necessity of degranulation assays', Clinical and Experimental Allergy, vol. 41, no. 11, pp. 1631-1642. https://doi.org/10.1111/j.1365-2222.2011.03830.x
Vissers, Y. M. ; Iwan, M. ; Adel-Patient, K. ; Stahl Skov, P. ; Rigby, N. M. ; Johnson, P. E. ; Mandrup Müller, P. ; Przybylski-Nicaise, L. ; Schaap, M. ; Ruinemans-Koerts, J. ; Jansen, A. P.H. ; Mills, E. N.C. ; Savelkoul, H. F.J. ; Wichers, H. J. / Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6 : The necessity of degranulation assays. In: Clinical and Experimental Allergy. 2011 ; Vol. 41, No. 11. pp. 1631-1642.
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T2 - The necessity of degranulation assays

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AU - Iwan, M.

AU - Adel-Patient, K.

AU - Stahl Skov, P.

AU - Rigby, N. M.

AU - Johnson, P. E.

AU - Mandrup Müller, P.

AU - Przybylski-Nicaise, L.

AU - Schaap, M.

AU - Ruinemans-Koerts, J.

AU - Jansen, A. P.H.

AU - Mills, E. N.C.

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AU - Wichers, H. J.

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N2 - Background Peanuts are often consumed after roasting, a process that alters the three-dimensional structure of allergens and leads to Maillard modification. Such changes are likely to affect their allergenicity. Objective We aimed to establish the effect of thermal treatment mimicking the roasting process on the allergenicity of Ara h 1 and a mix of 2S albumins from peanut (Ara h 2/6). Methods Ara h 1 and Ara h 2/6 were purified from raw peanuts and heated in a dry form for 20min at 145°C in the presence (R+g) or absence (R-g) of glucose, and soluble proteins were then extracted. Sera obtained from 12 well-characterized peanut-allergic patients were used to assess the IgE binding and degranulation capacities of the allergens. Results Extensive heating at low moisture resulted in the hydrolysis of both Ara h 1 and Ara h 2/6. However, in contrast to Ara h 2/6, soluble R+g Ara h 1 formed large aggregates. Although the IgE-binding capacity of R+g and R-g Ara h 1 was decreased 9000- and 3.6-fold, respectively, compared with native Ara h 1, their capacity to elicit mediator release was increased. Conversely, both the IgE-binding capacity and the degranulation capacity of R-g Ara h 2/6 were 600-700-fold lower compared with the native form, although the presence of glucose during heating significantly moderated these losses. Conclusions and Clinical Relevance Extensive heating reduced the degranulation capacity of Ara h 2/6 but significantly increased the degranulation capacity of Ara h 1. This observation can have important ramifications for component-resolved approaches for diagnosis and demonstrates the importance of investigating the degranulation capacity in addition to IgE reactivity when assessing the effects of food processing on the allergenicity of proteins.

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KW - Ara h 2/6

KW - Glycation

KW - Histamine release

KW - IgE binding

KW - Peanut allergy

KW - RBL

KW - Roasting

KW - Thermal processing

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