Allergenic Properties and Molecular Characteristics of Food Allergens

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

Deadline for manuscript submissions: 15 August 2024 | Viewed by 1176

Special Issue Editor


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Guest Editor
1. Associated Centers for Molecular Allergology (CAAM), 00100 Rome, Italy
2. Allergy Data Laboratories (ADL), 04100 Latina, Italy
Interests: molecular allergy; food allergy

Special Issue Information

Dear Colleagues,

Food allergy represents a burgeoning health crisis. Its prevalence has surged rapidly in recent decades, and likewise, research in the field of food allergy is increasing. Meanwhile, vital progress has been made regarding the characterization of food allergens, the study of their immunological properties, and their detection in natural sources and in processed products. A food allergen first elicits an immunoglobulin E (IgE) response in predisposed subjects, and then, on subsequent exposures, may elicit a clinical reaction to the same or similar proteins.

Known food allergens belong to a relatively restricted number of protein families, characterized by biochemical and physicochemical properties that may or may not include thermal stability and resistance to proteolysis. The allergenicity of a food protein cannot be predicted.  However, determining whether it belongs to a certain family of allergenic proteins enables us to understand whether a molecule is possibly predisposed to becoming an allergen; this represents an important first step, and may contribute to determining the allergenic risk.

The aim of this Special Issue of Foods is to gather and present cutting-edge research on the properties and molecular characteristics of food allergens.  This Special Issue welcomes the submission of original research articles and reviews on this topic.

Dr. Claudia Alessandri
Guest Editor

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.

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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

  • allergen
  • allergy diagnosis
  • IgE
  • immunoassays
  • mass spectrometry
  • allergen detection
  • new allergenic proteins
  • bioinformatics of allergens
  • food allergens

Published Papers (1 paper)

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Review

20 pages, 4214 KiB  
Review
Plant and Arthropod IgE-Binding Papain-like Cysteine Proteases: Multiple Contributions to Allergenicity
by Ivana Giangrieco, Maria Antonietta Ciardiello, Maurizio Tamburrini, Lisa Tuppo, Adriano Mari and Claudia Alessandri
Foods 2024, 13(5), 790; https://doi.org/10.3390/foods13050790 - 04 Mar 2024
Viewed by 928
Abstract
Papain-like cysteine proteases are widespread and can be detected in all domains of life. They share structural and enzymatic properties with the group’s namesake member, papain. They show a broad range of protein substrates and are involved in several biological processes. These proteases [...] Read more.
Papain-like cysteine proteases are widespread and can be detected in all domains of life. They share structural and enzymatic properties with the group’s namesake member, papain. They show a broad range of protein substrates and are involved in several biological processes. These proteases are widely exploited for food, pharmaceutical, chemical and cosmetic biotechnological applications. However, some of them are known to cause allergic reactions. In this context, the objective of this review is to report an overview of some general properties of papain-like cysteine proteases and to highlight their contributions to allergy reactions observed in humans. For instance, the literature shows that their proteolytic activity can cause an increase in tissue permeability, which favours the crossing of allergens through the skin, intestinal and respiratory barriers. The observation that allergy to PLCPs is mostly detected for inhaled proteins is in line with the reports describing mite homologs, such as Der p 1 and Der f 1, as major allergens showing a frequent correlation between sensitisation and clinical allergic reactions. In contrast, the plant food homologs are often digested in the gastrointestinal tract. Therefore, they only rarely can cause allergic reactions in humans. Accordingly, they are reported mainly as a cause of occupational diseases. Full article
(This article belongs to the Special Issue Allergenic Properties and Molecular Characteristics of Food Allergens)
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