Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products

Allergy. 2013 Dec;68(12):1546-54. doi: 10.1111/all.12261. Epub 2013 Nov 23.


Background: Recent immunological data demonstrated that dendritic cells preferentially recognize advanced glycation end product (AGE)-modified proteins, upregulate expression of the receptor for AGE (RAGE), and consequently bias the immune response toward allergy.

Methods: Peanut extract was characterized by mass spectrometry (MS) to elucidate the specific residues and specific AGE modifications found in raw and roasted peanuts and on rAra h 1 that was artificially glycated by incubation with glucose or xylose. The binding of the RAGE-V1C1 domain to peanut allergens was assessed by PAGE and Western analysis with anti-Ara h 1, 2, and 3 antibodies. IgE binding to rAra h 1 was also assessed using the same methods.

Results: AGE modifications were found on Ara h 1 and Ara h 3 in both raw and roasted peanut extract. No AGE modifications were found on Ara h 2. Mass spectrometry and Western blot analysis demonstrated that RAGE binds selectively to Ara h 1 and Ara h 3 derived from peanut extract, whereas the analysis failed to demonstrate Ara h 2 binding to RAGE. rAra h 1 with no AGE modifications did not bind RAGE; however, after AGE modification with xylose, rAra h 1 bound to RAGE.

Conclusions: AGE modifications to Ara h 1 and Ara h 3 can be found in both raw and roasted peanuts. Receptor for AGE was demonstrated to selectively interact with AGE-modified rAra h 1. If sensitization to peanut allergens occurs in dendritic cells via RAGE interactions, these cells are likely interacting with modified Ara h 1 and Ara h 3, but not Ara h 2.

Keywords: advanced glycation end product; allergens; epitopes; peanuts; receptor for AGE.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Allergens / chemistry*
  • Allergens / immunology
  • Amino Acid Sequence
  • Antigens, Plant / chemistry
  • Antigens, Plant / immunology
  • Antigens, Plant / metabolism
  • Arachis / chemistry*
  • Arachis / immunology
  • Glycation End Products, Advanced / chemistry
  • Glycation End Products, Advanced / immunology
  • Glycation End Products, Advanced / metabolism*
  • Glycoproteins / immunology
  • Glycoproteins / metabolism
  • Glycosylation
  • Humans
  • Immunoglobulin E / immunology
  • Immunoglobulin E / metabolism
  • Maillard Reaction*
  • Membrane Proteins
  • Models, Molecular
  • Plant Proteins / chemistry
  • Plant Proteins / immunology
  • Plant Proteins / metabolism
  • Protein Binding
  • Protein Conformation
  • Tandem Mass Spectrometry


  • Allergens
  • Antigens, Plant
  • Ara h 1 protein, Arachis hypogaea
  • Glycation End Products, Advanced
  • Glycoproteins
  • Membrane Proteins
  • Plant Proteins
  • Immunoglobulin E