Identification and characterization of Crassostrea angulata arginine kinase, a novel allergen that causes cross-reactivity among shellfish
Identification and characterization of Crassostrea angulata arginine kinase, a novel allergen that causes cross-reactivity among shellfish
复制标题
角牡蛎精氨酸激酶的鉴定和表征，一种引起贝类之间交叉反应的新型过敏原
DOI：
10.1039/d1fo02042k
复制
发表时间：
2021
期刊：
影响因子：
6.1
通讯作者：
Liu Guang-Ming
中科院分区：
文献类型：
--
作者：
Huan Fei;Han Tian-Jiao;Liu Meng;Li Meng-Si;Yang Yang;Liu Qing-Mei;Lai Dong;Cao Min-Jie;Liu Guang-Ming
牡蛎是一种常见的引起过敏的食物。然而，关于其过敏原和交叉反应性的信息很少。在这项研究中，精氨酸激酶（AK）被鉴定为角牡蛎中的一种新型过敏原。克隆了编码350个氨基酸的AK一级序列，获得重组AK(rAK)。免疫点结果、二级结构和消化稳定性表明天然 AK 和 rAK 具有相似的 IgG/IgE 结合活性和理化性质。对 14 名牡蛎敏感个体的血清学分析表明，AK 在牡蛎、虾和螃蟹之间表现出交叉反应性。此外，通过抑制斑点印迹和抑制酶联免疫吸附试验验证了牡蛎AK中的9个表位，其中6个表位与虾/蟹AK的表位相似。最保守的表位是 P5 (121-133) 和 P6 (133-146)，它们可能是 AK 引起的交叉反应的原因。这些发现将有助于更深入地了解牡蛎过敏原和贝类之间的交叉反应。
Oyster is a common food that causes allergy. However, little information is available about its allergens and cross-reactivity. In this study, arginine kinase (AK) was identified as a novel allergen in Crassostrea angulata. The primary sequence of AK was cloned which encoded 350 amino acids, and recombinant AK (rAK) was obtained. The immunodot results, secondary structure and digestive stability showed that native AK and rAK had similar IgG/IgE-binding activity and physicochemical properties. Serological analysis of 14 oyster-sensitive individuals demonstrated that AK exhibited cross-reactivity among oysters, shrimps, and crabs. Furthermore, nine epitopes in oyster AK were verified using inhibition dot blots and inhibition enzyme linked immunosorbent assay, six of which were similar to the epitopes of shrimp/crab AK. The most conserved epitopes were P5 (121–133) and P6 (133–146), which may be responsible for the cross-reactivity caused by AK. These findings will provide a deeper understanding of oyster allergens and cross-reactivity among shellfish.