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Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies

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A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Quality and Safety".

Deadline for manuscript submissions: closed (5 March 2022) | Viewed by 39476

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Special Issue Editors

Dr. Sara Benedé

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Guest Editor

Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM), 28049 Madrid, Spain
Interests: Food allergens, Food chemistry, Allergy & Clinical Immunology, Food Science & Technology

Dr. Daniel Lozano-Ojalvo

E-Mail Website
Guest Editor

Jaffe Food Allergy Institute, Immunology Institute, Icahn School of Medicine at Mount Sinai, New York, 10029, NY, USA
Interests: food allergy; antigen-specific T cells; peptides; egg hydrolysates

Special Issue Information

Dear Colleagues,

IgE-mediated food allergy is an increasing health problem that affects millions of persons worldwide. New developments in molecular allergology have allowed the advancement of knowledge in structure, characteristics and cellular interactions of food allergens, which could lead to a better food allergy management.

Molecular applications offer the opportunity to obtain a full panel of the sensitizing allergens in allergic patients and know the potential IgE-reactivities to cross-reactive allergens. To date there is no cure for food allergy, being the strict avoidance of the offending food the standard of treatment. However, an accurate diagnosis allows the development of specific treatments using safer and more efficacious products for allergy therapy. Molecule-based hypoallergenic preparations are the next generation of allergy vaccines. In addition, food labelling is an issue of relevance to food allergic consumers because processed foods may contain hidden allergens. Advances in allergen detection techniques allow quantifying trace levels of allergens, expanding food labelling information and protecting consumers from allergic reactions derived from cross-reactions.

This Special Issue is dedicated to the recent advances on diagnosis and treatment of food allergy as well as on identification of allergens. Therefore, articles addressing the development of innovative, reliable and rapid solutions for these matters are in the scope of this Foods Special Issue.

Regards,

Dr. Sara Benedé
Dr. Daniel Lozano-Ojalvo
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

food allergy
allergens
allergen characterization
diagnostic tests
molecular therapy
detection methods

Published Papers (11 papers)

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Editorial

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4 pages, 207 KiB

Open AccessEditorial

Molecular Approaches for Food Protein Allergenicity Assessment and the Diagnosis and Treatment of Food Allergies

by Daniel Lozano-Ojalvo and Sara Benedé

Foods 2023, 12(6), 1205; https://doi.org/10.3390/foods12061205 - 12 Mar 2023

Viewed by 1528

Abstract

Food allergy, an adverse immune reaction triggered by commonly innocuous food proteins, is a health problem that affects millions of people worldwide (around 10% of the global population), and the most recent reports suggest its increasing progression [...] Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

Research

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12 pages, 790 KiB

Open AccessArticle

The Quantification of IgG Specific to α-Gal Could Be Used as a Risk Marker for Suffering Mammalian Meat Allergy

by Alejandro Joral, Nahikari Azketa, Patricia Sanchez, Ainara Vélez-del-Burgo, María-Ascensión Aranzabal-Soto, Susana Lizarza, Jorge Martínez and Idoia Postigo

Foods 2022, 11(3), 466; https://doi.org/10.3390/foods11030466 - 04 Feb 2022

Cited by 4 | Viewed by 2657

Abstract

The alpha-Gal Syndrome is a delayed meat allergy characterized by the presence of sIgE against α-Gal epitope. It is known that the α-Gal present in tick saliva induces the sensitization to this epitope ending in the production of sIgG and sIgE to α-Gal. It could be considered that the more times a person is bitten by tick species, the higher the probability of making the switch from sIgG to sIgE to α-Gal and developing allergy, but it is no clear when the switch occurs. To determine the likelihood that a subject bitten by ticks but without AGS be at risk of developing this allergy, we quantified the levels of sIgG to α-Gal by an automated system (ImmunoCap). To stablish a cut-off value for sIgG to α-Gal, a receiving operating curve (ROC) was constructed. The statistical analysis demonstrated that the risk of suffering AGS in individuals bitten by ticks was 35% when the sIgG to α-Gal was greater than or equal to 40 µg/mL. Our data indicate that the sIgG values against α-Gal could be used as a prognostic marker for developing mammalian meat allergy. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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14 pages, 4282 KiB

Open AccessArticle

Recombinant Tropomyosin from the Pacific Oyster (Crassostrea gigas) for Better Diagnosis

by Roni Nugraha, Thimo Ruethers, Aya C. Taki, Elecia B. Johnston, Shaymaviswanathan Karnaneedi, Sandip D. Kamath and Andreas L. Lopata

