Search Results (19)

Population growth and the depletion of natural resources have driven the incorporation of edible insects into the human food matrix. Despite their high nutritional value and the environmental benefits of insect farming compared to conventional protein sources, their consumption poses potential risks, including food allergies. Sensitization to insect allergens can occur through various exposure routes, with cross-reactions involving other foods and environmental allergens being well-documented. Vulnerable groups such as children and the elderly may have increased susceptibility not only because of genetic predisposition but also because of age-related physiological factors. This review explores the emerging risks of edible insect consumption, with a focus on children and the elderly. Age-related alterations in the gut microbiota, digestion, immune function, and overall physiology can facilitate the absorption of intact allergenic proteins and impair immune responses. Furthermore, the allergenic potential of insect proteins and their associated microbiota remains poorly characterized. Limited research exists on the effects of processing methods on these proteins. Consequently, incorporating edible insects into food products could present an additional allergenic risk, particularly for these vulnerable populations. Understanding these risks is essential for ensuring the safety and acceptance of edible insects as sustainable food ingredients. Full article

Peanut allergies, driven by sensitization to key allergens Ara h1, Ara h2, and Ara h3, present significant health risks, particularly in food processing and consumer settings where accidental exposure is frequent. To mitigate this risk, we developed AYA22AR321, a novel aptamer with selective, high-affinity binding to these allergens (Kd values: 0.5 nM for Ara h1, 14.5 nM for Ara h2, and 6.6 nM for crude peanut extract). Functional assays using RBL-2H3 (rat basophilic leukemia cell line) cells showed that AYA22AR321 significantly reduces IgE-mediated degranulation, indicating its potential to attenuate allergic responses. To translate these findings into practical use, we formulated an allergen-neutralizing spray, FISTOQ, containing AYA22AR321, which effectively neutralized peanut allergens on peanut-butter-contaminated surfaces. Stability tests confirmed that FISTOQ, comprising eco-friendly surfactant and preservative, maintains its allergen-neutralizing efficacy over time. Comprehensive safety assessments, including immunogenicity, cytotoxicity in human PBMCs, and mutagenicity via the Ames test, demonstrated that AYA22AR321 is non-immunogenic, non-cytotoxic, and non-mutagenic. This study establishes AYA22AR321 as a promising, targeted strategy for allergen control, providing a significant advancement in allergen mitigation and food safety for high-risk environments. Full article

Background: Tree nut allergy affects approximately 1% of the U.S. population and the prevalence is increasing. Walnut allergy is the most commonly reported tree nut allergy in the United States. This study aimed to investigate the IgE cross-reactivity between walnut allergen Jug r 4 and peanut allergen Ara h 3 in individuals with dual walnut and peanut allergies. Methods: Jug r 4 was purified from whole walnut extract and analyzed via western blot using anti-Ara h 3 antibodies alongside serum IgE from walnut allergic patients. Sera from individuals allergic to both peanuts and walnuts were utilized to examine peptide microarrays comprising synthetic overlapping 15 mer peptides, offset by five amino acids, of Ara h 3 and Jug r 4. These results were compared against computationally predicted IgE epitopes using the Structural Database for Allergic Proteins (SDAP). Additionally, SWISS-MODEL protein modeling software was employed to map IgE epitopes onto Ara h 3 and Jug r 4. Results: Our findings revealed previously unreported IgE epitopes for dual-allergic sera within both allergens, highlighting the locations of empirically determined and SDAP-predicted IgE epitopes. Conclusions: While six epitopes were predicted as cross-reactive, only three were frequently recognized by IgE in dual-allergic individuals, underscoring their potential significance in clinically relevant cross-reactivity. Full article

Peanut allergy, a significant public health issue, poses challenges due to its potential for life-threatening anaphylaxis and profound impact on quality of life. Traditional management approaches, including allergen avoidance and epinephrine administration, are effective in mitigating acute symptoms but do not address the underlying allergy or long-term disease burden. Recent advances in immunotherapy and biologics, as well as innovative technologies such as gene editing and microbiome modulation, have introduced promising pathways for desensitization and sustained unresponsiveness. This review provides a comprehensive exploration of emerging therapies for peanut allergy, including oral, sublingual, and epicutaneous immunotherapy, biologic agents, gene-editing techniques, and novel drug therapies. We discuss their mechanisms, clinical efficacy, and associated challenges, emphasizing the potential for these innovations to revolutionize peanut allergy treatment. Despite significant progress, barriers such as adverse reactions, cost, and limited access remain. Addressing these challenges through further research and standardization could transform the future of peanut allergy management. Full article

