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使用细胞和小鼠模型评估酶促交联原肌球蛋白的致敏性和口服耐受性。

Allergenicity and Oral Tolerance of Enzymatic Cross-Linked Tropomyosin Evaluated Using Cell and Mouse Models.

作者信息

Liu GuangYu, Hu MengJun, Sun Le-Chang, Han XinYu, Liu QingMei, Alcocer Marcos, Fei DanXia, Cao Min-Jie, Liu Guang-Ming

机构信息

College of Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Jimei University , 43 Yindou Road, Xiamen 361021, Fujian, People's Republic of China.

School of Biosciences, The University of Nottingham , Sutton Bonington Campus, Loughborough LE12 5RD, United Kingdom.

出版信息

J Agric Food Chem. 2017 Mar 15;65(10):2205-2213. doi: 10.1021/acs.jafc.6b05816. Epub 2017 Mar 6.

DOI:10.1021/acs.jafc.6b05816
PMID:28234465
Abstract

The enzymatic cross-linking of proteins to form high-molecular-weight compounds may alter their sensitization potential. The IgG-/IgE-binding activity, digestibility, allergenicity, and oral tolerance of cross-linked tropomyosin with tyrosinase (CTC) or horseradish peroxidase (CHP) were investigated. ELISA results demonstrated CTC or CHP reduced its IgE-binding activity by 34.5 ± 1.8 and 63.5 ± 0.6%, respectively. Compared with native tropomyosin or CTC, CHP was more easily digested into small fragments; CHP decreased the degranulation of RBL-2H3 cells and increased endocytosis by dendritic cells. CHP can induce oral tolerance and reduce allergenicity in mice by decreasing IgE and IgG1 levels in serum, the production of T-cell cytokines, and the percentage composition of dendritic cells. These findings demonstrate CHP has more potential of reducing the allergenicity than CTC via influencing the morphology of protein, changing the original method of antigen presentation, modulating the Th1/Th2 immunobalance, and inducing the oral tolerance of the allergen tropomyosin.

摘要

蛋白质的酶促交联形成高分子量化合物可能会改变其致敏潜力。研究了用酪氨酸酶(CTC)或辣根过氧化物酶(CHP)交联原肌球蛋白后的IgG-/IgE结合活性、消化率、致敏性和口服耐受性。酶联免疫吸附测定(ELISA)结果表明,CTC和CHP分别使其IgE结合活性降低了34.5±1.8%和63.5±0.6%。与天然原肌球蛋白或CTC相比,CHP更容易被消化成小片段;CHP降低了RBL-2H3细胞的脱颗粒作用,并增加了树突状细胞的内吞作用。CHP可通过降低血清中IgE和IgG1水平、T细胞细胞因子的产生以及树突状细胞的百分比组成,诱导小鼠口服耐受性并降低致敏性。这些发现表明,CHP通过影响蛋白质形态、改变抗原呈递的原始方式、调节Th1/Th2免疫平衡以及诱导过敏原原肌球蛋白的口服耐受性,比CTC具有更大的降低致敏性潜力。

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