Foods 2022, 11(3), 404; https://doi.org/10.3390/foods11030404 - 30 Jan 2022

Cited by 4 | Viewed by 2886

Abstract

The Pacific oyster is a commercially important mollusc and, in contrast to most other shellfish species, frequently consumed without prior heat treatment. Oysters are rich in many nutrients but can also cause food allergy. Knowledge of their allergens and cross-reactivity remains very limited. These limitations make an optimal diagnosis of oyster allergy difficult, in particular to the Pacific oyster (Crassostrea gigas), the most cultivated and consumed oyster species worldwide. This study aimed to characterise IgE sensitisation profiles of 21 oyster-sensitised patients to raw and heated Pacific oyster extract using immunoblotting and advanced mass spectrometry, and to assess the relevance of recombinant oyster allergen for improved diagnosis. Tropomyosin was identified as the major allergen recognised by IgE from 18 of 21 oyster-sensitised patients and has been registered with the WHO/IUIS as the first oyster allergen (Cra g 1). The IgE-binding capacity of oyster-sensitised patients’ IgE to purified natural and recombinant tropomyosin from oyster, prawn, and dust mite was compared using enzyme-linked immunosorbent assay. The degree of IgE binding varied between patients, indicating partial cross-sensitisation and/or co-sensitisation. Amino acid sequence alignment of tropomyosin from these three species revealed five regions that contain predicted IgE-binding epitopes, which are most likely responsible for this cross-reactivity. This study fully biochemically characterises the first and major oyster allergen Cra g 1 and demonstrates that the corresponding recombinant tropomyosin should be implemented in improved component-resolved diagnostics and guide future immunotherapy. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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16 pages, 5626 KiB

Open AccessArticle

Does the Food Ingredient Pectin Provide a Risk for Patients Allergic to Non-Specific Lipid-Transfer Proteins?

by Hanna Steigerwald, Frank Blanco-Perez, Melanie Albrecht, Caroline Bender, Andrea Wangorsch, Hans-Ulrich Endreß, Mirko Bunzel, Cristobalina Mayorga, Maria José Torres, Stephan Scheurer and Stefan Vieths

Foods 2022, 11(1), 13; https://doi.org/10.3390/foods11010013 - 21 Dec 2021

Cited by 3 | Viewed by 4568

Abstract

Pectin, a dietary fiber, is a polysaccharide that is widely used in food industry as a gelling agent. In addition, prebiotic and beneficial immunomodulatory effects of pectin have been demonstrated, leading to increased importance as food supplement. However, as cases of anaphylactic reactions after consumption of pectin-supplemented foods have been reported, the present study aims to evaluate the allergy risk of pectin. This is of particular importance since most of the pectin used in the food industry is extracted from citrus or apple pomace. Both contain several allergens such as non-specific lipid transfer proteins (nsLTPs), known to induce severe allergic reactions, which could impair the use of pectins in nsLTP allergic patients. Therefore, the present study for the first time was performed to analyze residual nsLTP content in two commercial pectins using different detection methods. Results showed the analytical sensitivity was diminished by the pectin structure. Finally, spiking of pectin with allergenic peach nsLTP Pru p 3 led to the conclusion that the potential residual allergen content in both pectins is below the threshold to induce anaphylactic reactions in nsLTP-allergic patients. This data suggests that consumption of the investigated commercial pectin products provides no risk for inducing severe reactions in nsLTP-allergic patients. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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16 pages, 3074 KiB

Open AccessArticle

Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1

by Soraya Chebib and Wilfried Schwab

Foods 2021, 10(11), 2771; https://doi.org/10.3390/foods10112771 - 11 Nov 2021

Cited by 5 | Viewed by 2350

Abstract

Pathogenesis-related (PR)-10 proteins, due to their particular secondary structure, can bind various ligands which could be important for their biological function. Accordingly, the PR-10 protein Mal d 1, the major apple allergen, probably also binds molecules in the hydrophobic cavity of its secondary structure, but it has not yet been investigated in this respect. In this study, various natural products found in apples such as flavonoids, glutathione (GSH), and glutathione disulfide (GSSG) were investigated as possible ligands of Mal d 1 using microscale thermophoresis. Dissociation constants of 16.39 µM, 29.51 µM, 35.79 µM, and 0.157 µM were determined for catechin, quercetin-3-O-rhamnoside, GSH, and GSSG, respectively. Molecular docking was performed to better understand the underlying binding mechanism and revealed hydrophobic interactions that stabilize the ligands within the pocket while hydrophilic interactions determine the binding of both GSH derivatives. The binding of these ligands could be important for the allergenicity of the PR-10 protein and provide further insights into its physiological role. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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12 pages, 532 KiB

