Stability of allergens. (August 2018)

• Record Type: Journal Article
• Authors: Pekar, Judith; Ret, Davide; Untersmayr, Eva
• Is Part Of: Molecular immunology. Volume 100(2018:Aug.)
• Page Start: 14
• Page End: 20
• Publication Date: 2018-08
• Subjects: Allergen -- Allergen stability -- Protein sequence -- Protein structure -- Protein digestion -- Protein processing -- Posttranslational protein modification; Immunochemistry -- Periodicals; Molecular biology -- Periodicals; Immunochemistry -- Periodicals; Allergy and Immunology -- Periodicals; Molecular Biology -- Periodicals; Immunochimie -- Périodiques; Biologie moléculaire -- Périodiques; Immunochemistry; Molecular biology; Periodicals; Electronic journals; 571.96
• DOI: 10.1016/j.molimm.2018.03.017
• Languages: English
• ISSNs: 0161-5890

Abstract

Highlights: Allergen stability requirements depend on the entry route into the human body. Gastrointestinal physiology and food matrix effects influence allergen stability. Thermal and non-thermal food processing alter protein structure and stability. Protein intrinsic characteristics influence allergenicity of orally ingested proteins. 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.