<scp>A</scp>ra h 1 structure is retained after roasting and is important for enhanced binding to <scp>I</scp>g<scp>E</scp>

Nesbit, Jacqueline B.; Hurlburt, Barry K.; Schein, Catherine H.; Cheng, Hsiaopo; Wei, Hui; Maleki, Soheila J.

doi:10.1002/mnfr.201100815

Cited by 38 publications

(43 citation statements)

References 42 publications

(92 reference statements)

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“…According to the present study, YM+M seeds have a Sin a 1 level of 1.05-1.37 g/100 g seeds (16.59-23.16 g/100 g of napin). Similarly, in a study 35 using the major peanut allergen, Ara h 1, the isolated Ara h 1 from roasted peanuts showed enhanced allergenic properties compared to that of unroasted peanuts although the tertiary and secondary structure elements of both proteins were similar. The level of Sin a 1 of the seeds received for this study was below the range of 2.65 to 5.98 g/100 g of seeds which was reported for commercial varieties produced in Saskatchewan in our previous study and could represent the effect of environmental factors and seed variety.…”

Section: Binding Of Sin a 1 Ae-abmentioning

confidence: 90%

Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

et al. 2015

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This study investigated the structural stability of yellow mustard (YM, Sinapis alba L.) napin and the changes of its Sin a 1 anti-epitope antibody-binding ability during myrosinase enzyme inactivation process. The food industry uses myrosinase-inactive non-pungent YM for uses beyond spice applications. Napin was isolated from seeds received from an industrial processor before (YM + M) and after (YM - M) myrosinase inactivation. Secondary and tertiary structural features and surface hydrophobicity parameters of napin were analyzed. The Sin a 1 content in YM seeds and the stability of Sin a 1-containing napin during simulated in vitro gastrointestinal (GI) digestion were determined by a non-competitive indirect enzyme-linked immunosorbent assay using the Sin a 1 anti-epitope antibody (AE-Ab) as the primary Ab. YM napin retained the dominant alpha-helical components of secondary and tertiary structure folds during this process. YM - M napin showed changes in hydrophobicity parameters of the molecules and binding ability of AE-Ab: 2.19 ± 0.48 g per 100 g of YM - M seeds vs. 1.49 ± 0.16 g per 100 g YM + M seeds. YM - M proteins were more susceptible for in vitro GI digestion and also showed a 30% reduction in AE-Ab binding ability upon digestion of napins. This suggests that the myrosinase inactivation process has induced the surface modification of napin, exposing Sin a 1 epitope, leading to an increase in AE-Ab binding. However, the epitope region of YM - M napin showed improved susceptibility for hydrolysis during GI digestion resulting in fewer available epitope regions, suggesting a possible reduction in napin immune reactivity.

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Section: Binding Of Sin a 1 Ae-abmentioning

confidence: 90%

Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

et al. 2015

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“…This leads to more peanut protein surviving digestion, and, therefore, more whole protein entering the gut. The surviving proteins or fragments thereof are likely to maintain structural elements [81]. This probably stimulates the immune system by both the adaptive immune system via IgE binding and the innate immure response through lectin receptors and receptors such as RAGE recognizing the glycosylation and glycation modifcations, respectively.…”

Section: Molecular Modificationsmentioning

confidence: 99%

The Molecular Basis of Peanut Allergy

Mueller

Maleki

Pedersen

2014

Curr Allergy Asthma Rep

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Peanut allergens can trigger a potent and sometimes dangerous immune response in an increasing number of people. The molecular structures of these allergens form the basis for understanding this response. This review describes the currently known peanut allergen structures and discusses how modifications both enzymatic and non-enzymatic affect digestion, innate immune recognition, and IgE interactions. The allergen structures help explain cross-reactivity among allergens from different sources, which is useful in improving patient diagnostics. Surprisingly, it was recently noted that related short peptide sequences among peanut allergens could also be a source of cross-reactivity. The molecular features of peanut allergens continue to inform predictions and provide new research directions in the study of allergic disease.

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“…It is commonly agreed that allergens from roasted peanut have an increased capacity to bind preformed peanut-specific IgE compared to raw peanut, as this has been demonstrated for several peanut allergens, including the Ara h 3 samples of this study [3, 6, 7, 18]. However, the interaction of such thermal-processed peanut allergens with DCs in the sensitization phase of allergy is poorly understood.…”

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confidence: 95%

“…This result indicates that increased and/or different receptors could be involved in the enhanced uptake and internalization of Ara h 3-roas by MDDCs. During roasting, chemical reactions occur, which can modify peanut allergens and their interaction with the immune system [6, 7, 9]. One of the reactions that may favor this mechanism is the Maillard reaction, which is a nonenzymatic chemical reaction that occurs during roasting that implies modifications of amino groups of proteins by reducing sugars, thereby generating glycated proteins called advanced glycation end (AGE) adducts [3, 19].…”

mentioning

confidence: 99%

“…Allergens from roasted peanut have a higher capacity to bind peanut-specific IgE from the sera of peanut-allergic patients than raw, boiled, or fried peanut [3-5]. The chemical reactions that occur during roasting seem to play a pivotal role in the increased capacity of peanut allergens to bind peanut-specific IgE in the elicitation phase of the allergic response [3, 6, 7]. However, little information is available regarding the role of roasted peanut allergens in the initial phase of allergy, the so-called “sensitization” phase, where an immunological priming towards an allergic response takes place.…”

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Differences in the Uptake of Ara h 3 from Raw and Roasted Peanut by Monocyte-Derived Dendritic Cells

Cabanillas

Maleki

Cheng

et al. 2018

Int Arch Allergy Immunol

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Roasting has been implicated in the increase of peanut allergenicity due to the chemical reactions that occur during the process. However, this increase is not fully understood, and little information is available regarding the role of roasted peanut allergens in the initial phase of allergy, where dendritic cells (DCs) play a key role. We sought to analyze differences in the internalization of Ara h 3 from raw and roasted peanut by immature monocyte-derived DCs (MDDCs) and the implication of the mannose receptor in the uptake. Ara h 3 was purified from raw and roasted peanut (Ara h 3-raw and Ara h 3-roas) and labeled with a fluorescent dye. The labeled allergens were added to MDDCs obtained from 7 donors and internalization was analyzed after 10, 30, and 120 min by flow cytometry. In parallel, mannan, which blocks the mannose receptor, was added 30 min before adding the labeled allergens. Results showed that the internalization of Ara h 3-roas by MDDCs was significantly increased at every time point. However, the increase in the internalization of Ara h 3-raw was only significant after 2 h of incubation. Ara h 3-roas had an enhanced capacity to be internalized by MDDCs in comparison with Ara h 3-raw at every time point. Blocking the mannose receptor decreased the internalization of Ara h 3-roas but not Ara h 3-raw. In conclusion, the internalization of Ara h 3-roas by the MDDCs is enhanced when compared to Ara h 3-raw, and the mannose receptor might be implicated in this enhancement.

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Ara h 1 structure is retained after roasting and is important for enhanced binding to IgE

Abstract: Enhanced IgE binding to roasted Ara h 1 could be due to alterations such as chemical modifications to individual amino acids or increased epitope exposure. IgE binding is significantly reduced with loss of structure.

Cited by 38 publications

References 42 publications

Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

The Molecular Basis of Peanut Allergy

Differences in the Uptake of Ara h 3 from Raw and Roasted Peanut by Monocyte-Derived Dendritic Cells

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