Are physicochemical properties shaping the allergenic potency of plant allergens?

  • Molecular and Translational Allergology
September 02, 2020 By:
  • Costa J
  • Bavaro SL
  • Benedé S
  • Diaz-Perales A
  • Bueno-Diaz C
  • Gelencser E
  • Klueber J
  • Larré C
  • Lozano-Ojalvo D
  • Lupi R
  • Mafra I
  • Mazzucchelli G
  • Molina E
  • Monaci L
  • Martín-Pedraza L
  • Piras C
  • Rodrigues PM
  • Roncada P
  • Schrama D
  • Cirkovic-Velickovic T
  • Verhoeckx K
  • Villa C
  • Kuehn A
  • Hoffmann-Sommergruber K
  • Holzhauser T.

This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.

2020 Sep. Clin Rev Allergy Immunol. Online ahead of print.
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