Open AccessArticle

Storage Proteins Are Driving Pediatric Hazelnut Allergy in a Lipid Transfer Protein-Rich Area

by Teresa Valbuena, Marta Reche, Guadalupe Marco, Inmaculada Toboso, Anna Ringauf, Israel J. Thuissard-Vasallo, Daniel Lozano-Ojalvo, Mónica Martínez-Blanco and Elena Molina

Foods 2021, 10(10), 2463; https://doi.org/10.3390/foods10102463 - 15 Oct 2021

Cited by 3 | Viewed by 1424

Abstract

Oral food challenge (OFC) remains the gold standard for the diagnosis of food allergies. However, this test is not without risks, given that severe allergic reactions can be triggered while it is conducted. The purpose of this study is to identify potential demographic variables, clinical characteristics of the patients and biomarkers that may be associated with severe reactions during the hazelnut oral challenge test. The sample included 22 children allergic to hazelnut who underwent a tree nut skin prick test (SPT), specific IgE (sIgE) to hazelnut, component-resolved diagnosis (CRD) with different hazelnut allergens (Cor a 1, Cor a 8, Cor a 9, Cor a 11, Cor a 14), and a single-blind placebo-controlled challenge with hazelnut. A statistically significant relationship was found between the severity of the reaction and the highest values of sIgE to hazelnut, Cor a 11 and Cor a 14, cumulative symptom-triggering dose and sunflower seed sensitization. The use of the CRD is a useful tool to identify patients at higher risk of developing a severe reaction. In this pediatric population sample from Spain, storage proteins were confirmed to be most involved in hazelnut allergy and the development of severe reactions. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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16 pages, 9709 KiB

Open AccessArticle

Characterization of Relevant Biomarkers for the Diagnosis of Food Allergies: An Overview of the 2S Albumin Family

by Cristina Bueno-Díaz, Laura Martín-Pedraza, Jorge Parrón, Javier Cuesta-Herranz, Beatriz Cabanillas, Carlos Pastor-Vargas, Eva Batanero and Mayte Villalba

Foods 2021, 10(6), 1235; https://doi.org/10.3390/foods10061235 - 29 May 2021

Cited by 9 | Viewed by 3407

Abstract

2S albumins are relevant and often major allergens from several tree nuts and seeds, affecting mainly children and young people. The present study aims to assess how the structural features of 2S albumins could affect their immunogenic capacity, which is essential to comprehend the role of these proteins in food allergy. For this purpose, twelve 2S albumins were isolated from their respective extracts by chromatographic methods and identified by MALDI-TOF mass-spectrometry. Their molecular and structural characterization was conducted by electrophoretic, spectroscopic and in silico methods, showing that these are small proteins that comprise a wide range of isoelectric points, displaying a general high structure stability to thermal treatment. Despite low amino acid sequence identity, these proteins share structural features, pointing conformational epitopes to explain cross-reactivity between them. Immunoblotting with allergic patients’ sera revealed those possible correlations between evolutionarily distant 2S albumins from different sources. The availability of a well-characterized panel of 2S albumins from plant-derived sources allowed establishing correlations between their structural features and their allergenic potential, including their role in cross-reactivity processes. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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Review

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17 pages, 1407 KiB

Open AccessReview

Non-IgE-Mediated Gastrointestinal Food Protein-Induced Allergic Disorders. Clinical Perspectives and Analytical Approaches

by Elisa Zubeldia-Varela, Tomás Clive Barker-Tejeda, Frank Blanco-Pérez, Sonsoles Infante, José M. Zubeldia and Marina Pérez-Gordo

Foods 2021, 10(11), 2662; https://doi.org/10.3390/foods10112662 - 02 Nov 2021

Cited by 8 | Viewed by 4578

Abstract

Non-IgE-mediated gastrointestinal food allergy (non-IgE-GI-FA) is the name given to a series of pathologies whose main entities are food protein-induced allergic proctocolitis (FPIAP), food protein-induced enteropathy (FPE), and food protein-induced enterocolitis syndrome (FPIES). These are more uncommon than IgE-mediated food allergies, their mechanisms remain largely unknown, and their diagnosis is mainly done by clinical history, due to the lack of specific biomarkers. In this review, we present the latest advances found in the literature about clinical aspects, the current diagnosis, and treatment options of non-IgE-GI-FAs. We discuss the use of animal models, the analysis of gut microbiota, omics techniques, and fecal proteins with a focus on understanding the pathophysiological mechanisms of these pathologies and obtaining possible diagnostic and/or prognostic biomarkers. Finally, we discuss the unmet needs that researchers should tackle to advance in the knowledge of these barely explored pathologies. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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23 pages, 2006 KiB

