Removal of Peanut 2S Albumins, Ara h 2 and Ara h 6, from a Soluble Peanut Protein Extract Significantly Reduces Allergic Reactions in Peanut-Sensitized Mice

2010 ◽  
Vol 125 (2) ◽  
pp. AB223
Author(s):  
J. Lew ◽  
M. Kulis ◽  
L. Pons ◽  
X. Chen ◽  
H. Porterfield ◽  
...  
Keyword(s):  
Peanut Protein ◽  
Allergic Reactions ◽  
Protein Extract ◽  
Ara H 2 ◽  
2S Albumins ◽  
Ara H 6

scholarly journals Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions

2006 ◽  
Vol 395 (3) ◽  
pp. 463-472 ◽  
Author(s):  
Katrin Lehmann ◽  
Kristian Schweimer ◽  
Gerald Reese ◽  
Stefanie Randow ◽  
Martin Suhr ◽  
...  
Keyword(s):  
Proteolytic Enzymes ◽  
Binding Capacity ◽  
Homology Modelling ◽  
Antibody Binding ◽  
Allergic Reactions ◽  
2S Albumin ◽  
Ara H 2 ◽  
Ige Antibody ◽  
Peanut Allergens ◽  
Ara H 6

Resistance to proteolytic enzymes and heat is thought to be a prerequisite property of food allergens. Allergens from peanut (Arachis hypogaea) are the most frequent cause of fatal food allergic reactions. The allergenic 2S albumin Ara h 2 and the homologous minor allergen Ara h 6 were studied at the molecular level with regard to allergenic potency of native and protease-treated allergen. A high-resolution solution structure of the protease-resistant core of Ara h 6 was determined by NMR spectroscopy, and homology modelling was applied to generate an Ara h 2 structure. Ara h 2 appeared to be the more potent allergen, even though the two peanut allergens share substantial cross-reactivity. Both allergens contain cores that are highly resistant to proteolytic digestion and to temperatures of up to 100 °C. Even though IgE antibody-binding capacity was reduced by protease treatment, the mediator release from a functional equivalent of a mast cell or basophil, the humanized RBL (rat basophilic leukaemia) cell, demonstrated that this reduction in IgE antibody-binding capacity does not necessarily translate into reduced allergenic potency. Native Ara h 2 and Ara h 6 have virtually identical allergenic potency as compared with the allergens that were treated with digestive enzymes. The folds of the allergenic cores are virtually identical with each other and with the fold of the corresponding regions in the undigested proteins. The extreme immunological stability of the core structures of Ara h 2 and Ara h 6 provides an explanation for the persistence of the allergenic potency even after food processing.

scholarly journals Epitope Mapping of 2S albumins and Comparison of Ara h 2, Ara h 6 and Ara h 7 from Peanut

2019 ◽  
Vol 143 (2) ◽  
pp. AB68
Author(s):  
Barry K. Hurlburt ◽  
Hsiaopo Cheng ◽  
Soheila J. Maleki
Keyword(s):  
Epitope Mapping ◽  
Ara H 2 ◽  
2S Albumins ◽  
Ara H 6

scholarly journals Epitope Mapping of 2S albumins and Comparison of Ara h 2, Ara h 6 and Ara h 7 from Peanut

2018 ◽  
Vol 141 (2) ◽  
pp. AB238
Author(s):  
Soheila J. Maleki ◽  
Hsiaopo Cheng ◽  
Barry K. Hurlburt
Keyword(s):  
Epitope Mapping ◽  
Ara H 2 ◽  
2S Albumins ◽  
Ara H 6

scholarly journals Variable IgE cross‐reactivity between peanut 2S‐albumins: The case for measuring IgE to both Ara h 2 and Ara h 6

2019 ◽  
Author(s):  
Stéphane Hazebrouck ◽  
Blanche Guillon ◽  
Evelyne Paty ◽  
Stephen C. Dreskin ◽  
Karine Adel‐Patient ◽  
...  
Keyword(s):  
Cross Reactivity ◽  
Ara H 2 ◽  
2S Albumins ◽  
Ara H 6

scholarly journals Engineering of structural variants of the major peanut allergens Ara h 2 and Ara h 6 for allergen-specific immunotherapy

2019 ◽  
Vol 143 (3) ◽  
pp. 1226-1229.e10 ◽  
Author(s):  
Merima Bublin ◽  
Maria Kostadinova ◽  
Christian Radauer ◽  
Eva-Maria Varga ◽  
Christine Hafner ◽  
...  
Keyword(s):  
Specific Immunotherapy ◽  
Structural Variants ◽  
Allergen Specific Immunotherapy ◽  
Ara H 2 ◽  
Peanut Allergens ◽  
Ara H 6

scholarly journals Interaction of Monocyte-Derived Dendritic Cells with Ara h 2 from Raw and Roasted Peanuts

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 863 ◽  
Author(s):  
Natalija Novak ◽  
Soheila J. Maleki ◽  
Carmen Cuadrado ◽  
Jesus F. Crespo ◽  
Beatriz Cabanillas
Keyword(s):  
Dendritic Cells ◽  
Human Monocyte ◽  
Mannose Receptor ◽  
Allergic Reactions ◽  
Ara H 2 ◽  
Allergenic Potential ◽  
Sensitization Phase ◽  
Mannose Receptors ◽  
Dose Dependent

Ara h 2 is a relevant peanut allergen linked to severe allergic reactions. The interaction of Ara h 2 with components of the sensitization phase of food allergy (e.g., dendritic cells) has not been investigated, and could be key to understanding the allergenic potential of this allergen. In this study, we aimed to analyze such interactions and the possible mechanism involved. Ara h 2 was purified from two forms of peanut, raw and roasted, and labeled with a fluorescent dye. Human monocyte-derived dendritic cells (MDDCs) were obtained, and experiments of Ara h 2 internalization by MDDCs were carried out. The role of the mannose receptor in the internalization of Ara h 2 from raw and roasted peanuts was also investigated. Results showed that Ara h 2 internalization by MDDCs was both time and dose dependent. Mannose receptors in MDDCs had a greater implication in the internalization of Ara h 2 from roasted peanuts. However, this receptor was also important in the internalization of Ara h 2 from raw peanuts, as opposed to other allergens such as raw Ara h 3.

scholarly journals Impact of Cross-reactivity between Major Peanut Allergens Ara h 2 and Ara h 6 on Specific IgE Measurements

2018 ◽  
Vol 141 (2) ◽  
pp. AB237
Author(s):  
Blanche Guillon ◽  
Hervé Bernard ◽  
Evelyne Paty ◽  
Stephen C. Dreskin ◽  
Karine Adel-Patient ◽  
...  
Keyword(s):  
Specific Ige ◽  
Cross Reactivity ◽  
Ara H 2 ◽  
Peanut Allergens ◽  
Ara H 6
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