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Research Article | Open Access

Study on mechanism of increased allergenicity induced by Ara h 3 from roasted peanut using bone marrow-derived dendritic cells

MinJia Wanga,1Shuo Wanga,1Xiaodong SunbZhiRui Denga( )Bing NiuaQin Chena( )
School of Life Sciences, Shanghai University, Shanghai 200444, China
Medical School, Shanghai University, Shanghai 200444, China

1 Authors contributed equally to this article.Peer review under responsibility of KeAi Communications Co., Ltd.]]>

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Abstract

Little information was so far available about allergenic mechanism of the roasted peanut allergens during initial stages of allergy. The purpose of this study was to determine the influence of roasting (150 °C, 20 min) on biochemical and biological properties of Ara h 3, a major peanut allergen. Allergenicity of roasted peanut emulsion to mice, differences in uptakes between Ara h 3 purified from raw peanuts (named as Ara h 3-Raw) and that purified from roasted peanuts (named as Ara h 3-Roasted) by bone marrow-derived dendritic cells (BMDCs) and the implication of cell surface receptors involving in uptake, and changes in glycosylation and structure of Ara h 3 after roasting were analyzed in this study. This study suggested that roasting increased allergenicity of peanut to BALB/c mice. Maillard reaction and structural changes of Ara h 3 induced by roasting significantly altered the uptake of Ara h 3-Roasted by BMDCs, and modified Ara h 3 fate in processes involved in immunogenicity and hyper allergenicity, indicating that food processing pattern can change food allergenicity.

References

[1]

B.I. Nwaru, L. Hickstein, S.S. Panesar, et al., Prevalence of common food allergies in Europe: a systematic review and meta-analysis, Allergy 69 (2014) 992-1007. https://doi.org/10.1111/all.12423.

[2]

A.M. Branum, S.L. Lukacs, Food allergy among U.S. children: trends in prevalence and hospitalizations, Nchs. Data. Brief. 10 (2008) 1-18.

[3]

S.A. Bock, A. Muñoz-Furlong, H.A. Sampson, Further fatalities caused by anaphylactic reactions to food, 2001-2006, J. Allergy Clin. Immunol. 119 (2007) 1016-1018. https://doi.org/10.1067/mai.2001.11203.

[4]

H. Li, J. Yu, M. Ahmedna, et al., Reduction of major peanut allergens Ara h 1 and Ara h 2, in roasted peanuts by ultrasound assisted enzymatic treatment, Food Chem. 141 (2013) 762-768. https://doi.org/10.1016/j.foodchem.2013.03.049.

[5]

B. Cabanillas, U. Jappe, N. Novak, Allergy to peanut, soybean, and other legumes: recent advances in allergen characterization, stability to processing and IgE cross-reactivity, Mol. Nutr. Food Res. 62 (2018) 1700446. https://doi.org/10.1002/mnfr.201700446.

[6]

P.A. Eigenmann, A.W. Burks, G.A. Bannon, et al., Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies, J. Allergy Clin. Immunol. 98 (1996) 969-978. https://doi.org/10.1016/S0091-6749(96)80014-5.

[7]

P. Rabjohn, E.M. Helm, J.S. Stanley, et al., Molecular cloning and epitope analysis of the peanut allergen Ara h 3, J. Clin. Invest. 103 (1999) 535-542. https://doi.org/10.1172/JCI5349.

[8]

T. Kleber-Janke, R. Crameri, U. Appenzeller, et al., Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology, Int. Arch. Allergy Immunol. 119 (1999) 265-274. https://doi.org/10.1159/000024203.

[9]

C.M. Hebling, M.M. Ross, J.H. Callahan, et al., Size-selective fractionation and visual mapping of allergen protein chemistry in arachis hypogaea, J. Proteome Res. 11 (2012) 5384-5395. https://doi.org/10.1021/pr300617a.

