Browsing by Author "Piras, Cristian"
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- Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?Publication . Costa, Joana; Villa, Caterina; Verhoeckx, Kitty; Cirkovic-Velickovic, Tanja; Schrama, Denise; Roncada, Paola; Rodrigues, Pedro M.; Piras, Cristian; Martin-Pedraza, Laura; Monaci, Linda; Molina, Elena; Mazzucchelli, Gabriel; Mafra, Isabel; Lupi, Roberta; Lozano-Ojalvo, Daniel; Larre, Colette; Klueber, Julia; Gelencser, Eva; Bueno-Diaz, Cristina; Diaz-Perales, Araceli; Benede, Sara; Bavaro, Simona Lucia; Kuehn, Annette; Hoffmann-Sommergruber, Karim; Holzhauser, ThomasKey determinants for the development of an allergic response to an otherwise 'harmless' food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing. Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens. We found that each parameter can have variable effects, ranging on an axis from allergenicity enhancement to resolution, depending on its nature and the allergen. While glycosylation and phosphorylation are common, both are not universal traits of animal allergens. High molecular structures can favour allergenicity, but structural loss and uncovering hidden epitopes can also have a similar impact. We discovered that there are important knowledge gaps in regard to physicochemical parameters shaping protein allergenicity both from animal and plant origin, mainly because the comparability of the data is poor. Future biomolecular studies of exhaustive, standardised design together with strong validation part in the clinical context, together with data integration model systems will be needed to unravel causal relationships between physicochemical properties and the basis of protein allergenicity.
- Are physicochemical properties shaping the allergenic potency of plant allergens?Publication . Costa, Joana; Bavaro, Simona Lucia; Benede, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larre, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martin-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Cirkovic-Velickovic, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, ThomasThis 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.
- Proteomics in food: Quality, safety, microbes, and allergensPublication . Piras, Cristian; Roncada, Paola; Guerreiro, Pedro M; Bonizzi, Luigi; Soggiu, AlessioFood safety and quality and their associated risks pose a major concern worldwide regarding not only the relative economical losses but also the potential danger to consumer's health. Customer's confidence in the integrity of the food supply could be hampered by inappropriate food safety measures. A lack of measures and reliable assays to evaluate and maintain a good control of food characteristics may affect the food industry economy and shatter consumer confidence. It is imperative to create and to establish fast and reliable analytical methods that allow a good and rapid analysis of food products during the whole food chain. Proteomics can represent a powerful tool to address this issue, due to its proven excellent quantitative and qualitative drawbacks in protein analysis. This review illustrates the applications of proteomics in the past few years in food science focusing on food of animal origin with some brief hints on other types. Aim of this review is to highlight the importance of this science as a valuable tool to assess food quality and safety. Emphasis is also posed in food processing, allergies, and possible contaminants like bacteria, fungi, and other pathogens.