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卷曲螺旋结构蛋白 C 过敏原优势区域的晶体结构分析和免疫球蛋白 E 表位作图

Crystal Structure Analysis and IgE Epitope Mapping of Allergic Predominant Region in Filamin C, Scy p 9.

机构信息

College of Marine 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 361000, China.

College of Environment and Public Health, Xiamen Huaxia University, Xiamen, Fujian 361000, China.

出版信息

J Agric Food Chem. 2022 Feb 2;70(4):1282-1292. doi: 10.1021/acs.jafc.1c07922. Epub 2022 Jan 18.

DOI:10.1021/acs.jafc.1c07922
PMID:35040643
Abstract

Filamin C (FLN c) is a novel allergen in shellfish. In this study, FLN c from was divided into three regions for recombinant expression based on the number of domains and amino acids. Using dot blot and basophil activation tests, the allergic predominant region of FLN c was determined to be 336-531 amino acid positions (named FLN c-M). It was confirmed that by X-ray diffraction, the crystal structure of FLN c-M with immunoglobulin-like folding at a resolution of 1.7 Å was obtained. The monomer was a barrel structure composed of 16 β-strands and 2 α-helices. Three conformational epitopes were predicted, six linear epitopes were verified by serological test, and they were positioned on the crystal structure of FLN c-M. For the first time, the crystal structure of the allergic predominant region of FLN c was determined, and it provided an accurate template for the localization of IgE epitopes.

摘要

纤连蛋白 C(FLN c)是贝类中的一种新型过敏原。在这项研究中,根据结构域和氨基酸的数量,将 中的 FLN c 分为三个区域进行重组表达。通过点印迹和嗜碱性粒细胞活化试验,确定 FLN c 的主要过敏原区域为 336-531 个氨基酸位置(命名为 FLN c-M)。通过 X 射线衍射证实,获得了分辨率为 1.7 Å 的具有免疫球蛋白折叠的 FLN c-M 的晶体结构。单体是由 16 个β-链和 2 个α-螺旋组成的桶状结构。预测了三个构象表位,通过血清学试验验证了六个线性表位,并将其定位在 FLN c-M 的晶体结构上。首次确定了 FLN c 的主要过敏原区域的晶体结构,为 IgE 表位的定位提供了准确的模板。

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