College of 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.
Women and Children's Hospital Affiliated to Xiamen University, Xiamen, Fujian 361003, China.
Food Funct. 2021 Sep 20;12(18):8570-8582. doi: 10.1039/d1fo01058a.
Sarcoplasmic-calcium-binding protein (SCP) has been investigated as a novel allergen in . Nevertheless, knowledge of its effector-cell-based allergic relevance and epitopes is limited. In this study, the heat-resistant allergen SCP was able to induce significant upregulation of CD63 and CD203c ( < 0.05), which showed obvious allergenicity in a basophil activation test. Furthermore, immunoinformatic tools, a one-bead-one-compound peptide library, and phage display technology were combined to analyze the allergenic epitopes of SCP. Five linear epitopes named L-SCP-1 (AA), L-SCP-2 (AA), L-SCP-3 (AA), L-SCP-4 (AA), and L-SCP-5 (AA) were verified using serological tests. Additionally, two conformational epitopes (C-SCP-1 and C-SCP-2) were determined, and C-SCP-1 was located at one of the calcium-binding sites (AA). Moreover, SCP showed weaker typical α-helical features and higher hydrophobicity after Ca depletion, which reduced its IgE-binding capacity. Overall, these epitope data could enhance our understanding of oyster allergens, which could be used to develop hypoallergenic shellfish products.
肌浆钙结合蛋白（SCP）已被研究作为一种新型过敏原在 。然而，其效应细胞相关的过敏相关性和表位的知识是有限的。在这项研究中，耐热过敏原 SCP 能够诱导 CD63 和 CD203c 的显著上调（ < 0.05），这在嗜碱性粒细胞活化试验中显示出明显的变应原性。此外，免疫信息学工具、一种单珠一单化合物肽文库和噬菌体展示技术被结合起来分析 SCP 的过敏原表位。五个线性表位分别命名为 L-SCP-1（AA）、L-SCP-2（AA）、L-SCP-3（AA）、L-SCP-4（AA）和 L-SCP-5（AA），通过血清学试验得到验证。此外，确定了两个构象表位（C-SCP-1 和 C-SCP-2），并且 C-SCP-1 位于一个钙结合位点（AA）。此外，SCP 在 Ca 耗竭后显示出较弱的典型 α-螺旋特征和更高的疏水性，这降低了其 IgE 结合能力。总的来说，这些表位数据可以增强我们对牡蛎过敏原的理解，这可以用来开发低变应原性贝类产品。
