Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products
| Autor: | Barry K. Hurlburt, Soheila J. Maleki, Hsiaopo Cheng, Anna Pomés, Sanbao Ruan, Robert E. London, Allison N. Schorzman, Kenneth B. Tomer, Geoffrey A. Mueller, Jacqueline B. Nesbit, Jason Williams, Lori L. Edwards, HaJeung Park, Katina L. Johnson, Leesa J. Deterding |
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| Rok vydání: | 2013 |
| Předmět: |
Glycation End Products
Advanced Models Molecular Glycosylation Arachis Protein Conformation Immunology Immunoglobulin E Article RAGE (receptor) chemistry.chemical_compound symbols.namesake Western blot Tandem Mass Spectrometry Glycation medicine Humans Immunology and Allergy Amino Acid Sequence Receptor Glycoproteins Plant Proteins biology medicine.diagnostic_test Membrane Proteins food and beverages Allergens Antigens Plant biochemical phenomena metabolism and nutrition Maillard Reaction carbohydrates (lipids) Maillard reaction Biochemistry chemistry biology.protein symbols Advanced glycation end-product Protein Binding |
| Zdroj: | Allergy. 68:1546-1554 |
| ISSN: | 0105-4538 |
| DOI: | 10.1111/all.12261 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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