Peanut digestome: Identification of digestion resistant IgE binding peptides

Stasio, Luigia Di; Picariello, Gianluca; Mongiello, Mariantonietta; Nocerino, Rita; Canani, Roberto Berni; Bavaro, Simona L.; Monaci, Linda; Ferranti, Pasquale; Mamone, Gianfranco

doi:10.1016/j.fct.2017.06.029

Cited by 50 publications

(39 citation statements)

References 53 publications

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“…In earlier studies, peanut allergens were detected in breast milk, suggesting that digestion‐resistant immunoreactive fragments of peanut allergens can reach the circulation . Moreover, a recent study showed the presence of IgE‐reactive peptides after gastric/intestinal and brush border proteases digestion of whole peanut grains …”

Section: Discussionmentioning

confidence: 98%

“…Di Stasio et al reported that after gastrointestinal digestion, Ara h 1 was almost completely digested and no peptides larger than 6 kDa were detected. The most of Ara h 1 was proteolysed to a digestion‐resistant fragment of 60 kDa, and half of it was further digested, resulting in cascade pattern of Ara h 1 pepsin proteolysis (Figure A).…”

Section: Discussionmentioning

confidence: 99%

“…23 Moreover, a recent study showed the presence of IgE-reactive peptides after gastric/intestinal and brush border proteases digestion of whole peanut grains. 9 In vitro digestion studies with purified proteins reported dramatically higher protein digestibility than possible under physiological conditions. In addition, it is well known that pure proteins in solution can have different sensitivities to proteolysis compared to proteins adsorbed at oil-in-water interface owing to changes in the protein structure.…”

Section: Discussionmentioning

confidence: 99%

“…Plundrich et al investigated digestibility of light‐roasted peanut flour (12% fat) by pepsin and monitored degradation of allergens using 1‐dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (1D SDS‐PAGE). The study of Di Stasio et al investigated digestibility of proteins from the whole peanut by complete oral‐gastric‐intestinal‐brush border membrane proteases, but it did not report the gastric digestion products. Therefore, the immunoreactive protein/peptide species to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins remains unknown.…”

Section: Introductionmentioning

confidence: 99%

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Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

Prodić¹,

Stanić-Vučinić

Apostolović

et al. 2018

Clin Experimental Allergy

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

Prodić¹,

Stanić-Vučinić

Apostolović

et al. 2018

Clin Experimental Allergy

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“…Several previous studies have investigated digestibility of peanut allergens by in vitro simulated digestion (Burks, 2008;Di Stasio et al, 2017;Hazebrouck et al, 2012). Most of that related to the effects of processing or gastrointestinal digestion on immunoreactivity focused on purified peanut allergens or peanut extracts.…”

Section: Introductionmentioning

confidence: 99%

In vitro digestibility and immunoreactivity of thermally processed peanut

Rao

Tian

et al. 2018

Food and Agricultural Immunology

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Food processing affects the bioavailability and immunoreactivity of allergens. However, there was a lack of the combined study of the influence of the processing and gastrointestinal digestion on peanut matrix. Digestibility of peanut matrices was assessed by using an in vitro digestion model and monitored by SDS-PAGE, immunoblotting with polyclonal antibody and serum from peanut-allergic patients. The IgE-binding ability of digested samples will be assessed by immunoassay. Peanut proteins were digested by pepsin after only 2 min which was accompanied by a loss of high molecular weight proteins and enrichment in polypeptides with molecular weight lower than 10 kDa. Ara h 1 and Ara h 3 were partly proteolysis, and Ara h 2/6 containing a digestion-resistant fragment. All soluble fractions after 120 min gastric digestion reduced a higher IgE-binding ability than that after 10 min. Our findings provide a more realistic picture, considering the role of food processing and food matrix. ARTICLE HISTORY

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The Effect of the Food Matrix on the In Vitro Bio‐Accessibility and IgE Reactivity of Peanut Allergens

Rao

Baricevic

Bernard

et al. 2020

Molecular Nutrition Food Res

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ScopeFactors such as food processing, the food matrix, and antacid medication may affect the bio‐accessibility of proteins in the gastrointestinal tract and hence their allergenic activity. However, at present they are poorly understood.Methods and ResultsRoasted peanut flour was incorporated into either a chocolate dessert or cookie matrix and bio‐accessibility were assessed using an in vitro digestion system comprising a model chew and simulated gastric and duodenal digestion. Protein digestion was monitored by SDS‐PAGE and immunoreactivity analyzed by immunoblotting and immunoassay. IgE reactivity was assessed by immunoassay using serum panels from peanut‐allergic subjects. Roasted peanut flour proteins proved highly digestible following gastro‐duodenal digestion even when incurred into a food matrix, with only low molecular weight polypeptides of Mr < 8 kDa remaining. When gastric digestion was performed at pH 6.5 (simulating the effect of antacid medication), peanut proteins are not digested; subsequent duodenal digestion is also limited. IgE reactivity of the major peanut allergens Ara h 1, Ara h 2, and Ara h 6, although reduced, was retained after oral‐gastro‐duodenal digestion irrespective of digestion conditions employed.ConclusionPeanut allergen bio‐accessibility is unaffected by the dessert or cookie matrices whilst high intra‐gastric pH conditions render allergens more resistant to digestion.

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Peanut digestome: Identification of digestion resistant IgE binding peptides

Cited by 50 publications

References 53 publications

Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

In vitro digestibility and immunoreactivity of thermally processed peanut

The Effect of the Food Matrix on the In Vitro Bio‐Accessibility and IgE Reactivity of Peanut Allergens

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