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Special Issue "Advances on Allergens Identification and Characterization"

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A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (30 September 2020) | Viewed by 18649

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Dr. Isabel Mafra

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Guest Editor

REQUIMTE—LAQV, Faculdade de Farmácia, Universidade do Porto, Porto, Portugal
Interests: allergen detection; DNA analysis; food analysis; food authentication; GMO detection; food chemistry; real-time PCR
Special Issues, Collections and Topics in MDPI journals

Dr. Linda Monaci

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Guest Editor

Institute of Sciences of Food Production, Italian National Council of Research, ISPA-CNR, Via Amendola 122/O, 70126 Bari, Italy
Interests: food quality; food safety; allergen discovery and characterization; mass spectrometry; allergenicity assessment
Special Issues, Collections and Topics in MDPI journals

Dr. Joana Costa

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Guest Editor

REQUIMTE—LAQV, Faculdade de Farmácia, Universidade do Porto, Porto, Portugal
Interests: food allergy; food chemistry; clinical immunology and allergy assessment; allergen detection methods; allergen characterization; food quality; food safety
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food-induced allergies are currently one major issue of food safety and food security, representing an emerging problem of public health. They can be triggered by a wide variety of foods, being 90% of the food allergic reactions attributed to eight groups of foods: soybean, peanut, tree nuts, gluten-containing cereals, milk, eggs, fish, and crustaceans. Their ingestion represents a severe and concrete risk for sensitized individuals, who might suffer a diversity of adverse reactions, from mild (oral allergy syndrome, urticaria) to potentially life-threatening, such as anaphylaxis. Since the avoidance of food allergens is the only effective means of protecting the health of allergic individuals, the assessment of labelling compliance is essential to prevent any accidental exposure to the offending foods. The allergenic proteins in foods are diversified in nature (e.g., tropomyosins, albumins, vicilins, and legumins) and their immunoreactivity is associated with the presence of conformational and/or linear epitopes displayed by tri-dimensional folding or linear amino acid sequences, respectively. Any modification on their structure might affect the IgE-binding capacity, which can be the result of food processing, food matrix, or digestibility. Therefore, understanding their impact on molecular structure and allergenic potential is crucial for managing allergen risks in the food chain. This Special Issue intends to gather new analytical methodologies for the detection/identification of food allergens and advances on their characterization. The allergenic properties relating to the exposure of food allergens to new and current food processing technologies and in vitro digestibility are also particularly relevant to this Issue.

Dr. Linda Monaci
Dr. Isabel Mafra
Dr. Joana Costa
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. Biomolecules is an international peer-reviewed open access monthly 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 2700 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 allergens
allergen detection
allergen characterization
immunochemical methods
immunoreactivity
allergenicity
real-time PCR
proteomics
food processing
in vitro digestibility

Published Papers (6 papers)

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Research

Open AccessArticle

Impact of Different Lipid Ligands on the Stability and IgE-Binding Capacity of the Lentil Allergen Len c 3

Ekaterina I. Finkina

Daria N. Melnikova

Ivan V. Bogdanov

Natalia S. Matveevskaya

Anastasia A. Ignatova

Ilia Y. Toropygin

and

Tatiana V. Ovchinnikova

Biomolecules 2020, 10(12), 1668; https://doi.org/10.3390/biom10121668 - 13 Dec 2020

Cited by 14 | Viewed by 2178

Abstract

Previously, we isolated the lentil allergen Len c 3, belonging to the class of lipid transfer proteins, cross-reacting with the major peach allergen Pru p 3 and binding lipid ligands. In this work, the allergenic capacity of Len c 3 and effects of different lipid ligands on the protein stability and IgE-binding capacity were investigated. Impacts of pH and heat treating on ligand binding with Len c 3 were also studied. It was shown that the recombinant Len c 3 (rLen c 3) IgE-binding capacity is sensitive to heating and simulating of gastroduodenal digestion. While being heated or digested, the protein showed a considerably lower capacity to bind specific IgE in sera of allergic patients. The presence of lipid ligands increased the thermostability and resistance of rLen c 3 to digestion, but the level of these effects was dependent upon the ligand’s nature. The anionic lysolipid LPPG showed the most pronounced protective effect which correlated well with experimental data on ligand binding. Thus, the Len c 3 stability and allergenic capacity can be retained in the conditions of food heat cooking and gastroduodenal digestion due to the presence of certain lipid ligands. Full article

(This article belongs to the Special Issue Advances on Allergens Identification and Characterization)

