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Influence of peanut matrix on stability of allergens in gastric-simulated digesta : 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

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Abstract
Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs; <10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
Keywords
ARA H 2, IN-VITRO, MAJOR ALLERGEN, BREAST-MILK, FOOD, PROTEINS, EPITOPES, CHILDREN, REVEALS, digestion-resistant peptides, food matrix, gastric-simulated digestion, peanut allergy, proteolysis resistance

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Citation

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MLA
Prodic, I et al. “Influence of Peanut Matrix on Stability of Allergens in Gastric-simulated Digesta : 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-resistant Peptides.” CLINICAL AND EXPERIMENTAL ALLERGY 48.6 (2018): 731–740. Print.
APA
Prodic, I., Stanic-Vucinic, D., Apostolovic, D., Mihailovic, J., Radibratovic, M., Radosavljevic, J., Burazer, L., et al. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta : 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. CLINICAL AND EXPERIMENTAL ALLERGY, 48(6), 731–740.
Chicago author-date
Prodic, I, D Stanic-Vucinic, D Apostolovic, J Mihailovic, M Radibratovic, J Radosavljevic, L Burazer, et al. 2018. “Influence of Peanut Matrix on Stability of Allergens in Gastric-simulated Digesta : 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-resistant Peptides.” Clinical and Experimental Allergy 48 (6): 731–740.
Chicago author-date (all authors)
Prodic, I, D Stanic-Vucinic, D Apostolovic, J Mihailovic, M Radibratovic, J Radosavljevic, L Burazer, M Milcic, K Smiljanic, M van Hage, and Tanja Cirkovic Velickovic. 2018. “Influence of Peanut Matrix on Stability of Allergens in Gastric-simulated Digesta : 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-resistant Peptides.” Clinical and Experimental Allergy 48 (6): 731–740.
Vancouver
1.
Prodic I, Stanic-Vucinic D, Apostolovic D, Mihailovic J, Radibratovic M, Radosavljevic J, et al. Influence of peanut matrix on stability of allergens in gastric-simulated digesta : 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. CLINICAL AND EXPERIMENTAL ALLERGY. 2018;48(6):731–40.
IEEE
[1]
I. Prodic et al., “Influence of peanut matrix on stability of allergens in gastric-simulated digesta : 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides,” CLINICAL AND EXPERIMENTAL ALLERGY, vol. 48, no. 6, pp. 731–740, 2018.
@article{8615095,
  abstract     = {Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs; <10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated.
Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains.
Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta.
Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential.
Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.},
  author       = {Prodic, I and Stanic-Vucinic, D and Apostolovic, D and Mihailovic, J and Radibratovic, M and Radosavljevic, J and Burazer, L and Milcic, M and Smiljanic, K and van Hage, M and Cirkovic Velickovic, Tanja},
  issn         = {0954-7894},
  journal      = {CLINICAL AND EXPERIMENTAL ALLERGY},
  keywords     = {ARA H 2,IN-VITRO,MAJOR ALLERGEN,BREAST-MILK,FOOD,PROTEINS,EPITOPES,CHILDREN,REVEALS,digestion-resistant peptides,food matrix,gastric-simulated digestion,peanut allergy,proteolysis resistance},
  language     = {eng},
  number       = {6},
  pages        = {731--740},
  title        = {Influence of peanut matrix on stability of allergens in gastric-simulated digesta : 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides},
  url          = {http://dx.doi.org/10.1111/cea.13113},
  volume       = {48},
  year         = {2018},
}

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