Browsing by Author "Rodrigues, Pedro M."
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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.
- Effects of dietary lipid sources on hepatic nutritive contents, fatty acid composition and proteome of Nile tilapia (Oreochromis niloticus)Publication . Boonanuntanasarn, Surintorn; Nakharuthai, Chatsirin; Schrama, Denise; Duangkaew, Rungsun; Rodrigues, Pedro M.Dietary oils of varying fatty acid composition have been used in tilapia feeds; nevertheless, investigation of their effects on metabolism and physiological processes has been limited. Therefore, in this study, using proteomic technology, the effects of different dietary lipids (DLs) on hepatic lipid metabolism and physiological processes were investigaed in Nile tilapia (Oreochromis niloticus). Fish were fed with different DL, which included palm oil (PO), linseed oil (LO) and soybean oil (SBO) for 90 days. Growth performance appeared to be similar among the dietary group. Hepatic FA contents were reflected by DL. Dietary PO (source of saturated fatty acids; SFA) led to an increase in the hepatosomatic index as well as lipid and protein contents in liver. Dietary SBO (source of n-6 polyunsaturated fatty acids; n-6 PUFAs) increased hepatic carbohydrate contents, but decreased the hepatic protein. The proteomic analysis showed that these nutritive changes in the liver were mediated by several proteins involved in lipid, carbohydrate, and amino acid metabolism. Dietary SBO showed an increased accumulation in proteins related to oxidative stress, immune and inflammatory processes. Dietary LO (source of n-3 PUFAs) increased abundance of cytoskeleton-related proteins. qRT-PCR was performed to provide supportive information for the result of proteomic study. Similar effects of DLs on mRNA levels were observed for atp5b, krt18, and selenbp1. Combined together, dietary SFA could supply as energy reservoir for regular activites. Dietary n-3 and n-6 PUFAs led to induce vital metabolic and physiologic processes which would contribute to maintaining normal health and/or providing health-related benefits. Significance: Dietary SBO increased hepatic carbohydrate contents, but decreased the hepatic protein. Different dietary lipid led to alter the abundance of several proteins (i.e., DHRS1, ATP5B, PLA2G12B, APO, AMY2A, GRP78, PRSS1, FAH, and PRSS36) involved in lipid, carbohydrate, and amino acid metabolism. Dietary SBO showed an increased accumulation in proteins (i.e., QDPR, CABC1, and PRDX6) that respond to oxidative stress, suggesting that n-6 PUFAs induce oxidative conditions. Dietary SBO led to increase the accumulation of proteins (i.e., NITR26, NCCRP1, and LCN) involved in immune and inflammatory processes. Dietary LO increased the abundant levels of cytoskeleton-related proteins (i.e., ACTB, AHNAK, ERC2, KRT18, and RILP1). Other proteins (i.e., SELENBP1, FAM46C, and ANC1) involved in other physiological processes were also modulated by DL. qRT-PCR was performed to provide supportive information of proteomic study. Similar effects of DLs on mRNA levels were observed for atp5b, krt18, and selenbp1.