Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut

Yvonne M. Vissers, Fany Blanc, Per Stahl Skov, Phil E. Johnson, Neil M. Rigby, Laetitia Przybylski-Nicaise, Hervé Bernard, Jean Michel Wal, Barbara Ballmer-Weber, Laurian Zuidmeer-Jongejan, Zsolt Szépfalusi, Janneke Ruinemans-Koerts, Ad P.H. Jansen, Huub F.J. Savelkoul, Harry J. Wichers, Alan R. Mackie, Clare E.N. Mills, Karine Adel-Patient

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

Background: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. Methodology/Principal Findings: Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. Conclusions/Significance: Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.

Original languageEnglish (US)
Article numbere23998
JournalPloS one
Volume6
Issue number8
DOIs
StatePublished - Aug 25 2011

Fingerprint

allergenicity
glycation
Heating
Immunoglobulin E
peanuts
albumins
Albumins
heat
Allergies
Denaturation
peanut protein
Proteins
Allergens
mononuclear leukocytes
Hot Temperature
allergens
denaturation
Galectin 3
T-cells
proteins

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Cite this

Vissers, Y. M., Blanc, F., Skov, P. S., Johnson, P. E., Rigby, N. M., Przybylski-Nicaise, L., ... Adel-Patient, K. (2011). Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PloS one, 6(8), [e23998]. https://doi.org/10.1371/journal.pone.0023998

Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. / Vissers, Yvonne M.; Blanc, Fany; Skov, Per Stahl; Johnson, Phil E.; Rigby, Neil M.; Przybylski-Nicaise, Laetitia; Bernard, Hervé; Wal, Jean Michel; Ballmer-Weber, Barbara; Zuidmeer-Jongejan, Laurian; Szépfalusi, Zsolt; Ruinemans-Koerts, Janneke; Jansen, Ad P.H.; Savelkoul, Huub F.J.; Wichers, Harry J.; Mackie, Alan R.; Mills, Clare E.N.; Adel-Patient, Karine.

In: PloS one, Vol. 6, No. 8, e23998, 25.08.2011.

Research output: Contribution to journalArticle

Vissers, YM, Blanc, F, Skov, PS, Johnson, PE, Rigby, NM, Przybylski-Nicaise, L, Bernard, H, Wal, JM, Ballmer-Weber, B, Zuidmeer-Jongejan, L, Szépfalusi, Z, Ruinemans-Koerts, J, Jansen, APH, Savelkoul, HFJ, Wichers, HJ, Mackie, AR, Mills, CEN & Adel-Patient, K 2011, 'Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut', PloS one, vol. 6, no. 8, e23998. https://doi.org/10.1371/journal.pone.0023998
Vissers, Yvonne M. ; Blanc, Fany ; Skov, Per Stahl ; Johnson, Phil E. ; Rigby, Neil M. ; Przybylski-Nicaise, Laetitia ; Bernard, Hervé ; Wal, Jean Michel ; Ballmer-Weber, Barbara ; Zuidmeer-Jongejan, Laurian ; Szépfalusi, Zsolt ; Ruinemans-Koerts, Janneke ; Jansen, Ad P.H. ; Savelkoul, Huub F.J. ; Wichers, Harry J. ; Mackie, Alan R. ; Mills, Clare E.N. ; Adel-Patient, Karine. / Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. In: PloS one. 2011 ; Vol. 6, No. 8.
@article{9c239efcfeef44f79a924c3749491b7c,
title = "Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut",
abstract = "Background: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. Methodology/Principal Findings: Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. Conclusions/Significance: Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.",
author = "Vissers, {Yvonne M.} and Fany Blanc and Skov, {Per Stahl} and Johnson, {Phil E.} and Rigby, {Neil M.} and Laetitia Przybylski-Nicaise and Herv{\'e} Bernard and Wal, {Jean Michel} and Barbara Ballmer-Weber and Laurian Zuidmeer-Jongejan and Zsolt Sz{\'e}pfalusi and Janneke Ruinemans-Koerts and Jansen, {Ad P.H.} and Savelkoul, {Huub F.J.} and Wichers, {Harry J.} and Mackie, {Alan R.} and Mills, {Clare E.N.} and Karine Adel-Patient",
year = "2011",
month = "8",
day = "25",
doi = "10.1371/journal.pone.0023998",
language = "English (US)",
volume = "6",
journal = "PLoS One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "8",

}

TY - JOUR

T1 - Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut

AU - Vissers, Yvonne M.

AU - Blanc, Fany

AU - Skov, Per Stahl

AU - Johnson, Phil E.

AU - Rigby, Neil M.

AU - Przybylski-Nicaise, Laetitia

AU - Bernard, Hervé

AU - Wal, Jean Michel

AU - Ballmer-Weber, Barbara

AU - Zuidmeer-Jongejan, Laurian

AU - Szépfalusi, Zsolt

AU - Ruinemans-Koerts, Janneke

AU - Jansen, Ad P.H.

AU - Savelkoul, Huub F.J.

AU - Wichers, Harry J.

AU - Mackie, Alan R.

AU - Mills, Clare E.N.

AU - Adel-Patient, Karine

PY - 2011/8/25

Y1 - 2011/8/25

N2 - Background: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. Methodology/Principal Findings: Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. Conclusions/Significance: Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.

AB - Background: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. Methodology/Principal Findings: Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. Conclusions/Significance: Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.

UR - http://www.scopus.com/inward/record.url?scp=80052039485&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80052039485&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0023998

DO - 10.1371/journal.pone.0023998

M3 - Article

C2 - 21901150

AN - SCOPUS:80052039485

VL - 6

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 8

M1 - e23998

ER -