Different thermal processing effects on peanut allergenicity

Zhang, Tong; Shi, Yunfeng; Zhao, Yanqing; Wang, Jianying; Wang, Minjia; Niu, Bing; Qin, Chen

doi:10.1002/jsfa.9430

Cited by 37 publications

(42 citation statements)

References 33 publications

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“…42 The decreased α-helix content of Ara h 2 and the increased random coil content after roasting were found, as previously reported. 43 In fact, the low content of the α-helix was also found on thermally processed purified Ara h 1. 44 For Act d 2, another heat-stable protein, thermal stress significantly affected its secondary structure, losing the α-helix and obtaining more random coils.…”

Section: Discussionmentioning

confidence: 94%

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Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix

Chang

Zhou

Zhang

et al. 2022

J. Agric. Food Chem.

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Peanut allergy is the leading pediatric food allergy. Many attempts have been made to reduce its allergenicity by processing. After roasting, Ara h 2 and its derivatives in the matrix were isolated by immunoaffinity chromatography (IAC). The structure and allergenicity of Ara h 2 were analyzed by circular dichroism, mass spectrometry (MS), western blotting, the enzymelinked immunoassay, and cell modeling. Our results showed that a large portion of Ara h 2 was fragmented and cross-linked. Ara h 2 monomers accounted for only 13% of the total proteins after IAC purification. In addition, the structure of Ara h 2 changed after roasting. In addition to methylation and oxidation modification, the disulfide bonds of Ara h 2 were found to be rearranged after roasting. In the conformational structure of Ara h 2, the content of the α-helix decreased from 27.1 to 21.6% after roasting, while the content of the random coil increased from 29.1 to 34.3%. Six cleavage sites of trypsin were exposed, while three were covered. In terms of allergenicity, most of the cross-linking products were not recognized by patients' sera. Only one faint band around 40 kDa was observed in our blotting. For Ara h 2 monomers, roasting enhanced their IgE binding capacity and ability to stimulate the degranulation of basophils. The potential allergenicity increase of Ara h 2 monomers did not reflect the allergenicity change of Ara h 2 in the matrix due to the amount and property of its derivatives after roasting.

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Section: Discussionmentioning

confidence: 94%

“…42 The absorbance value at 280 nm increased for Ara h 2 extracted from the roasted peanut. 43 The structural changes of Ara h 2 have been shown to change its digestibility. 5,46 Ara h 2 is a trypsin inhibitor, and roasting was reported to decrease its digestibility.…”

Section: Discussionmentioning

confidence: 99%

Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix

Chang

Zhou

Zhang

et al. 2022

J. Agric. Food Chem.

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“…Main allergens include Ara h 1, Ara h 2, Ara h 3, and Ara h 6. 3 In its natural state, Ara h 3 is a hexamer protein with multiple subunits 4 and a molecular weight of more than 400 kDa. Four main bands of Ara h 3 can be observed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) to denature and separate the protein subunits.…”

Section: Introductionmentioning

confidence: 99%

Effect of roasted peanut allergen Ara h 3 protein on the sensitization of Caco‐2 cells

et al. 2021

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BACKGROUND: Roasted peanut is widely loved as a kind of food with rich taste. However, peanut allergy is one of the major threats to human health, which affects about 5% of children and 1.4-2% of adults in the world. RESULTS: To evaluate the sensitization mechanism of peanut allergen Ara h 3, Caco-2 cells as the model, which has the similar structure and function to differentiated small intestinal epithelial cells. Compared with Ara h 3-raw (purified from raw peanut) group, more significant results such as the inhibited Caco-2 cell viability and proliferation, the increased secretion of reactive oxygen species (ROS) and the decreased transepithelial electrical resistance were obtained in Ara h 3-roasted (purified from roasted peanut) group. Accordingly, oxidative stress and NF-κB signaling pathway were more imbalanced, which lead to the increased of thymic stromal lymphopoietin (TSLP), interleukin 6 (IL-6), IL-8 and monocyte chemotactic protein 1 (MCP-1). Then, the gene expression of tight junction proteins ZO-1, occludin and JAM-1 were reduced, which proved that the integrity of the Caco-2 monolayer barrier is severely damaged.CONCLUSION: These finding identify the mechanisms of the allergenicity of roasted peanut allergy proteins are probably associated with intestinal uptake and cytokine dependent allergies. The aggravated allergic reaction might be caused by the increment of TSLP, IL-6, IL-8 and MCP-1 due to the activated NF-κB signaling pathway, and the enhanced transport of Ara h 3-roasted protein by Caco-2 monolayer.

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“…Heating is known to induce protein denaturation, leading to reduced allergenicity of food proteins under normal physiological conditions [10]. However, in vitro studies have shown that allergenicity of food proteins is enhanced by heating [17,18]. These contradictory observations could be explained by their differential susceptibility to digestion and/or absorption in the gastrointestinal tract [14,23].…”

Section: Discussion/conclusionmentioning

confidence: 99%

“…Thermal processing of OVA is known to enhance its allergenicity [17,18], suggesting different potencies of naive OVA (nOVA) and heated OVA (hOVA) for MC desensitization in vitro. Therefore, we compared the consequences of nOVA and hOVA desensitization.…”

Section: Desensitization Efficiency Differs Between Naive and Heated Ovamentioning

confidence: 99%

FcεRI Cluster Size Determines Effective Mast Cell Desensitization without Effector Responses in vitro

Nagata¹,

Suzuki²

2021

Int Arch Allergy Immunol

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Background: Allergen-specific desensitization of mast cell (MC) IgE receptors (FcεRI) is an important mechanism of allergen-specific immunotherapy that enables tolerance induction via systemic desensitization. Experimental in vitro IgE-mediated MC desensitization is a potential tool to understand the molecular mechanisms underlying this therapy. Desensitized MCs exhibit internalized IgE and its FcεRI receptors in response to suboptimal doses of allergen without provoking activation. The ovalbumin (OVA) allergen exhibits altered allergenicity upon heat treatment. MC reactions are fundamentally regulated by allergen features (i.e., allergenicity); however, the effects of allergenicity on desensitization remain unclear. Objectives: This study aimed to examine the impact of allergenicity on the establishment of in vitro MC desensitization using naive OVA (nOVA) and heated OVA (hOVA), which could induce varying MC effector responses. Method: Bone marrow-derived MCs (BMMCs) were sensitized with OVA-specific IgE, desensitized with sequentially increasing doses of nOVA or hOVA at 10-min intervals, and challenged with nOVA. To evaluate desensitization, the cell surface expression level and subcellular localization of FcεRI-bound IgE were analyzed before and after the final nOVA challenge. MC activation was determined by measuring the release of β-hexosaminidase into supernatants. Results: Desensitized cells exhibited impaired activation following OVA challenge. Both nOVA and hOVA induced BMMC desensitization under different conditions. Formation of small IgE-FcεRI cluster BMMCs, which adequately represent the desensitized state, was significant. The size of the internalized IgE-FcεRI clusters might be correlated with the desensitized state of MCs. Conclusions: We demonstrate that the optimal size of IgE-FcεRI clusters for in vitro BMMC desensitization differed significantly depending on allergenicity, and the efficacy of desensitization was reflected by IgE-FcεRI cluster formation. Our study provides information on the characteristics of IgE-FcεRI internalization for successful desensitization in vitro.

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Different thermal processing effects on peanut allergenicity

Cited by 37 publications

References 33 publications

Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix

Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix

Effect of roasted peanut allergen Ara h 3 protein on the sensitization of Caco‐2 cells

FcεRI Cluster Size Determines Effective Mast Cell Desensitization without Effector Responses in vitro

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