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Open AccessArticle

Immunoglobulin E-Binding Pattern of Canadian Peanut Allergic Children and Cross-Reactivity with Almond, Hazelnut and Pistachio

and

Biomolecules 2020, 10(8), 1091; https://doi.org/10.3390/biom10081091 - 22 Jul 2020

Cited by 4 | Viewed by 2865

Abstract

Peanut allergic individuals can be both co-sensitized and co-allergic to peanut and tree nuts. At the moment, standard diagnostic approaches do not always allow differentiation between clinically relevant sensitization and nonsignificant cross-reactions, and the responsibility of each allergen remains unclear. The objective of this study was therefore to determine a peanut sensitization profile in a cohort of Canadian peanut allergic children and assess the immunoglobulin E (IgE) molecular cross-reactivity between peanut, almond, hazelnut and pistachio. The specific IgE (sIgE) levels of each patient serum were determined by ImmunoCAP, indirect ELISA and immunoblot to examine their sIgE-binding levels and profiles to peanut proteins. Reciprocal inhibition ELISA and immunoblotting were used to study sIgE cross-reactions between peanut and the selected tree nuts using an adjusted and representative serum pool of the nine allergic patients. The results showed that the prepared peanut and tree nut protein extracts allowed for the detection of the majority of peanut and selected tree nut known allergens. The reciprocal inhibition ELISA experiments showed limited sIgE cross-reactivities between peanut and the studied tree nuts, with peanut being most likely the sensitizing allergen and tree nuts the cross-reactive ones. In the case of hazelnut and pistachio, a coexisting primary sensitization to hazelnut and pistachio was also demonstrated in the serum pool. Reciprocal inhibition immunoblotting further revealed that storage proteins (2S albumin, 7S vicilin and 11S legumin) could possibly account for the observed IgE-cross-reactions between peanut and the studied tree nuts in this cohort of allergic individuals. It also demonstrated the importance of conformational epitopes in the exhibited cross-reactions. Full article

(This article belongs to the Special Issue Advances on Allergens Identification and Characterization)

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Open AccessArticle

Proteomic and Bioinformatic Investigations of Heat-Treated Anisakis simplex Third-Stage Larvae

and

Biomolecules 2020, 10(7), 1066; https://doi.org/10.3390/biom10071066 - 16 Jul 2020

Cited by 7 | Viewed by 3119

Abstract

Anisakis simplex third-stage larvae are the main source of hidden allergens in marine fish products. Some Anisakis allergens are thermostable and, even highly processed, could cause hypersensitivity reactions. However, Anisakis proteome has not been studied under autoclaving conditions of 121 °C for 60 min, which is an important process in the food industry. The aim of the study was the identification and characterization of allergens, potential allergens, and other proteins of heat-treated A. simplex larvae. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify 470 proteins, including allergens—Ani s 1, Ani s 2, Ani s 3, Ani s 4, Ani s 5—and 13 potential allergens that were mainly homologs of Anisakis spp., Ascaris spp., and Acari allergens. Ani s 2, Ani s 3, Ani s 5, and three possible allergens were found among the top 25 most abundant proteins. The computational analysis allowed us to detect allergen epitopes, assign protein families, and domains as well as to annotate the localization of proteins. The predicted 3D models of proteins revealed similarities between potential allergens and homologous allergens. Despite the partial degradation of heated A. simplex antigens, their immunoreactivity with anti-A. simplex IgG antibodies was confirmed using a Western blot. In conclusion, identified epitopes of allergenic peptides highlighted that the occurrence of Anisakis proteins in thermally processed fish products could be a potential allergic hazard. Further studies are necessary to confirm the IgE immunoreactivity and thermostability of identified proteins. Full article

(This article belongs to the Special Issue Advances on Allergens Identification and Characterization)

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Open AccessArticle

Emerging Allergens in Goji Berry Superfruit: The Identification of New IgE Binding Proteins towards Allergic Patients’ Sera

Carina Gabriela Uasuf

Elisabetta De Angelis

and

Biomolecules 2020, 10(5), 689; https://doi.org/10.3390/biom10050689 - 29 Apr 2020

