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.
J Agric Food Chem. 2020 May 6;68(18):5221-5231. doi: 10.1021/acs.jafc.0c01543. Epub 2020 Apr 27.
Oysters are an important shellfish group known to cause food allergy; however, knowledge of their sensitization components and cross-reactivity is limited. This study aimed to identify a novel allergen in and investigate its cross-reactivity. To this end, a 20 kDa protein was purified from oyster and confirmed to be a sarcoplasmic-calcium-binding protein (SCP) by LC-MS/MS. A 537 bp open reading frame was obtained from oyster SCP total RNA, which encoded 179 amino acids, and was expressed in . According to the circular dichroism results, digestion assay, and inhibition ELISA, the recombinant SCP (rSCP) exhibited similar physicochemical properties and IgG-binding activity to native SCP. rSCP displayed stronger IgE-binding activity by immunological method. Moreover, a different intensity of cross-reactivity and sequence homology were demonstrated between shellfish species. Collectively, these findings provide novel insight into shellfish allergens, which can be used to aid in the diagnosis of oyster-sensitized patients.
牡蛎是一种重要的贝类，已知会引起食物过敏；然而，其致敏成分和交叉反应性的知识有限。本研究旨在鉴定一种新型贝类过敏原，并研究其交叉反应性。为此，从牡蛎中纯化了一种 20 kDa 的蛋白，并通过 LC-MS/MS 确认为肌浆钙结合蛋白 (SCP)。从牡蛎 SCP 总 RNA 中获得了一个 537 bp 的开放阅读框，编码 179 个氨基酸，并在 中表达。根据圆二色性结果、消化实验和抑制 ELISA，重组 SCP (rSCP) 表现出与天然 SCP 相似的理化性质和 IgG 结合活性。免疫学法显示 rSCP 具有更强的 IgE 结合活性。此外，贝类物种之间表现出不同强度的交叉反应性和序列同源性。总之，这些发现为贝类过敏原提供了新的见解，可用于辅助诊断对牡蛎敏感的患者。
