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Review
, 100, 14-20

Stability of Allergens

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Review

Stability of Allergens

Judith Pekar et al. Mol Immunol.

Abstract

For proteins to cause IgE-mediated allergic reactions, several common characteristics have to be defined, including small molecular size, solubility and stability to changing pH levels and enzymatic degradation. Nevertheless, these features are not unique for potent allergens, but are also observed in non-allergenic proteins. Due to the increasing awareness by regulatory authorities regarding the allergy pandemic, definition of characteristics unique to potent allergens would facilitate allergenicity assessment in the future. Despite major research efforts even to date the features unique for major allergens have not been elucidated so far. The route of allergen entry into the organism determines to a great extent these required characteristics. Especially orally ingested allergens are exposed to the harsh milieu of the gastrointestinal tract but might additionally be influenced by food processing. Depending on molecular properties such as disulphide bonds contributing to protein fold and formation of conformational IgE epitopes, posttranslational protein modification or protein food matrix interactions, enzymatic and thermal stability might differ between allergens. Moreover, also ligand binding influences structural stability. In the current review article, we aim at highlighting specific characteristics and molecular pattern contributing to a stabilized protein structure and overall allergenicity.

Keywords: Allergen; Allergen stability; Posttranslational protein modification; Protein digestion; Protein processing; Protein sequence; Protein structure.

Figures

Fig. 1
Fig. 1
Allergen uptake via skin and mucosal surfaces. To survive the compartment specific environment, different stability requirements enable allergens to penetrate epithelial barriers and to interact with immune cells for induction of an allergic response.
Fig. 2
Fig. 2
Protein digestion during the gastrointestinal transit. Gastrointestinal enzymes and varying pH levels influence digestion of orally ingested proteins.
Fig. 3
Fig. 3
Disulphide bonds contribute to protein stability. Due to the presence of intramolecular disulphide bonds, the three-dimensional allergen structure and IgE binding epitopes are preserved by enhanced protein resistance to proteolytic enzymes.
Fig. 4
Fig. 4
Different forms of protein interactions account for protein stability. Either by formation of oligomers or by interaction with matrix components, food allergens are modified, which contribute to conserved three-dimensional structure and overall stability.

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