Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer

E.L. van Boxtel, M.M.C. van Beers, S.J. Koppelman, L.A.M. van den Broek, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

37 Citations (Scopus)

Abstract

Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bring about any structural changes, whereas exposing the allergen to hydrophobic interaction chromatography caused it to partly dissociate into trimers, with increasing amounts of trimers at higher ionic strengths. The (partial) dissociation into trimers led to a change in the tertiary structure of the monomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compact tertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics are important for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 than previously described.
Original languageEnglish
Pages (from-to)7180-7186
JournalJournal of Agricultural and Food Chemistry
Volume54
Issue number19
DOIs
Publication statusPublished - 2006

Fingerprint

allergens
Oligomers
Allergens
peanuts
allergenicity
Chromatography
Monomers
Size exclusion chromatography
Ammonium Sulfate
ionic strength
Ionic strength
Hydrophobic and Hydrophilic Interactions
salt concentration
ammonium sulfate
Osmolar Concentration
Purification
Gel Chromatography
Anions
Arachis
Proteins

Keywords

  • ige-binding epitopes
  • ara-h-i
  • atopic-dermatitis
  • storage proteins
  • circular-dichroism
  • beta-conglycinin
  • food allergens
  • identification
  • hypersensitivity
  • superfamily

Cite this

van Boxtel, E.L. ; van Beers, M.M.C. ; Koppelman, S.J. ; van den Broek, L.A.M. ; Gruppen, H. / Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer. In: Journal of Agricultural and Food Chemistry. 2006 ; Vol. 54, No. 19. pp. 7180-7186.
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title = "Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer",
abstract = "Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bring about any structural changes, whereas exposing the allergen to hydrophobic interaction chromatography caused it to partly dissociate into trimers, with increasing amounts of trimers at higher ionic strengths. The (partial) dissociation into trimers led to a change in the tertiary structure of the monomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compact tertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics are important for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 than previously described.",
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year = "2006",
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Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer. / van Boxtel, E.L.; van Beers, M.M.C.; Koppelman, S.J.; van den Broek, L.A.M.; Gruppen, H.

In: Journal of Agricultural and Food Chemistry, Vol. 54, No. 19, 2006, p. 7180-7186.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer

AU - van Boxtel, E.L.

AU - van Beers, M.M.C.

AU - Koppelman, S.J.

AU - van den Broek, L.A.M.

AU - Gruppen, H.

PY - 2006

Y1 - 2006

N2 - Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bring about any structural changes, whereas exposing the allergen to hydrophobic interaction chromatography caused it to partly dissociate into trimers, with increasing amounts of trimers at higher ionic strengths. The (partial) dissociation into trimers led to a change in the tertiary structure of the monomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compact tertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics are important for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 than previously described.

AB - Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bring about any structural changes, whereas exposing the allergen to hydrophobic interaction chromatography caused it to partly dissociate into trimers, with increasing amounts of trimers at higher ionic strengths. The (partial) dissociation into trimers led to a change in the tertiary structure of the monomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compact tertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics are important for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 than previously described.

KW - ige-binding epitopes

KW - ara-h-i

KW - atopic-dermatitis

KW - storage proteins

KW - circular-dichroism

KW - beta-conglycinin

KW - food allergens

KW - identification

KW - hypersensitivity

KW - superfamily

U2 - 10.1021/jf061433+

DO - 10.1021/jf061433+

M3 - Article

VL - 54

SP - 7180

EP - 7186

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 19

ER -