Peanut allergy presents a significant and growing public health concern, marked by its increasing prevalence and potential for severe allergic reactions. Traditional diagnostic methods, such as skin prick testing and serum IgE assays, serve as cornerstone approaches but often fall short in specificity, sensitivity, and risk stratification. This has driven the development of innovative diagnostic technologies, including component-resolved diagnostics, basophil activation tests, bead-based epitope assays, molecular diagnostics, and artificial intelligence applications. These advancements promise greater diagnostic precision, improved patient stratification, and tailored management strategies. However, challenges such as high costs, accessibility issues, and the need for standardized protocols hinder their widespread clinical adoption. This review explores the evolution of peanut allergy diagnostics, comparing traditional and emerging methodologies, and discusses their clinical implications, limitations, and future directions. The integration of advanced technologies with established approaches holds the potential to revolutionize peanut allergy diagnosis and management, ultimately enhancing patient care and outcomes. Full article

Seafood is a crucial source of nutrients, with global consumption steadily increasing. Among seafood-related allergies, shellfish are a significant cause of food allergy and anaphylaxis worldwide, affecting approximately 0.5–2.5% of the general population. While the majority of existing research has focused on crustaceans, allergic reactions to mollusks, including their clinical characteristics, remain poorly understood. In the Canary Islands, limpets (a type of marine gastropod) are widely consumed as part of the traditional cuisine. Despite isolated reports of limpet allergy, no large-scale studies or comprehensive clinical analyses have been published on this topic. A cohort of patients sensitized to limpets was analyzed: 66 patients were monosensitized to limpets (Group A), while 64 patients demonstrated additional sensitization to other shellfish (Group B). Limpet ingestion was associated with delayed and severe symptoms, including anaphylaxis and severe asthma. Notably, only 11.5% of patients in Group A tested positive for shellfish allergens using ALEX testing compared to 67.9% in Group B. The identification of protein bands in the 25–40 and 50–200 kDa molecular weight ranges in monosensitized patients provides a novel finding that differentiates this study from prior research. Our study represents the largest reported series of patients with documented limpet allergy to date. Full article

This review explores strategies for mitigating food allergies by treating foods with biopolymers, bioactive compounds, and food-grade enzymes. Biopolymers like chitosan, alginate, and pectin show potential in reducing the allergenic properties of food. Polyphenols such as quercetin, resveratrol, curcumin, and epigallocatechin gallate demonstrate promise as anti-inflammatory molecules that can lessen the symptoms and severity of allergic reactions. Enzymes, including proteases such as pepsin, papain, and bromelain, and transferases like transglutaminase, offer the potential to reduce the allergenic potency of proteins by various mechanisms, though more research is needed for the optimization and assessment of the safety and palatability of treated foods. Overall, this review offers insights into potential strategies to alleviate allergic reactions by reducing the allergenic properties of food proteins. Full article

Food allergies (FAs) represent a significant and growing global health issue, with increasing prevalence across different age groups. This review provides a comprehensive analysis of the epidemiology, mechanisms, and risk factors involved in FA development. Currently, FAs are estimated to affect 2% of the general population, with higher rates in children (~8%). However, these figures may be inaccurate because of the reliance on self-reported data and immunoglobulin E (IgE) testing, which may not reflect clinically confirmed cases. Environmental and genetic factors, including exposure to bacterial toxins, dietary habits, and the gut microbiota, play critical roles in FA development. Specifically, Staphylococcus aureus enterotoxins are implicated in disrupting intestinal barriers and enhancing immune sensitization to allergenic proteins. This immune dysregulation promotes Th2 responses and compromises regulatory T cell function, crucial elements in allergy pathogenesis. As the prevalence of FAs continues to rise, there is a pressing need for accurate diagnostic tools, heightened public awareness, and effective prevention strategies. Further research is needed to elucidate the specific role of bacterial toxins and other environmental factors in FA development to advance clinical management approaches. Full article