Open AccessReview

New Insights in Therapy for Food Allergy

by Cristobalina Mayorga, Francisca Palomares, José A. Cañas, Natalia Pérez-Sánchez, Rafael Núñez, María José Torres and Francisca Gómez

Foods 2021, 10(5), 1037; https://doi.org/10.3390/foods10051037 - 10 May 2021

Cited by 19 | Viewed by 7366

Abstract

Food allergy is an increasing problem worldwide, with strict avoidance being classically the only available reliable treatment. The main objective of this review is to cover the latest information about the tools available for the diagnosis and treatment of food allergies. In recent years, many efforts have been made to better understand the humoral and cellular mechanisms involved in food allergy and to improve the strategies for diagnosis and treatment. This review illustrates IgE-mediated food hypersensitivity and provides a current description of the diagnostic strategies and advances in different treatments. Specific immunotherapy, including different routes of administration and new therapeutic approaches, such as hypoallergens and nanoparticles, are discussed in detail. Other treatments, such as biologics and microbiota, are also described. Therefore, we conclude that although important efforts have been made in improving therapies for food allergies, including innovative approaches mainly focusing on efficacy and safety, there is an urgent need to develop a set of basic and clinical results to help in the diagnosis and treatment of food allergies. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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22 pages, 453 KiB

Open AccessReview

Oral Mucosa as a Potential Site for Diagnosis and Treatment of Allergic and Autoimmune Diseases

by Cristina Gomez-Casado, Javier Sanchez-Solares, Elena Izquierdo, Araceli Díaz-Perales, Domingo Barber and María M. Escribese

Foods 2021, 10(5), 970; https://doi.org/10.3390/foods10050970 - 28 Apr 2021

Cited by 10 | Viewed by 5618

Abstract

Most prevalent food allergies during early childhood are caused by foods with a high allergenic protein content, such as milk, egg, nuts, or fish. In older subjects, some respiratory allergies progressively lead to food-induced allergic reactions, which can be severe, such as urticaria or asthma. Oral mucosa remodeling has been recently proven to be a feature of severe allergic phenotypes and autoimmune diseases. This remodeling process includes epithelial barrier disruption and the release of inflammatory signals. Although little is known about the immune processes taking place in the oral mucosa, there are a few reports describing the oral mucosa-associated immune system. In this review, we will provide an overview of the recent knowledge about the role of the oral mucosa in food-induced allergic reactions, as well as in severe respiratory allergies or food-induced autoimmune diseases, such as celiac disease. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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Other

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8 pages, 1397 KiB

Open AccessBrief Report

Caco-2 Cell Response Induced by Peptides Released after Digestion of Heat-Treated Egg White Proteins

by Sara Benedé, Leticia Pérez-Rodríguez and Elena Molina

Foods 2022, 11(22), 3566; https://doi.org/10.3390/foods11223566 - 09 Nov 2022

Cited by 3 | Viewed by 1383

Abstract

The heat treatment of food proteins induces structural modifications that influence their interaction with human fluids and cells. We aimed to evaluate the Caco-2 cell response induced by peptides produced after digestion of heat-treated egg white proteins. In vitro digestion of ovalbumin (OVA), ovomucoid (OM), and lysozyme (LYS), untreated or previously heated, was performed. The digestibility of proteins and the response of Caco-2 cells exposed to peptides (<10 kDa) generated during digestion were evaluated. Intact OVA and LYS persisted after the digestion of native proteins, whereas OM was completely hydrolysed. A heat treatment at 65 °C for 30 min did not alter the digestibility of OVA, whereas at 90 °C for 3 min, protein degradation was favoured. The digestibility of OM and LYS was not affected by heat treatment. Peptides derived from OVA and OM digestion induced IL-6 and IL-8 production. OVA and LYS digestion promoted the expression of Tslp, and Il6 and Il33, respectively. A heat treatment prior to OVA digestion reduced IL-6 production and Tslp expression. It was concluded that heat treatments can reduce the release of OVA-derived peptides, but not OM and LYS, with proinflammatory activity during digestion. Full article

(This article belongs to the Special Issue Molecular Approaches for Food Protein Allergenicity Assesment and the Diagnosis and Treatment of Food Allergies)

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