[10]

T. Jin, A. Howard, Y.Z. Zhang, Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3, Acta Crystallogr. Sect. F: Struct. Biol. Commun. 63 (2007) 848-851. https://doi.org/10.1107/S1744309107041176.

[11]

D.K. Chu, Z. Mohammed-Ali, R. Jimenez-Saiz, et al., T helper cell IL-4 drives intestinal Th2 priming to oral peanut antigen, under the control of OX40L and independent of innate-like lymphocytes, Mucosal Immunol. 7 (2014) 1395-1404. https://doi.org/10.1038/mi.2014.29.

[12]

L. Tordesillas, R. Goswami, S. Benede, et al., Skin exposure promotes a Th2-dependent sensitization to peanut allergens, J. Clin. Invest. 124 (2014) 4965-4975. https://doi.org/10.1172/JCI75660.

[13]

P. Rupa, and Y. Mine, Comparison of glycated ovalbumin-monosaccharides in the attenuation of ovalbumin-induced allergic response in a BALB/c mouse model, J. Agric. Food. Chem. 67 (2019) 8138-8148. https://doi.org/10.1021/acs.jafc.9b02132.

[14]

M. Perusko, M. van Roest, D. Stanic-Vucinic, et al., Glycation of the major milk allergen beta-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation, Mol. Nutr. Food Res. 62 (2018). https://doi.org/10.1002/mnfr.201800341.

[15]

M. Teodorowicz, J. van Neerven, H. Savelkoul, Food processing: the influence of the maillard reaction on immunogenicity and allergenicity of food proteins, Nutrients 9 (2017) 835-853. https://doi.org/10.3390/nu9080835.

[16]

J.J. Dolence, T. Kobayashi, K. Iijima, et al., Airway exposure initiates peanut allergy by involving the IL-1 pathway and T follicular helper cells in mice, J. Allergy Clin. Immunol. 142 (2018) 1144-1185. https://doi.org/10.1016/j.jaci.2017.11.020.

[17]
M. Wang, B. Niu, Z. Deng, et al., Purification of peanut allergen protein Ara h 3, BIBE 2019; The Third International Conference on Biological Information and Biomedical Engineering, VDE, 2019, pp. 374-377.
[18]

C. Prado, V. Ugalde, H. Gonzalez, et al., STAT3 activation in combination with NF-KappaB inhibition induces tolerogenic dendritic cells with high therapeutic potential to attenuate collagen-induced arthritis, J. Immunol. Res. 2019 (2019) 1-12. https://doi.org/10.1155/2019/1982570.

[19]

K. Masityama, K. Yamamoto, K. Ito, et al., Simplified methods for purification of peanut allergenic proteins: Ara h 1, Ara h 2, and Ara h 3, Food Sci. Technol. Res. 20 (2014) 875-881. https://doi.org/10.1155/2019/1982570.

[20]

A. Sanchiz, C. Cuadrado, M.C. Dieguez, et al., Thermal processing effects on the IgE-reactivity of cashew and pistachio, Food Chem. 245 (2018) 595-602. https://doi.org/10.1016/j.foodchem.2017.10.132.

[21]

N. Mikiashvili, J. Yu, Changes in immunoreactivity of allergen-reduced peanuts due to post-enzyme treatment roasting, Food Chem. 256 (2018) 188-194. https://doi.org/10.1016/j.foodchem.2018.02.119.

[22]

A.K. Verma, S. Kumar, A. Sharma, et al., Allergic manifestation by black gram (Vigna mungo) proteins in allergic patients, BALB/c mice and RBL-2H3 cells, Int. Immunopharmacol. 23 (2014) 92-103. https://doi.org/10.1016/j.intimp.2014.08.016.

[23]

S.Y. Chung, C.L. Butts, S.J. Maleki, et al., Linking peanut allergenicity to the processes of maturation, curing, and roasting, J. Agric. Food. Chem. 51 (2003) 4273-4277. https://doi.org/DOI:10.1021/jf021212d.