Food allergy, particularly peanut allergy (PA), is a growing health concern affecting millions globally. PA can lead to severe reactions, including fatal anaphylaxis. Despite the availability of FDA-approved therapies like Palforzia, a cure remains elusive. Current immunotherapies show promise but lack a definitive cure. This study applies an established computational biology tool to design aptamers targeting Ara h1 and Ara h2. The in silico design aims to streamline the selection process, enabling cost-effective and rapid identification of aptamer candidates. The developed aptamers (AYA22A, including AYA22AR321, AYA22AR211, and AYA22AR524), demonstrated efficacy in inhibiting degranulation of RBL-2H3 cells (rat basophilic leukemia cell line) in vitro. They showed promise in neutralizing peanut allergen-induced immune responses. The selected aptamers inhibited degranulation in RBL-2H3 cells, addressing concerns in raw peanuts. Moreover, these aptamers demonstrated stability and effectiveness in peanut plant seeds and commercial products. Our aptamers exhibited potential in modulating immune responses associated with peanut allergy. They influenced Th1/Th2 balance, indicating a role in cytokine regulation. In vitro studies also showed the aptamers’ impact on immune cell expression and cytokine production, resembling responses observed with established immunotherapies. The findings suggest AYA22A aptamers as a potential therapeutic option for peanut allergy, providing a basis for further in vivo investigations. Full article

Background: Food allergy management requires avoidance of allergenic food. While the direct costs of food allergy management have been described, avoidance may also contribute to time and opportunity costs. We aimed to conduct a scoping review of the peer-reviewed literature on the indirect costs of food allergy, and to characterise these costs through a series of fictitious case studies. Methods: We performed a scoping review, guided by Arskey and O’Malley’s methodological framework, and reported using the Preferred Reporting Items for Systematic Reviews and Meta-analyses extension for Scoping Reviews. Eligible studies included original, peer-reviewed, English language literature with no lower limits to publication dates, which addressed the indirect costs of food allergy, including time and opportunity costs. A search strategy was developed by content experts with experience performing multi-database scoping reviews. The search was performed on 10 July 2023, managed using Rayyan (Cambridge, USA), and screened for eligibility. Results: Searches yielded 104 articles. After deduplication, 96 articles were screened at the title and abstract level; 12 articles were included following full-text screening. Of these, three studies were performed on adults with food allergy, eight studies were based on data collected from caregivers of children with food allergy, and one study made use of data reflecting adults and caregivers of children with food allergy. Collectively, indirect costs were identified as higher amongst those with vs. without food allergy. The few studies on age and food allergy differences (e.g., type and number of food allergies, history of reaction) are equivocal. Conclusions: The limited body of peer-reviewed literature supports that food allergy commonly carries substantial indirect costs across diverse measurement tools, albeit with age-group differences. Full article

Most of the allergenic proteins from fruits identified so far belong to different families of pathogenesis-related (PR) proteins. These PR proteins have been classified in different families of structurally and functionally unrelated proteins, but the majority of all fruit allergens belong to three groups, in particular PR-5 thaumatin-like proteins (TLP), PR-10 Bet v 1-like proteins, and PR-14 non-specific lipid transfer proteins (nsTLP). Some allergenic proteins from fruits can also be found among PR-protein families of PR-2 β1,3-glucanase proteins, PR-3 chitinases I, II, IV–VII, and PR-8 chitinases III. In addition, other important fruit allergens occur in protein families unrelated to the PR-protein families, such as the profilins and the newly emerging group of gibberellin-regulated proteins (GBRP). Finally, proteins that belong to seed storage proteins from higher plants, including 2S albumins, 7S globulins (vicilin), and 11S globulins (legumin), must be retained as possible potential fruit allergens resulting from the unintended consumption of the seeds. Here, we present an overview of the structural organization, functional properties, and phylogenetical relationships among these different groups of fruit allergens, supporting the occurrence of cross-reactivity and cross-allergenicity often described between fruit allergens, and the corresponding allergens from vegetables and pollens. Full article

