68 research outputs found

    Critical review on proteotypic peptide marker tracing for six allergenic ingredients in incurred foods by mass spectrometry

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    Peptide marker identification is one of the most important steps in the development of a mass spectrometry (MS) based method for allergen detection, since the robustness and sensitivity of the overall analytical method will strictly depend on the reliability of the proteotypic peptides tracing for each allergen. The European legislation in place issues the mandatory labelling of fourteen allergenic ingredients whenever used in different food formulations. Among these, six allergenic ingredients, namely milk, egg, peanut, soybean, hazelnut and almond, can be prioritized in light of their higher occurrence in food recalls for undeclared presence with serious risk decision. In this work, we described the results of a comprehensive evaluation of the current literature on MS-based allergen detection aiming at collecting all available information about proteins and peptide markers validated in independent studies for the six allergenic ingredients of interest. The main features of the targeted proteins were commented reviewing all details available about known isoforms and sequence homology particularly in plant-derived allergens. Several critical aspects affecting peptide markers reliability were discussed and according to this evaluation a final short-list of candidate markers was compiled likely to be standardized and implemented in MS methods for allergen analysis

    Recent Progress and Recommendations on Celiac Disease From the Working Group on Prolamin Analysis and Toxicity

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    Celiac disease (CD) affects a growing number of individuals worldwide. To elucidate the causes for this increase, future multidisciplinary collaboration is key to understanding the interactions between immunoreactive components in gluten-containing cereals and the human gastrointestinal tract and immune system and to devise strategies for CD prevention and treatment beyond the gluten-free diet. During the last meetings, the Working Group on Prolamin Analysis and Toxicity (Prolamin Working Group, PWG) discussed recent progress in the field together with key stakeholders from celiac disease societies, academia, industry and regulatory bodies. Based on the current state of knowledge, this perspective from the PWG members provides recommendations regarding clinical, analytical and legal aspects of CD. The selected key topics that require future multidisciplinary collaborative efforts in the clinical field are to collect robust data on the increasing prevalence of CD, to evaluate what is special about gluten-specific T cells, to study their kinetics and transcriptomics and to put some attention to the identification of the environmental agents that facilitate the breaking of tolerance to gluten. In the field of gluten analysis, the key topics are the precise assessment of gluten immunoreactive components in wheat, rye and barley to understand how these are affected by genetic and environmental factors, the comparison of different methods for compliance monitoring of gluten-free products and the development of improved reference materials for gluten analysis

    Statement of the Prolamin Working Group on the Determination of Gluten in Fermented Foods Containing Partially Hydrolyzed Gluten

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    On August 12, 2020, the U.S. Food and Drug Administration (FDA) has finalized a rule related to gluten-free labeling for foods containing fermented, hydrolyzed ingredients. The FDA believes that there is no scientifically valid analytical method e ective for determining gluten in fermented or hydrolyzed foods. In the absence of an analytical method, the FDA has decided to evaluate gluten-free claims on these foods based only on evidence that the food or ingredient used is gluten-free before fermentation or hydrolysis. For example, barley-based beers from which gluten is removed during brewing using special filtration, adsorption and/or enzymatic treatment are therefore excluded from bearing a gluten-free label. The Prolamin Working Group (PWG) acknowledges that the FDA rule is a regulatory act and might have to take into consideration several aspects other than scientific evidence, including risk assessment. Nevertheless, the PWG thinks that science has to be the most important driver for regulatory acts in risk management.Fil: Scherf, Katharina Anne. Karlsruher Institut FĂŒr Technologie; AlemaniaFil: Catassi, Carlo. UniversitĂ  Politecnica Delle Marche; ItaliaFil: Chirdo, Fernando Gabriel. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - La Plata. Instituto de Estudios InmunolĂłgicos y FisiopatolĂłgicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios InmunolĂłgicos y FisiopatolĂłgicos; ArgentinaFil: Ciclitira, Paul J.. University of East Anglia; Reino UnidoFil: Feighery, Conleth Francis. Universidad de Dublin; IrlandaFil: Gianfrani, Carmen. Institute of Biochemistry and Cell Biology; ItaliaFil: Koning, Frits. Leiden University; PaĂ­ses BajosFil: Lundin, Knut E. A.. University of Oslo; NoruegaFil: Masci, Stefania. No especifĂ­ca;Fil: Schuppan, Detlef. No especifĂ­ca;Fil: Smulders, Marinus J. M.. Wageningen University and Research; PaĂ­ses BajosFil: Tranquet, Olivier. No especifĂ­ca;Fil: Troncone, Riccardo. University Federico II; ItaliaFil: Koehler, Peter. No especifĂ­ca

    Statement of the Prolamin Working Group on the Determination of Gluten in Fermented Foods Containing Partially Hydrolyzed Gluten

