Browsing by Author "Holzhauser, Thomas"
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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.
- Current (Food) allergenic risk assessment: is it fit for novel foods? status quo and identification of gapsPublication . Mazzucchelli, Gabriel; Holzhauser, Thomas; Cirkovic Velickovic, Tanja; Diaz Perales, Araceli; Molina, Elena; Roncada, P.; Rodrigues, Pedro; Verhoeckx, Kitty; Hoffmann-Sommergruber, KarinFood allergies are recognized as a global health concern. In order to protect allergic consumers from severe symptoms, allergenic risk assessment for well-known foods and foods containing genetically modified ingredients is installed. However, population is steadily growing and there is a rising need to provide adequate protein-based foods, including novel sources, not yet used for human consumption. In this context safety issues such as a potential increased allergenic risk need to be assessed before marketing novel food sources. Therefore, the established allergenic risk assessment for genetically modified organisms needs to be re-evaluated for its applicability for risk assessment of novel food proteins. Two different scenarios of allergic sensitization have to be assessed. The first scenario is the presence of already known allergenic structures in novel foods. For this, a comparative assessment can be performed and the range of cross-reactivity can be explored, while in the second scenario allergic reactions are observed toward so far novel allergenic structures and no reference material is available. This review summarizes the current analytical methods for allergenic risk assessment, highlighting the strengths and limitations of each method and discussing the gaps in this assessment that need to be addressed in the near future.
- EAACI molecular allergology user's guide 2.0Publication . Dramburg, Stephanie; Hilger, Christiane; Santos, Alexandra F.; de las Vecillas, Leticia; Aalberse, Rob C.; Acevedo, Nathalie; Aglas, Lorenz; Altmann, Friedrich; Arruda, Karla L.; Asero, Riccardo; Ballmer‐Weber, Barbara; Barber, Domingo; Beyer, Kirsten; Biedermann, Tilo; Bilo, Maria Beatrice; Blank, Simon; Bosshard, Philipp P.; Breiteneder, Heimo; Brough, Helen A.; Bublin, Merima; Campbell, Dianne; Caraballo, Luis; Caubet, Jean Christoph; Celi, Giorgio; Chapman, Martin D.; Chruszcz, Maksymilian; Custovic, Adnan; Czolk, Rebecca; Davies, Janet; Douladiris, Nikolaos; Eberlein, Bernadette; Ebisawa, Motohiro; Ehlers, Anna; Eigenmann, Philippe; Gadermaier, Gabriele; Giovannini, Mattia; Gomez, Francisca; Grohman, Rebecca; Guillet, Carole; Hafner, Christine; Hamilton, Robert G.; Hauser, Michael; Hawranek, Thomas; Hoffmann, Hans Jürgen; Holzhauser, Thomas; Iizuka, Tomona; Jacquet, Alain; Jakob, Thilo; Janssen‐Weets, Bente; Jappe, Uta; Jutel, Marek; Kalic, Tanja; Kamath, Sandip; Kespohl, Sabine; Kleine‐Tebbe, Jörg; Knol, Edward; Knulst, André; Konradsen, Jon R.; Korošec, Peter; Kuehn, Annette; Lack, Gideon; Le, Thuy‐My; Lopata, Andreas; Luengo, Olga; Mäkelä, Mika; Marra, Alessandro Maria; Mills, Clare; Morisset, Martine; Muraro, Antonella; Nowak‐Wegrzyn, Anna; Nugraha, Roni; Ollert, Markus; Palosuo, Kati; Pastorello, Elide Anna; Patil, Sarita Ulhas; Platts‐Mills, Thomas; Pomés, Anna; Poncet, Pascal; Potapova, Ekaterina; Poulsen, Lars K.; Radauer, Christian; Radulovic, Suzana; Raulf, Monika; Rougé, Pierre; Sastre, Joaquin; Sato, Sakura; Scala, Enrico; Schmid, Johannes M.; Schmid‐Grendelmeier, Peter; Schrama, Denise; Sénéchal, Hélène; Traidl‐Hoffmann, Claudia; Valverde‐Monge, Marcela; van Hage, Marianne; van Ree, Ronald; Verhoeckx, Kitty; Vieths, Stefan; Wickman, Magnus; Zakzuk, Josefina; Matricardi, Paolo M.; Hoffmann‐Sommergruber, KarinSince the discovery of immunoglobulin E (IgE) as a mediator of allergic diseases in 1967, our knowledge about the immunological mechanisms of IgE-mediated allergies has remarkably increased. In addition to understanding the immune response and clinical symptoms, allergy diagnosis and management depend strongly on the precise identification of the elicitors of the IgE-mediated allergic reaction. In the past four decades, innovations in bioscience and technology have facilitated the identification and production of well-defined, highly pure molecules for component-resolved diagnosis (CRD), allowing a personalized diagnosis and management of the allergic disease for individual patients. The first edition of the "EAACI Molecular Allergology User's Guide" (MAUG) in 2016 rapidly became a key reference for clinicians, scientists, and interested readers with a background in allergology, immunology, biology, and medicine. Nevertheless, the field of molecular allergology is moving fast, and after 6 years, a new EAACI Taskforce was established to provide an updated document. The Molecular Allergology User's Guide 2.0 summarizes state-of-the-art information on allergen molecules, their clinical relevance, and their application in diagnostic algorithms for clinical practice. It is designed for both, clinicians and scientists, guiding health care professionals through the overwhelming list of different allergen molecules available for testing. Further, it provides diagnostic algorithms on the clinical relevance of allergenic molecules and gives an overview of their biology, the basic mechanisms of test formats, and the application of tests to measure allergen exposure.