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Research Article | Open Access

Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat

Linglin FuaRongrong WangaJinru Zhoua,bChong WangaYanbo Wanga( )
Food Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China
Zhejiang Engineering Research Institute of Food & Drug Quality and Safety, School of Management and E-Business, Zhejiang Gongshang University, Hangzhou 310018, China

Peer review under responsibility of KeAi Communications Co., Ltd.

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Abstract

N-glycans in many proteins are of great concern because of their strong association with food allergies. Triticum aestivum (bread wheat), a major food crop, is known as one of the "Big Eight" allergenic groups. However, little research has been done about N-glycans in wheat glycoproteins. In this study, a soluble wheat glycoprotein was purified from wheat and further identified as globulin-1 S allele (GSA). The wheat GSA displayed significant IgE-binding activity. Moreover, one N-glycosylation site and 6 kinds of N-glycans were identified by mass spectrometry, including 3 high mannose types and 3 complex types. Furthermore, the IgE-binding activity of wheat GSA is proved to be reduced by the removal of N-glycan, thermal treatment (temperatures > 80 ℃), and strong acidic treatment (pH 3.0). These findings would provide a better understanding of the effects of N-glycosylation, thermal treatment, and acidic treatment on the molecular characteristics of GSA, and further provide new insights into the development of hypoallergenic wheat products.

References

[1]

T.W. Song, J.Y. Hong, K.E. Lee, et al., IgE reactivity to carbohydrate moieties of glycoproteins in wheat allergy, Allergy Asthma Proc. 36(3) (2015) 192-199. https://doi.org/10.2500/aap.2015.36.3815.

[2]

M.E. Levin, C.L. Gray, J. Marrugo, Food allergy: international and developing world perspectives, Curr. Pediatr. Rep. 4(3) (2016) 129-137. https://doi.org/10.1007/s40124-016-0104-5.

[3]

M. Calvani, I. Berti, A. Fiocchi, et al., Oral food challenge: safety, adherence to guidelines and predictive value of skin prick testing, Pediatr. Allergy Immunol. 23(8) (2012) 755-761. https://doi.org/10.1111/pai.12016.

[4]

X.Y. Wang, Y. Zhuang, T.T. Ma, et al., Prevalence of self-reported food allergy in six regions of inner Mongolia, northern China: a population-based survey, Med. Sci. Monit. 24 (2018) 1902-1911. https://doi.org/10.12659/msm.908365.

[5]

L. Li, C. Wang, S. Qiang, et al., Mass spectrometric analysis of n-glycoforms of soybean allergenic glycoproteins separated by SDS-PAGE, J. Agric. Food Chem. 64(39) (2016) 7367-7376. https://doi.org/10.1021/acs.jafc.6b02773.

[6]

M. Kamalakannan, L.M. Chang, G. Grishina, et al., Identification and characterization of DC-SIGN-binding glycoproteins in allergenic foods, Allergy 71(8) (2016) 1145-1155. https://doi.org/10.1111/all.12873.

[7]

G.A. Rabinovich, M.A. Toscano, Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation, Nat. Rev. Immunol. 9(5) (2009) 338-352. https://doi.org/10.1038/nri2536.

[8]

A. Homann, G. Schramm, U. Jappe, Glycans and glycan-specific IgE in clinical and molecular allergology: sensitization, diagnostics, and clinical symptoms, J. Allergy Clin. Immunol. 140(2) (2017) 356-368. https://doi.org/10.1016/j.jaci.2017.04.019.

[9]

A. Yang, H. Deng, Q. Zu, et al., Structure characterization and IgE-binding of soybean 7S globulin after enzymatic deglycosylation, Int. J. Food Prop. 21(1) (2018) 186-197. https://doi.org/10.1080/10942912.2018.1437628.

[10]

Z. Zhang, H. Xiao, X. Zhang, et al., Insight into the effects of deglycosylation and glycation of shrimp tropomyosin on in vivo allergenicity and mast cell function, Food Funct. 10(7) (2019) 3934-3941. https://doi.org/10.1039/c9fo00699k.

[11]

S.B. Lehrer, W.E. Horner, G. Reese, Why are some proteins allergenic? implications for biotechnology, Crit. Rev. Food Sci. Nutr. 36(6) (1996) 553-564. https://doi.org/10.1080/10408399609527739.

