ArticleClinical and translational allergy2018
Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure.
Article in Clinical and translational allergy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- The "Survivor Peptide" Hypothesis: Structural Resilience and Immunological Persistence of Food Allergens in the Gut-Mammary Axis.Nutrients · 2026Review
- Safety evaluation of blue galdieria extract as a food additive.EFSA journal. European Food Safety Authority · 2026Article
- Identification and Characterization of a Pepsin- and Chymotrypsin-Resistant Peptide in the α Subunit of the 11S Globulin Legumin from Common Bean (Journal of agricultural and food chemistry · 2024Article
- Spatiotemporal proteolytic susceptibility of allergens: positive or negative effects on the allergic sensitization?Frontiers in allergy · 2024Review
- Slow alignment of GMO allergenicity regulations with science on protein digestibility.GM crops & food · 2022Article
- Fish Processing and Digestion Affect Parvalbumins Detectability in Gilthead Seabream and European Seabass.Animals : an open access journal from MDPI · 2022Article
- Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?Clinical reviews in allergy & immunology · 2022Review
- Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?Clinical reviews in allergy & immunology · 2022Review
- Differences in Linear Epitopes of Ara h 9 Recognition in Peanut Allergic and Tolerant, Peach Allergic Patients.Frontiers in allergy · 2022Article
- Impact of Food Matrices on Digestibility of Allergens and Poorly Allergenic Homologs.Frontiers in allergy · 2022Article
- Scientific Opinion on development needs for the allergenicity and protein safety assessment of food and feed products derived from biotechnology.EFSA journal. European Food Safety Authority · 2022Article
- Mass spectrometric analysis of digesta does not improve the allergenicity assessment of GM crops.Transgenic research · 2021Article
- Statement onEFSA journal. European Food Safety Authority · 2021Article
- Erroneous Belief that Digestive Stability Predicts Allergenicity May Lead to Greater Risk for Novel Food Proteins.Frontiers in bioengineering and biotechnology · 2021Article
- Abundance and Stability as Common Properties of Allergens.Frontiers in allergy · 2021Review
- Functional Dyspepsia and Food: Immune Overlap with Food Sensitivity Disorders.Current gastroenterology reports · 2020Review
- Accumulation of storage proteins in plant seeds is mediated by amyloid formation.PLoS biology · 2020Article
- Are Faba Bean and Pea Proteins Potential Whey Protein Substitutes in Infant Formulas? An In Vitro Dynamic Digestion Approach.Foods (Basel, Switzerland) · 2020Article
- Evidence runs contrary to digestive stability predicting protein allergenicity.Transgenic research · 2020Article
- Article
Corrections and comments
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Authors and funding
21 authors at 11 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSusceptibility to pepsin digestion of candidate transgene products is regarded an important parameter in the weight-of-evidence approach for allergenicity risk assessment of genetically modified crops. It has been argued that protocols used for this assessment should better reflect physiological conditions encountered in representative food consumption scenarios.
aimTo evaluate whether inclusion of more physiological conditions, such as sub-optimal and lower pepsin concentrations, in combination with pancreatin digestion, improved the performance of digestibility protocols used in characterization of protein stability.
methodsFour pairs of established allergens and their related non/weakly-allergenic counterparts (seed albumins, muscle tropomyosins, plant lipid transfer proteins [LTP] and collagens) plus fish parvalbumin, were subjected to nine combinations of pH (1.2-2.5-4.0) and pepsin-to-protein ratio (PPR: 10-1-0.1 U/µg) for pepsin digestion, followed by pancreatin digestion in the presence of bile salts. Digestion was monitored by SDS-PAGE in conjunction with Coomassie staining and immunoblotting using rabbit antisera and human IgE.
resultsAt pH 4.0 and at PPR 0.1 most proteins, both allergen and non-allergen, were highly resistant to pepsin. Under conditions known to favor pepsin proteolysis, the established major allergens Ara h 2, Pru p 3 and Pen a 1 were highly resistant to proteolysis, while the allergen Cyp c 1 was not. However, this resistance to pepsin digestion only made Ara h 2 and to a lesser extent Pen a 1 and Pru p 3 stand out compared to their non-allergenic counterparts. Largely irrespective of preceding pepsin digestion conditions, pancreatin digestion was very effective for all tested proteins, allergens and non-allergens, except for Cyp c 1 and bovine collagen.
conclusionsSub-optimal pH, low pepsin-to protein ratio, and sequential pepsin and pancreatin digestion protocols do not improve the predictive value in distinguish allergens from non-allergens. Digestion conditions facilitating such distinction differ per protein pair.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.