    Get PDF
    On August 12, 2020, the U.S. Food and Drug Administration (FDA) has finalized a rule related to gluten-free labeling for foods containing fermented, hydrolyzed ingredients. The FDA believes that there is no scientifically valid analytical method effective for determining gluten in fermented or hydrolyzed foods. In the absence of an analytical method, the FDA has decided to evaluate gluten-free claims on these foods based only on evidence that the food or ingredient used is gluten-free before fermentation or hydrolysis. For example, barley-based beers from which gluten is removed during brewing using special filtration, adsorption and/or enzymatic treatment are therefore excluded from bearing a gluten-free label

    Abstracts from the Food Allergy and Anaphylaxis Meeting 2016

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    Chimeric antibodies directed against sequences of the repeated domains of gliadins to mimic the IgE reactivity of wheat allergic patients

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    Les symptĂŽmes des allergies IgE dĂ©pendantes rĂ©sultent de l’activation des basophiles et de mastocytes. Cette activation est provoquĂ©e par l’agrĂ©gation Ă  la surface de ces cellules d’anticorps de type IgE par les allergĂšnes. Les allergĂšnes impliquĂ©s dans les formes les plus sĂ©vĂšres d’allergie au blĂ©, l’anaphylaxie induite par l’effort et l’allergie au gluten dĂ©samidĂ©, sont trĂšs particuliers dans la mesure oĂč ils contiennent des Ă©pitopes identiques rĂ©pĂ©tĂ©s plusieurs fois. Dans cette thĂšse, nous avons obtenu et caractĂ©risĂ© des IgE monoclonales chimĂ©riques souris/homme dirigĂ©es contre les domaines rĂ©pĂ©tĂ©s des gliadines, allergĂšnes impliquĂ©s dans ces phĂ©notypes sĂ©vĂšres d’allergie au blĂ©. Grace Ă  ces IgE chimĂ©riques monoclonales, nous avons explorĂ© le rĂŽle qu’avait ces rĂ©pĂ©titions sur le dĂ©clenchement des symptĂŽmes de l’allergie et leurs implications sur le rĂ©pertoire IgE des patients. Ces IgE chimĂ©riques ont dĂ©montrĂ© leur capacitĂ© Ă  mimer la rĂ©activitĂ© des IgE des patients. Elles ont par ailleurs rĂ©vĂ©lĂ© que l’organisation spatiale trĂšs particuliĂšre des Ă©pitopes permet l’activation des basophiles avec des IgE d’une seule spĂ©cificitĂ© dans ces deux types d’allergies au blĂ©. Il apparaĂźt ainsi que le rĂ©pertoire IgE des patients allergiques au blĂ© peut ĂȘtre extrĂȘmement restreint et tout de mĂȘme provoquer des rĂ©actions sĂ©vĂšres.The symptoms of IgE-dependent allergies result from the activation of basophils and mast cells. This activation is induced by the aggregation by allergens of IgE-type antibodies on the surface of these cells. The allergens involved in the more severe forms of wheat allergy, exercise-induced anaphylaxis and allergy to deamidated gluten, are very special in that they contain identical epitopes repeated several times. In this thesis, we obtained and characterized chimeric mouse/human monoclonal IgE antibodies directed against the repeated domains of gliadins, allergens involved in these severe wheat allergy phenotypes. Using these chimeric monoclonal IgE, we explored the role of these repeats on the onset of allergy symptoms and their implications on the IgE repertoire of patients. These chimeric IgE antibodies have been shown to mimic the reactivity of patients' IgE. They also revealed that the very particular spatial organization of the epitopes allows activation of basophils with IgE of a single specificity in these two types of wheat allergies. It thus appears that the IgE repertoire of patients with wheat allergy can be extremely restricted and still cause severe reactions

    Allergic reactions to hydrolysed wheat proteins: clinical aspects and molecular structures of the allergens involved

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    International audienceWheat gluten can be chemically or enzymatically hydrolysed to produce functional ingredients useful in food and cosmetics. However severe allergies to hydrolysed wheat proteins (HWP) have been described in Europe and Japan since the early 2000's. Triggering proteins and IgE epitopes were described both for French and Japanese cohorts and appeared remarkably similar leading to define a new wheat allergic entity. Deamidation induced by functionalisation generate neo-allergens responsible for this particular allergy. This article aims to review the processes leading to deamidation and the clinical features of the patients suffering from this allergy. Then the molecular determinants involved in HWP-allergy were exhaustively described and hypothesis regarding the sensitizing mechanism of HWP-allergy are discussed. Finally, current regulation and tools aiming at managing this risk associated with HWP are presented

    Milk Antibody Collection

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    Milk Antibody Collection. BiopolymÚres' 2010 Matrices alimentaires : Construction, déconstruction, propriétés sensorielles et nutritionnelle
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