[12]

R. van Ree, M. Cabanes-Macheteau, J. Akkerdaas, et al., Beta(1, 2)-xylose and alpha(1, 3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens, J. Biol. Chem. 275(15) (2000) 11451-11458. https://doi.org/10.1074/jbc.275.15.11451.

[13]

W. Hemmer, M. Focke, D. Kolarich, et al., Identification by immunoblot of venom glycoproteins displaying immunoglobulin E-binding N-glycans as cross-reactive allergens in honeybee and yellow jacket venom, Clin. Exp. Allergy 34(3) (2004) 460-469. https://doi.org/10.1111/j.1365-2222.2004.01897.x.

[14]

W.S. Veraverbeke, J.A. Delcour, Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality, Crit. Rev. Food Sci. Nutr. 42(3) (2002) 179-208. https://doi.org/10.1080/10408690290825510.

[15]

L. Gao, W. Ma, J. Chen, et al., Characterization and comparative analysis of wheat high molecular weight glutenin subunits by SDS-PAGE, RP-HPLC, HPCE, and MALDI-TOF-MS, J. Agric. Food Chem. 58(5) (2010) 2777-2786. https://doi.org/10.1021/jf903363z.

[16]

M. Laurière, I. Bouchez, C. Doyen, et al., Identification of glycosylated forms of wheat storage proteins using two-dimensional electrophoresis and blotting, Electrophoresis 17(3) (1996) 497-501. https://doi.org/10.1002/elps.1150170312.

[17]

S.J. Maleki, S.Y. Chung, E.T. Champagne, et al., The effects of roasting on the allergenic properties of peanut proteins, J. Allergy Clin. Immunol. 106(4) (2000) 763-768. https://doi.org/10.1067/mai.2000.109620.

[18]

B.M. Ehn, B. Ekstrand, U. Bengtsson, et al., Modification of IgE binding during heat processing of the cow's milk allergen beta-lactoglobulin, J. Agric. Food Chem. 52(5) (2004) 1398-1403. https://doi.org/10.1021/jf0304371.

[19]

R. Kasera, A.B. Singh, R. Kumar, et al., Effect of thermal processing and γ-irradiation on allergenicity of legume proteins, Food Chem. Toxicol. 50(10) (2012) 3456-3461. https://doi.org/10.1016/j.fct.2012.07.031.

[20]

K.S. Hansen, B.K. Ballmer-Weber, D. Lüttkopf, et al., Roasted hazelnutsallergenic activity evaluated by double-blind, placebo-controlled food challenge, Allergy 58(2) (2003) 132-138. https://doi.org/10.1034/j.1398-9995.2003.23959.x.

[21]

L.K. Kucek, L.D. Veenstra, P. Amnuaycheewa, et al., A grounded guide to gluten: how modern genotypes and processing impact wheat sensitivity, Compr. Rev. Food Sci. Food Saf. 14(3) (2015) 285-302. https://doi.org/10.1111/1541-4337.12129.

[22]

R. Kazemi, A. Taheri-Kafrani, A. Motahari, et al., Allergenicity reduction of bovine milk β-lactoglobulin by proteolytic activity of lactococcus lactis BMC12C and BMC19H isolated from Iranian dairy products, Int. J. Biol. Macromol. 112 (2018) 876-881. https://doi.org/10.1016/j.ijbiomac.2018.02.044.

[23]

X.H. Sun, K.X. Zhu, H.M. Zhou, Protein extraction from defatted wheat germ by reverse micelles: optimization of the forward extraction, J. Cereal Sci. 48(3) (2008) 829-835. https://doi.org/10.1016/j.jcs.2008.06.006.

[24]

H.Y. Park, T.J. Yoon, H.H. Kim, et al., Changes in the antigenicity and allergenicity of ovalbumin in chicken egg white by N-acetylglucosaminidase, Food Chem. 217 (2017) 342-345. https://doi.org/10.1016/j.foodchem.2016.08.112.

[25]

N.K. Singh, K.W. Shepherd, G.B. Cornish, A simplified SDS-PAGE procedure for separating LMW subunits of glutenin, Journal of Cereal Science 14(3) 1991 203-208. https://doi.org/10.1016/S0733-5210(09)80039-8.