Celiac peptide-generating α- and γ-gliadins consist of a disordered N-terminal domain extended by an α-helical-folded C-terminal domain. Celiac peptides, primarily located along the disordered part of α- and γ-gliadin molecules, are nicely exposed and directly accessible to proteolytic enzymes occurring in the gastric (pepsin) and intestinal (trypsin, chymotrypsin) fluids. More than half of the potential celiac peptides identified so far in gliadins exhibit cleavage sites for pepsin. However, celiac peptides proteolytically truncated by one or two amino acid residues could apparently retain some activity toward HLA-DQ2 and HLA-DQ8 receptors in docking experiments. Together with the uncleaved peptides, these still active partially degraded CD peptides account for the incapacity of the digestion process to inactivate CD peptides from gluten proteins. In contrast, sourdough fermentation processes involve other proteolytic enzymes susceptible to the deep degradation of celiac peptides. In particular, sourdough supplemented by fungal prolyl endoproteases enhances the degrading capacities of the sourdough fermentation process toward celiac peptides. Nevertheless, since tiny amounts of celiac peptides sufficient to trigger deleterious effects on CD people can persist in sourdough-treated bread and food products, it is advisable to avoid consumption of sourdough-treated food products for people suffering from celiac disease. As an alternative, applying the supplemented sourdough process to genetically modified low gluten or celiac-safe wheat lines should result in food products that are safer for susceptible and CD people. Full article

Plants are essential for humans as they serve as a source of food, fuel, medicine, oils, and more. The major elements that are utilized for our needs exist in storage organs, such as seeds. These seeds are rich in proteins, show a broad spectrum of physiological roles, and are classified based on their sequence, structure, and conserved motifs. With the improvements to our knowledge of the basic sequence and our structural understanding, we have acquired better insights into seed proteins and their role. However, we still lack a systematic analysis towards understanding the functional diversity associated within each family and their associations with allergy. This review puts together the information about seed proteins, their classification, and diverse functional roles along with their associations with allergy. Full article

Introduction: The progression of allergy disorders is termed “atopic march.” Having one allergic disorder increases the likelihood of acquiring others. Asthma and food allergies often coexist. There are no thresholds for specific IgE (sIgE) associated with the presence of clinical symptoms. Each allergen shows a particular trend with age. Objective: Our study and analysis aim to identify food sensitization in children with asthma and evaluate its impact on asthma attacks and clinical control. Material and methods: As a part of a bigger study, 56 children (mean age 11.07 years (5.3–17.5), 38 boys, and 18 girls) with bronchial asthma were tested for total IgE and sIgE against food and inhalator allergens. All children performed baseline and post-BD spirometry and were assessed for asthma control. Results: In the studied population of children, sIgE against several food allergens was positive in the same patient. A significant correlation was found between the positive sIgE for milk and soy (p < 0.0001), for milk and egg yolk (p = 0.01), compared to milk and peanuts (p = 0.004), compared to egg yolk and fish (p < 0.0001), compared to egg yolk and casein (p < 0.001), and soy (p < 0.0001). The children who are positive for sIgE antibodies in cats, dogs, Cladosporium, Aspergillus, wormwood from aeroallergens and soy from food allergens have a higher risk of hospitalization for exacerbation of bronchial asthma. (p < 0.05). In the studied population, sensitization to food allergens among asthmatics does not contribute to the number of asthma attacks. Conclusions: Food sensitivity is associated with eczema, while mite sensitization is strongly associated with rhinitis and asthma. Food sensitization is not a risk factor for asthma exacerbation in children older than five years old. Full article

Gly m 7, a novel soybean allergen, was recently reported. In this study, we attempted to detect Gly m 7 in various soybeans and processed soybean foods using raised anti-Gly m 7 antibodies and enzyme-linked streptavidin, specifically binding to the biotin moiety of Gly m 7. There was a large difference in Gly m 7 levels in various soybean-processed foods. When Gly m 7 levels were determined, all cultivars contained this allergen almost completely, but the biotin moiety detected by streptavidin varied, suggesting that biotinylated levels of Gly m 7 might differ among cultivars. The thermal stability of Gly m 7 was determined by heating soybean extracts. During detection using anti-peptide antibodies, detectable intact Gly m 7 was gradually reduced by heating. Gly m 7 was not detected by peptide or biotin detection in worm-wounded soybeans. Soybeans were immersed in distilled water as a pretreatment step for germination, and Gly m 7 levels were compared by immersion time (4–96 h). Intact Gly m 7 was rapidly degraded in detection by both peptide and biotin moieties. This suggested that Gly m 7 was degraded by some protease(s) during germination. These results would be useful for understanding the properties or risk assessment of Gly m 7, a newly discovered soybean allergen. Full article