[24]

Y.J. Cong, F. Lou, W.T. Xue, et al., The effect of cooking methods on the allergenicity of peanut, Food Agric. Immunol. 18 (2007) 53-65. https://doi.org/10.1080/09540100701269413.

[25]

M. Bublin, M. Kostadinova, C. Radauer, et al., IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3, J. Allergy Clin. Immunol. 132 (2013) 118-212. https://doi.org/10.1016/j.jaci.2013.01.022.

[26]

S. Scheurer, M. Toda, S. Vieths, What makes an allergen?, Clin. Exp. Allergy. 45 (2015) 1150-1161. https://doi.org/10.1111/cea.12571.

[27]

B. Cabanillas, S.J. Maleki, H. Cheng, et al., Differences in theuptake of Ara h 3 from raw and roasted peanut by monocyte-derived dendritic cells, Int. Arch. Allergy Immunol. 177 (2018) 35-39. https://doi.org/10.1159/000489277.

[28]

M. Perusko, A. Al-Hanish, J. Mihailovic, et al., Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction, Food Chem. 232 (2017) 744-752. https://doi.org/10.1016/j.foodchem.2017.04.074.

[29]

S.Y. Chung, E.T. Champagne, Association of end-product adducts with increased IgE binding of roasted peanuts, J. Agric. Food Chem. 49 (2001) 3911-3916. https://doi.org/10.1021/jf001186o.

[30]

D. Stanic-Vucinic, M. Stojadinovic, M. Atanaskovic-Markovic, et al., Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound, Mol. Nutr. Food Res. 56 (2012) 1894-1905. https://doi.org/10.1002/mnfr.201200179.

[31]

M. Teodorowicz, E. Fiedorowicz, H. Kostyra, et al., Effect of maillard reaction on biochemical properties of peanut 7S globulin (Ara h 1) and its interaction with a human colon cancer cell line (Caco-2), Mol. Nutr. Food Res. 52 (2013) 1927-1938. https://doi.org/10.1007/s00394-013-0494-x.

[32]

M. Teodorowicz, D. Swiatecka, H. Savelkoul, et al., Hydrolysates of glycated and heat-treated peanut 7S globulin (Ara h 1) modulate human gut microbial proliferation, survival and adhesion, J. Appl. Microbiol. 116 (2014) 424-434. https://doi.org/10.1111/jam.12358.

[33]

K. Suri, B. Singh, A. Kaur, et al., Impact of roasting and extraction methods on chemical properties, oxidative stability and maillard reaction products of peanut oils, J. Food Sci. Technol. 56 (2019) 2436-2445. https://doi.org/10.1007/s13197-019-03719-4.

[34]

S. Filep, D.S. Block, B.R.E. Smith, et al., Specific allergen profiles of peanut foods and diagnostic or therapeutic allergenic products, J. Allergy Clin. Immunol. 141 (2018) 626-631. https://doi.org/10.1016/j.jaci.2017.05.049.

[35]

R.A. Kopper, N.J. Odum, M. Sen, et al., Peanut protein allergens: the effect of roasting on solubility and allergenicity, Int. Arch. Allergy Immunol. 136 (2005) 16-22. https://doi.org/10.1159/000082580.

[36]

L. Perez-Rodriguez, M. Martinez-Blanco, D. Lozano-Ojalvo, et al., Egg yolk augments type 2 immunity by activating innate cells, Eur. J. Nutr. (2020) 1-12. https://doi.org/10.1159/000082580.

Food Science and Human Wellness
Pages 755-764
Cite this article:
Wang M, Wang S, Sun X, et al. Study on mechanism of increased allergenicity induced by Ara h 3 from roasted peanut using bone marrow-derived dendritic cells. Food Science and Human Wellness, 2023, 12(3): 755-764. https://doi.org/10.1016/j.fshw.2022.09.009

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Received: 21 April 2020
Revised: 25 October 2020
Accepted: 22 November 2020
Published: 15 October 2022
© 2023 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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