[26]

Y.X. Zhang, H.L. Chen, S.J. Maleki, et al., Purification, characterization, and analysis of the allergenic properties of myosin light chain in Procambarus clarkii, J. Agric. Food Chem. 63(27) (2015) 6271-6282. https://doi.org/10.1021/acs.jafc.5b01318.

[27]

H.W. Shen, M.J. Cao, Q.F. Cai, et al., Purification, cloning, and immunological characterization of arginine kinase, a novel allergen of Octopus fangsiao, J. Agric. Food Chem. 60(9) (2012) 2190-2199. https://doi.org/10.1021/jf203779w.

[28]

S. Pahr, C. Constantin, N.G. Papadopoulos, et al., α-Purothionin, a new wheat allergen associated with severe allergy, J. Allergy Clin. Immunol. 132(4) (2013) 1000-3.e1-4. https://doi.org/10.1016/j.jaci.2013.05.016.

[29]

Z. Zhang, H. Xiao, X. Zhang, et al., Conformation, allergenicity and human cell allergy sensitization of tropomyosin from Exopalaemon modestus: effects of deglycosylation and Maillard reaction, Food Chem. 276 (2019) 520-527. https://doi.org/10.1016/j.foodchem.2018.10.032.

[30]

W. Song, M.G. Henquet, R.A. Mentink, et al., N-glycoproteomics in plants: perspectives and challenges, J. Proteomics 74(8) (2011) 1463-1474. https://doi.org/10.1016/j.jprot.2011.05.007.

[31]

S. Mercx, N. Smargiasso, F. Chaumont, et al., Inactivation of the β(1, 2)-xylosyltransferase and the α(1, 3)-fucosyltransferase genes in Nicotiana tabacum BY-2 cells by a Multiplex CRISPR/Cas9 strategy results in glycoproteins without plant-specific glycans, Front. Plant Sci. 8 (2017) 403. https://doi.org/10.3389/fpls.2017.00403.

[32]

T. Liu, Y. Li, J. Xu, et al., N-glycosylation and enzymatic activity of the rHuPH20 expressed in Chinese hamster ovary cells, Anal. Biochem. 632 (2021) 114380. https://doi.org/10.1016/j.ab.2021.114380.

[33]

A. Rump, R. Risti, M.L. Kristal, et al., Dual ELISA using SARS-CoV-2 nucleocapsid protein produced in E. coli and CHO cells reveals epitope masking by N-glycosylation, Biochem. Biophys. Res. Commun. 534 (2021) 457-460. https://doi.org/10.1016/j.bbrc.2020.11.060.

[34]

A.L. Lopata, R.E. O'Hehir, S.B. Lehrer, Shellfish allergy, Clin. Exp. Allergy 40(6) (2010) 850-858. https://doi.org/10.1111/j.1365-2222.2010.03513.x.

[35]

R. Ayuso, G. Grishina, L. Bardina, et al., Myosin light chain is a novel shrimp allergen, Lit v 3, J. Allergy Clin. Immunol. 122(4) (2008) 795-802. https://doi.org/10.1016/j.jaci.2008.07.023.

[36]

M.L. Bernardi, D. Picone, L. Tuppo, et al., Physico-chemical features of the environment affect the protein conformation and the immunoglobulin E reactivity of kiwellin (Act d 5), Clin. Exp. Allergy 40(12) (2010) 1819-1826. https://doi.org/10.1111/j.1365-2222.2010.03603.x.

[37]

A. Taheri-Kafrani, J.C. Gaudin, H. Rabesona, et al., Effects of heating and glycation of beta-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients, J. Agric. Food Chem. 57(11) (2009) 4974-4982. https://doi.org/10.1021/jf804038t.

Food Science and Human Wellness
Pages 1601-1608
Cite this article:
Fu L, Wang R, Zhou J, et al. Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat. Food Science and Human Wellness, 2023, 12(5): 1601-1608. https://doi.org/10.1016/j.fshw.2023.02.020

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Received: 12 January 2022
Revised: 13 February 2022
Accepted: 02 March 2022
Published: 21 March 2023
© 2023 Beijing Academy of Food Sciences.

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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