Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity

Blanc, Fany; Vissers, Yvonne M.; Adel‐Patient, Karine; Rigby, Neil M.; Mackie, Alan; Gunning, A. Patrick; Wellner, Nikolaus; Skov, Per Stahl; Przybylski-Nicaise, Laetitia; Ballmer‐Weber, Barbara; Zuidmeer-Jongejan, Laurian; Szépfalusi, Zsolt; Ruinemans-Koerts, Janneke; Jansen, A.P.; Bernard, Hervé; Wal, J.-M.; Savelkoul, H.F.J.; Wichers, Harry J.; Mills, E. N. Clare

doi:10.1002/mnfr.201100251

Cited by 107 publications

(85 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Baking, roasting, and various forms of food processing are known to affect the antigenicity of peanuts [24,25], and, as a result, profiling processed foods can be problematic if the standards are not identically processed. Fortunately, as there were no indications that the ground cumins (A and B) were processed, the standards used to generate the data in Table 2 should be directly applicable to these two cumin samples.…”

Section: Cumin Profilingmentioning

confidence: 99%

Multiplex detection of food allergens and gluten

et al. 2015

View full text Add to dashboard Cite

To help safeguard the food supply and detect the presence of undeclared food allergens and gluten, most producers and regulatory agencies rely on commercial test kits. Most of these are ELISAs with a few being PCR-based. These methods are very sensitive and analyte specific, requiring different assays to detect each of the different food allergens. Mass spectrometry offers an alternative approach whereby multiple allergens may be detected simultaneously. However, mass spectrometry requires expensive equipment, highly trained analysts, and several years before a quantitative approach can be achieved. Using multianalyte profiling (xMAP®) technology, a commercial multiplex test kit based on the use of established antibodies was developed for the simultaneous detection of up to 14 different food allergens plus gluten. The assay simultaneously detects crustacean seafood, egg, gluten, milk, peanut, soy, and nine tree nuts (almond, Brazil nut, cashew, coconut, hazelnut, macadamia, pine nut, pistachio, and walnut). By simultaneously performing multiple tests (typically two) for each analyte, this magnetic bead-based assay offers built-in confirmatory analyses without the need for additional resources. Twenty-five of the assays were performed on buffer extracted samples, while five were conducted on samples extracted using reduced-denatured conditions. Thus, complete analysis for all 14 allergens and gluten requires only two wells of a 96-well microtiter plate. This makes it possible to include in a single analytical run up to 48 samples. All 30 bead sets in this multiplex assay detected 5 ng/mL of food allergen and gluten with responses greater than background. In addition, 26 of the bead sets displayed signal/noise ratios of five or greater. The bead-based design makes this 30-plex assay expandable to incorporate new antibodies and capture/detector methodologies by ascribing these new detectors to any of the unassigned bead sets that are commercially available.

show abstract

Section: Cumin Profilingmentioning

confidence: 99%

Multiplex detection of food allergens and gluten

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Some method of facilitated transport (e.g. endocytosis) would be likely, especially given the larger size of Ara h 1, and its tendency to aggregate into insoluble complexes, especially when heated [1,10,34,35]. It has been previously demonstrated that soluble molecules are more easily absorbed across the intestinal epithelium compared to larger insoluble aggregates, which are limited to M cell passage [36].…”

Section: Discussionmentioning

confidence: 99%

Peanut Allergens Alter Intestinal Barrier Permeability and Tight Junction Localisation in Caco-2 Cell Cultures¹

Price

Ackland²,

Burks³

et al. 2014

Cell Physiol Biochem

View full text Add to dashboard Cite

Background/Aims: Allergen absorption by epithelia may play an important role in downstream immune responses. Transport mechanisms that can bypass Peyer's patches include transcellular and paracellular transport. The capacity of an allergen to cross via these means can modulate downstream processing of the allergen by the immune system. The aim of this study was to investigate allergen-epithelial interactions of peanut allergens with the human intestinal epithelium. Methods: We achieved this using the human Caco-2 cell culture model, exposed to crude peanut extract. Western and immunofluorescence analysis were used to identify the cellular and molecular changes of peanut extract on the intestinal epithelium. Results: Following exposure of Caco-2 cells to peanut extract, binding of the peanut allergens Ara h 1 and Ara h 2 to the apical cellular membrane and transcytosis across the monolayers were observed. Additionally, the co-localisation of the transmembrane tight junction proteins occludin, JAM-A and claudin-1, with the intracellular adhesion protein ZO-1 was modified. Conclusion: Disruption of Caco-2 barrier integrity through tight junction disruption may enable movement of peanut proteins across the intestinal epithelium. This accounts for peanut's increased allergenicity, compared to other food allergens, and provides an explanation for the potency of peanut allergens in immune response elicitation.

show abstract

“…The compound formed by Ara h 1 and Ara h 6 has a strong immunoreactivity when compared with the native allergen (Guillon, Bernard, Drumare, Hazebrouck, & Adel-Patient, 2016). It has also been reported by Blanc et al (2011) that complex branched aggregates of natural Ara h 1 were produced through boiling, and thus caused a relatively decreased sensitivity. Similar to this result, our data showed that rAra h 1 tends to aggregate after 20 min of heating (Figure 4(A,B)).…”

Section: Discussionmentioning

confidence: 90%

“…However, more extreme thermal processing such as roasting at 140°C appeared to enhance IgE-binding capacity of Ara h 1 (Rao et al, 2016). According to Blanc et al (2011), Ara h 1 boiled in the absence or presence of glucose produced aggregates and thus maintained a relatively lower sensitivity. Researchers utilized various thermal methods to treat peanut kernel or a certain allergen and explored the influence of heat treatment on the immunoreactivity, and the results were not consistent with each other.…”

Section: Introductionmentioning

confidence: 99%

Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1

Tian

Rao

Tao

et al. 2018

Food and Agricultural Immunology

View full text Add to dashboard Cite

Ara h 1 is a key peanut allergen and its activity is significantly affected by protein intrinsic structure which is found to be regulated by heat treatment, although the molecular basis for this regulation has remained largely unknown. Here, we explored the effect of boiling on the structure and allergenicity of recombinant peanut protein Ara h 1 (rAra h 1). rAra h 1 was purified from E. Coli BL21(DE3) plysS cells and structurally studied. According to the results, rAra h 1 undergoes degradation during the heating process, and the aggregation of fragments happened after 20 min of heating. An increased surface hydrophobic index and a decreased content of α-helixes were found in rAra h 1, indicating a looser protein structure of rAra h 1 caused by heat treatment. Destroyed epitopes during protein degradation and aggregation could be a mechanism of reducing the allergenic nature of rAra h 1 by heat treatment. ARTICLE HISTORY

show abstract

Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity

Cited by 107 publications

References 24 publications

Multiplex detection of food allergens and gluten

Multiplex detection of food allergens and gluten

Peanut Allergens Alter Intestinal Barrier Permeability and Tight Junction Localisation in Caco-2 Cell Cultures¹

Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1

Contact Info

Product

Resources

About

Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity

Cited by 107 publications

References 24 publications

Multiplex detection of food allergens and gluten

Multiplex detection of food allergens and gluten

Peanut Allergens Alter Intestinal Barrier Permeability and Tight Junction Localisation in Caco-2 Cell Cultures1

Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1

Contact Info

Product

Resources

About

Peanut Allergens Alter Intestinal Barrier Permeability and Tight Junction Localisation in Caco-2 Cell Cultures¹