Gastro‐duodenal digestion products of the major peanut allergen Ara h 1 retain an allergenic potential

Eiwegger, Thomas; Rigby, Neil M.; Mondoulet, Lucie; Bernard, Hervé; Krauth, M.-T.; Boehm, Alexandra; Dehlink, Eleonora; Valent, Peter; Wal, J.-M.; Mills, E. N. Clare; Szépfalusi, Zsolt

doi:10.1111/j.1365-2222.2006.02565.x

Cited by 89 publications

(86 citation statements)

References 38 publications

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“…[10], [120], [121], [122] and [123] [124], [125], [126], [127], [128], [129] and [130] However, other studies at different shifting offsets, with different peptides sizes, or both revealed different sets of immunodominant sequential epitopes for the same allergens. [29], [124], [125], [126], [127], [130] and [131] Nevertheless, approaches to use these alleged immunodominant peptides for the risk assessment of life-threatening symptoms, as well as the prediction of persistence in food hypersensitivity, were apparently successful.…”

Section: Diagnosis Of Food Allergy With Synthetic Sequential Epitopesmentioning

confidence: 99%

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Steckelbroeck¹,

Ballmer‐Weber²,

Vieths³

2008

Journal of Allergy and Clinical Immunology

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This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both. However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both.However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. IgE-mediated and non-IgE-mediated syndromes, where IgE-mediated manifestations are responsible for the majority of food-induced, immediate-type, immune-mediated hypersensitivity reactions. 3 The development of an IgE-mediated response to food requires a series of molecular and cellular interactions, which involve antigenpresenting cells, T lymphocytes, and B lymphocytes. [4] and [5] Depending on the route of sensitization, food allergy is the result of either genuine reactivity to comestibles through the gastrointestinal tract (class I food allergens) or secondary sensitization to cross-reactive food allergens as a consequence of the initial reactivity to homologous pollen-related allergens (class II food allergens). [6] and [7] The majority of class I food allergens are heat stable and resistan...

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Section: Diagnosis Of Food Allergy With Synthetic Sequential Epitopesmentioning

confidence: 99%

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Steckelbroeck¹,

Ballmer‐Weber²,

Vieths³

2008

Journal of Allergy and Clinical Immunology

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“…The protocol followed was derived from prior reports (19,20,21). Lyophilized powders of enzymes and comparator proteins (α-casein from bovine milk, β-lactoglobulin from bovine milk, trypsin inhibitor from Glycine max) as well as reagents were purchased from Sigma-Aldrich.…”

Section: Methodsmentioning

confidence: 99%

“…We evaluated the digestibility of colicin proteins in the human GI tract using treatments with simulated gastric and intestinal fluids (SGF and SIF, respectively). Sequential exposure studies using physiological enzyme-to-substrate ratios were conducted to mimic the natural human GI tract conditions (19)(20)(21). For these studies, the colicins were first exposed to either SGF without or with pepsin, at a pepsin-to-colicin ratio of 1:20 on a weight basis, followed by exposure of the resultant hydrolysate products to SIF supplemented with trypsin and chymotrypsin at a ratio of 1:4:400 (trypsin:chymotrypsin:colicin peptides, on a weight basis).…”

Section: Gastric and Intestinal Proteases Digest Plant-produced Colicmentioning

confidence: 99%

Broad and efficient control of major foodborne pathogenic strains of Escherichia coli by mixtures of plant-produced colicins

Schulz

Stephan

Hahn

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

100

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Enterohemorrhagic Escherichia coli (EHEC) is one of the leading causes of bacterial enteric infections worldwide, causing ∼100,000 illnesses, 3,000 hospitalizations, and 90 deaths annually in the United States alone. These illnesses have been linked to consumption of contaminated animal products and vegetables. Currently, other than thermal inactivation, there are no effective methods to eliminate pathogenic bacteria in food. Colicins are nonantibiotic antimicrobial proteins, produced by E. coli strains that kill or inhibit the growth of other E. coli strains. Several colicins are highly effective against key EHEC strains. Here we demonstrate very high levels of colicin expression (up to 3 g/kg of fresh biomass) in tobacco and edible plants (spinach and leafy beets) at costs that will allow commercialization. Among the colicins examined, plant-expressed colicin M had the broadest antimicrobial activity against EHEC and complemented the potency of other colicins. A mixture of colicin M and colicin E7 showed very high activity against all major EHEC strains, as defined by the US Department of Agriculture/Food and Drug Administration. Treatments with low (less than 10 mg colicins per L) concentrations reduced the pathogenic bacterial load in broth culture by 2 to over 6 logs depending on the strain. In experiments using meats spiked with E. coli O157:H7, colicins efficiently reduced the population of the pathogen by at least 2 logs. Plant-produced colicins could be effectively used for the broad control of pathogenic E. coli in both plant-and animal-based food products and, in the United States, colicins could be approved using the generally recognized as safe (GRAS) regulatory approval pathway.antimicrobials | colicin | EHEC | food safety | plant-made recombinant proteins

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“…23,24 Ara h 1 is a readily digestible allergen, being digested to small peptide fragments by gastroduodenal digestion. 9,10 Even though Ara h 1 is a labile protein, Eiwegger et al 9 and Bøgh et al 10 showed that the digestion products of Ara h 1 retain allergenic potential, being able to sensitize as well as elicit allergic reactions. These studies indicated that aggregation of peptides may play a major role in maintaining allergenic activity.…”

Section: ■ Introductionmentioning

confidence: 99%

“…11−13 However, while pepsin stability as a part of an allergenicity assessment would still seem reasonable for the purpose of safety evaluation of most food proteins, we now know that for some allergenic proteins, this approach would be misleading. The milk allergen β-casein (Bos d 8) 7,14,15 as well as the peanut allergen Ara h 1 9,10 have several times been shown to be easily digestible food allergens.…”

Section: ■ Introductionmentioning

confidence: 99%

Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

Bøgh

Barkholt²,

Rigby

et al. 2012

J. Agric. Food Chem.

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The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.

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Gastro‐duodenal digestion products of the major peanut allergen Ara h 1 retain an allergenic potential

Abstract: Gastro-duodenal digestion fragments of Ara h 1 retain T cell stimulatory and IgE-binding and cross-linking properties of the intact protein.

Cited by 89 publications

References 38 publications

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Broad and efficient control of major foodborne pathogenic strains of Escherichia coli by mixtures of plant-produced colicins

Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

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