Food Allergen Epitope Mapping

Liu, Changqi; Sathe, Shridhar K.

doi:10.1021/acs.jafc.8b01967

Cited by 85 publications

(61 citation statements)

References 103 publications

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“…Concerning epitope mapping of allergen-antibody interactions, only some allergen-antibody cocrystals have been elucidated so far, whereas the majority of binding regions were indirectly determined by in vitro mutagenesis (22,43,44). Besides, H/D exchange monitored by mass spectrometry can be explored for determination of interaction sites at the peptide level.…”

Section: Discussionmentioning

confidence: 99%

Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins

Muzio

Wildner

Huber

et al. 2020

Journal of Biological Chemistry

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Identification of antibody binding epitopes is crucial to understand immunological mechanisms. It is of particular interest for allergenic proteins with high cross-reactivity as observed in the lipid transfer protein (LTP) syndrome that is characterized by severe allergic reactions. Art v 3, a pollen LTP from mugwort is frequently involved in this cross-reactivity, but no antibody binding epitopes have been determined so far. To reveal human IgE binding regions of Art v 3, we produced three murine high-affinity monoclonal antibodies (mAbs), which showed 70-90% coverage of the allergenic epitopes from mugwort pollen allergic patients. As reliable methods to determine structural epitopes with tightly interacting intact antibodies under native conditions are lacking, we developed a straightforward NMR approach termed hydrogen/deuterium exchange memory (HDXMEM). It relies on the slow exchange between the invisible antigen-mAb complex and the free 15N-labeled antigen whose 1H-15N correlations are detected. Due to a memory effect, changes of NH protection during antibody binding are measured. Differences in H/D exchange rates and analyses of mAb reactivity to homologous LTPs revealed three structural epitopes: two partially cross-reactive regions around α-helices 2 and 4, as well as a novel Art v 3-specific epitope at the C-terminus. Protein variants with exchanged epitope residues confirmed the antibody-binding sites and revealed strongly reduced IgE reactivity. Using the novel HDXMEM for NMR epitope mapping allowed identification of the first structural epitopes of an allergenic pollen LTP. This knowledge enables improved cross-reactivity prediction for patients suffering from LTP-allergy and facilitates design of therapeutics.

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Section: Discussionmentioning

confidence: 99%

Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins

Muzio

Wildner

Huber

et al. 2020

Journal of Biological Chemistry

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“…They are of two types: (i) linear epitopes, corresponding to continuous amino acids in the protein sequence, (ii) conformational epitopes, formed by discontinuous amino acids in the three-dimensional structure of the protein. Experimental epitope identification is an expensive procedure and comprises several challenges even if helpful computational approaches are employed [ 43 ]. Methods using overlapping synthetic peptides, recombinant allergenic fragments, or unfolded allergens to identify linear epitopes permitted the identification of many linear epitopes as reported in IEDB ( , 31 May 2020) [ 44 , 45 , 46 ].…”

Section: Food Processing and Protein Allergenicitymentioning

confidence: 99%

Allergenicity of Fermented Foods: Emphasis on Seeds Protein-Based Products

Mecherfi

Todorov

Albuquerque

et al. 2020

Foods

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Food allergy is an IgE-mediated abnormal response to otherwise harmless food proteins, affecting between 5% and 10% of the world preschool children population and 1% to 5% adults. Several physical, chemical, and biotechnological approaches have been used to reduce the allergenicity of food allergens. Fermentation processes that contribute to technological and desirable changes in taste, flavor, digestibility, and texture of food products constitute one of these approaches. Lactic acid bacteria (LAB), used as starter cultures in dairy products, are a subject of increasing interest in fermentation of plant proteins. However, the studies designed to assess the impact of LAB on reduction of allergenicity of seed proteins are at an early stage. This review presents the current knowledge on food fermentation, with a focus on seed proteins that are increasingly used as ingredients, and its impacts on food potential allergenicity.

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“…In the specific field of food allergens, epitopes have been identified for several molecules using synthetic peptides and phage display approaches and review articles on the topic are already available [39,40]. An exemplificative case can be considered the study carried out on tropomyosin, a major crustacean allergen.…”

Section: Epitope Mapping By Molecular Approachesmentioning

confidence: 99%

Progress in the Analysis of Food Allergens through Molecular Biology Approaches

Volpicella

Leoni

Dileo

et al. 2019

Cells

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Food allergies associated with class E immunoglobulins (IgE) are a serious health problem that affects between 1% and 10% of the population of developing countries, with a variability that depends on the geographical area and age range considered. These allergies are caused by a cross-link reaction between a specific food protein (the allergen) and the host IgE. Allergic reactions can range from mild itching to anaphylactic shock and there are no clues to predict the effects of an allergen. Strict avoidance of allergenic food is the only way to avoid possible serious allergic reactions. In the last 30 years a growing number of molecular studies have been conducted to obtain information on the diffusion of food allergens and to establish the structural basis of their allergenicity. At the same time, these studies have also allowed the development of molecular tools (mainly based on synthetic peptides and recombinant allergens) that can be of great help for diagnostic and therapeutic approaches of food allergies. Accordingly, this review focuses on advances in the study of food allergens made possible by molecular technologies and how results and technologies can be integrated for the development of a systematic food molecular allergology. The review may be of interest both to scientists approaching this field of investigation and to physicians who wish to have an update on the progress of research in diagnosis and therapy of food allergies.

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Food Allergen Epitope Mapping

Cited by 85 publications

References 103 publications

Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins

Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins

Allergenicity of Fermented Foods: Emphasis on Seeds Protein-Based Products

Progress in the Analysis of Food Allergens through Molecular Biology Approaches

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