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鉴定和表征精氨酸激酶,一种导致贝类之间发生交叉反应的新型过敏原。

Identification and characterization of arginine kinase, a novel allergen that causes cross-reactivity among shellfish.

机构信息

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.

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

出版信息

Food Funct. 2021 Oct 19;12(20):9866-9879. doi: 10.1039/d1fo02042k.

Abstract

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 . 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.

摘要

牡蛎是一种常见的过敏原食物。然而,关于其过敏原和交叉反应的信息很少。本研究鉴定出贻贝中的一种新型过敏原——精氨酸激酶(AK)。克隆了 AK 的一级序列,其编码 350 个氨基酸,并获得了重组 AK(rAK)。免疫印迹结果、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、虾和蟹之间具有交叉反应性。此外,使用抑制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 个与虾/蟹 AK 的表位相似。最保守的表位是 P5(121-133)和 P6(133-146),这可能是 AK 引起交叉反应的原因。这些发现将为贝类过敏原和交叉反应提供更深入的了解。

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