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肌球蛋白轻链的鉴定、表位鉴定和交叉反应性分析:的一种重要过敏原。

Characterization, Epitope Identification, and Cross-reactivity Analysis of Tropomyosin: An Important Allergen of .

机构信息

College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Jimei University, Xiamen, Fujian 361021, China.

The Second Affiliated Hospital of Xiamen Medical College, Xiamen, Fujian 361021, China.

出版信息

J Agric Food Chem. 2022 Jul 27;70(29):9201-9213. doi: 10.1021/acs.jafc.2c03754. Epub 2022 Jul 18.

Abstract

Oyster is a common shellfish product in China, which is associated with food allergy. However, there is still lack of research on allergens in oysters. In this study, tropomyosin (TM), an important allergen of , was purified and identified by mass spectrometry. Subsequently, TM was cloned and expressed, with a sequence of size 852 bp, encoding 284 amino acid residues. The results of circular dichroism, digestion assay, inhibition enzyme-linked immunosorbent assay, and basophil activation test showed that recombinant TM had similar physicochemical properties and immunological properties to native TM. Furthermore, two conformational mimotopes were obtained and 10 IgE linear epitopes were verified. Meanwhile, different degrees of cross-reactivity were observed between TM and the other 8 shellfish TMs using antibodies and serological analysis, which may relate to the 3 conserved epitope regions. These findings are expected to provide a theoretical basis for the molecular diagnosis of oyster allergy and cross-reactivity among shellfish.

摘要

牡蛎是中国常见的贝类产品,与食物过敏有关。然而,目前对贝类过敏原的研究仍相对较少。在这项研究中,通过质谱分析对肌球蛋白(TM)这一重要过敏原进行了纯化和鉴定。随后,对 TM 进行了克隆和表达,得到了大小为 852bp、编码 284 个氨基酸残基的序列。圆二色性、消化实验、抑制酶联免疫吸附试验和嗜碱性粒细胞激活试验的结果表明,重组 TM 具有与天然 TM 相似的理化性质和免疫学特性。此外,还获得了两个构象模拟表位,并验证了 10 个 IgE 线性表位。同时,使用抗体和血清学分析发现,TM 与其他 8 种贝类 TM 之间存在不同程度的交叉反应性,这可能与 3 个保守表位区域有关。这些发现有望为牡蛎过敏和贝类之间的交叉反应的分子诊断提供理论依据。

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