Can Physicochemical Properties Alter the Potency of Aeroallergens? Part 1 - Aeroallergen Protein Families.

PURPOSE OF REVIEW: Respiratory allergies are non-communicable diseases caused by the hypersensitivity of the immune system to environmental aeroallergens. The culprits are aero-transported proteins eliciting respiratory symptoms in sensitized/allergic individuals. This review intends to provide a holistic overview on the categorization of aeroallergens into protein families (Part 1) and to exploit the impact of physicochemical properties on inhalant protein allergenicity (Part 2). This first part will focus particularly on aeroallergen organization into families and how this classification fits their physicochemical properties. RECENT FINDINGS: Aeroallergen classification into protein families facilitates the identification of common physicochemical properties, thus aiding a better comprehension of known allergens, while predicting the behavior of novel ones. The available online databases gathering important features of aeroallergens are currently scarce. Information on distinct aeroallergen classification is still lacking, as data is dispersed and often outdated, hampering an efficient evaluation of new aeroallergens.

Can Physicochemical Properties Alter the Potency of Aeroallergens? Part 2 - Impact of Physicochemical Properties.

PURPOSE OF REVIEW: A holistic perspective on how physicochemical properties modulate the allergenicity of proteins has recently been performed for food allergens, launching the challenge of a similar analysis for aeroallergens. After a first review on aeroallergen classification into protein families (Part 1), this second part (Part 2) will exploit the impact of physicochemical properties (abundance/biological function, protein structure/presence of post-translational modifications, ligand/cofactor/lipid-binding) on inhalant protein allergenicity. RECENT FINDINGS: The abundance linked to biological function is correlated with increased allergenic risk for most protein families, while the loss of structural integrity with consequent destruction of conformational epitopes is well linked with decreased allergenicity. Ligand-binding effect totally depends on the ligand type being highly variable among aeroallergens. Knowledge about the physicochemical properties of aeroallergens is still scarce, which highlights the need for research using integrated approaches (in silico and experimental) to generate and analyze new data on known/new aeroallergens.

γ-Conglutin Immunoreactivity Is Differently Affected by Thermal Treatment and Gastrointestinal Digestion in Lupine Species.

Lupine is a legume commonly used in human diet as a functional food due to its high nutritional content and important technological properties. However, its consumption can lead to the manifestation of adverse immunological reactions, posing significant health issues in sensitized/allergic patients. This work aims to investigate the effect of food processing combined with simulated gastrointestinal (GI) digestion on the immunoreactivity of lupine γ-conglutin. Model foods of wheat pasta containing 35% of lupine flour (Lupinus albus, L. luteus, and L. angustifolius) were prepared and submitted to a boiling process. The proteins were extracted and their profiles characterized by SDS-PAGE. Simulated GI digestion was performed on thermally treated pasta using the INFOGEST harmonized digestion protocol 2.0. The IgG binding capacity of γ-conglutin was assessed by immunoblotting in non-reducing conditions and indirect ELISA with specific antibodies. Results demonstrate that the boiling treatment affected the immunoreactivity of the three lupine species differently. Simulated GI digestion led to extensive destruction of the protein structure, more significant in the intestinal phase, reducing but not abolishing the IgG affinity to γ-conglutin and its potential presentation to immunocompetent cells. This information can offer valuable insights to the food industry for developing food formulations with reduced allergenic properties.