Cited by 9 | Viewed by 2625

Abstract

The goji berry (Lycium barbarum L.) (GB) is gaining increasing attention with high consumption worldwide due to its exceptional nutritional value and medicinal benefits displayed in humans. Beyond their beneficial properties, GBs contain renowned allergenic proteins, and therefore deserve inclusion among the allergenic foods capable of inducing allergic reactions in sensitive consumers. GB allergy has been frequently linked to the panallergen lipid transfer protein (LTP), especially across the population of the Mediterranean area. Methods: In this study, we investigated the protein profile of GBs focusing on the most reactive proteins against immunoglobulins E (IgE) of allergic patients’ sera, as ascertained by immunoblot experiments. The protein spots displaying a clear reaction were excised, in-gel digested, and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by data searching against a restricted database for a reliable protein identification. Results: According to our data, three main spots were identified in GB extract as IgE binding proteins after immunoblot analysis. Some major proteins were identified and the three proteins that provided the highest reactivity were putatively attributed to vicilin and legumin proteins followed by a protein matching with 11S globulin belonging to the cupin superfamily. Finally, the whole GB protein extract was also submitted to bottom-up proteomics followed by a software-based database (DB) screening and a more exhaustive list of GB proteins was compiled. Full article

(This article belongs to the Special Issue Advances on Allergens Identification and Characterization)

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Open AccessEditor’s ChoiceArticle

Detection and Quantification of Milk Ingredients as Hidden Allergens in Meat Products by a Novel Specific Real-Time PCR Method

Caterina Villa

Joana Costa

and

Isabel Mafra

Biomolecules 2019, 9(12), 804; https://doi.org/10.3390/biom9120804 - 29 Nov 2019

Cited by 15 | Viewed by 3576

Abstract

Milk ingredients are often included in a wide range of meat products, such as cooked hams and sausages, to improve technological characteristics. However, milk proteins are also important food allergens. The aim of this study was the development of a highly sensitive and specific real-time PCR system targeting the 12S rRNA gene of Bos domesticus for the detection and quantification of milk as an allergenic ingredient in processed meat products. The method was able to achieve an absolute limit of detection (LOD) of 6 fg of milk DNA. Using a normalized approach (∆Ct method) for the detection of milk protein concentrate (MPC), it was possible to obtain sensitivities down to 0.01% (w/w) of MPC in model hams (raw and cooked) and autoclaved sausages, and 0.005% in raw sausage mixtures. The developed systems generally presented acceptable PCR performance parameters, being successfully validated with blind samples, applied to commercial samples, and further compared with an immunochemical assay. Trace amounts of milk material were quantified in two out of 13 samples, but the results mostly infer the excessive practice of the precautionary labeling. Full article

(This article belongs to the Special Issue Advances on Allergens Identification and Characterization)

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Open AccessArticle

Detection and Identification of Allergens from Canadian Mustard Varieties of Sinapis alba and Brassica juncea

Lamia L’Hocine

Mélanie Pitre

and

Allaoua Achouri

Biomolecules 2019, 9(9), 489; https://doi.org/10.3390/biom9090489 - 14 Sep 2019

Cited by 15 | Viewed by 3441

Abstract

Currently, information on the allergens profiles of different mustard varieties is rather scarce. Therefore, the objective of this study was to assess protein profiles and immunoglobulin E (IgE)-binding patterns of selected Canadian mustard varieties. Optimization of a non-denaturing protein extraction from the seeds of selected mustard varieties was first undertaken, and the various extracts were quantitatively and qualitatively analyzed by means of protein recovery determination and protein profiling. The IgE-binding patterns of selected mustard seeds extracts were assessed by immunoblotting using sera from mustard sensitized and allergic individuals. In addition to the known mustard allergens—Sin a 2 (11S globulins), Sin a 1, and Bra j 1 (2S albumins)—the presence of other new IgE-binding protein bands was revealed from both Sinapis alba and Brassica juncea varieties. Mass spectrometry (MS) analysis of the in-gel digested IgE-reactive bands identified the unknown ones as being oleosin, β-glucosidase, enolase, and glutathione-S transferase proteins. A bioinformatic comparison of the amino acid sequence of the new IgE-binding mustard proteins with those of know allergens revealed a number of strong homologies that are highly relevant for potential allergic cross-reactivity. Moreover, it was found that Sin a 1, Bra j 1, and cruciferin polypeptides exhibited a stronger IgE reactivity under non-reducing conditions in comparison to reducing conditions, demonstrating the recognition of conformational epitopes. These results further support the utilization of non-denaturing extraction and analysis conditions, as denaturing conditions may lead to failure in the detection of important immunoreactive epitopes. Full article

(This article belongs to the Special Issue Advances on Allergens Identification and Characterization)

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