中华绒螯蟹（Eriocheir sinensis）天然血蓝蛋白的分子和变应原特性。
Molecular and allergenic properties of natural hemocyanin from Chinese mitten crab (Eriocheir sinensis).
机构信息
Laboratory of Quality & Safety Risk Assessment for Aquatic Products on Storage and Preservation (Ministry of Agriculture and Rural Affairs), College of Food Science and Technology, Shanghai Ocean University, No. 999, Huchenghuan Road, Shanghai 201306, PR China; Shanghai Engineering Researching Center of Aquatic-Product Processing & Preservation, Shanghai 201306, PR China.
Laboratory of Quality & Safety Risk Assessment for Aquatic Products on Storage and Preservation (Ministry of Agriculture and Rural Affairs), College of Food Science and Technology, Shanghai Ocean University, No. 999, Huchenghuan Road, Shanghai 201306, PR China; Shanghai Engineering Researching Center of Aquatic-Product Processing & Preservation, Shanghai 201306, PR China.
出版信息
Food Chem. 2023 Oct 30;424:136422. doi: 10.1016/j.foodchem.2023.136422. Epub 2023 May 19.
Hemocyanin in crustaceans is an allergen for humans. However, little information was available on its molecular, structural and allergenic properties. In this study, the purified natural protein was identified as Eriocheir sinensis HC by LC-MS/MS, which was allergenic because its reaction with the serum IgE of crustacean patients. Results of the molecular properties showed that, HC was resistant to trypsin digestion, but not a heat-stable protein. Boiling (55.05 ± 3.50 %) and steaming (66.84 ± 1.65 %) induced an increase in β-sheet and decreased allergenicity of HC. By comparing the amino acid sequences of eight crustaceans, HC was found to be highly conserved. Five epitopes of HC were identified and validated by murine sensitization model, and two of them (P3 and P10) were exactly as the predicted by six types of bioinformatics. Multiple bioinformatics analysis combining with murine sensitization model seemed to be effective way for identification of allergenic epitopes.
甲壳类动物血蓝蛋白是人类的过敏原。然而，关于其分子、结构和变应原特性的信息很少。在这项研究中，通过 LC-MS/MS 将纯化的天然蛋白鉴定为中华绒螯蟹 HC，因为它与甲壳类动物患者的血清 IgE 发生反应而具有变应原性。分子特性的结果表明，HC 对胰蛋白酶消化具有抗性，但不是热稳定蛋白。煮沸（55.05±3.50%）和蒸制（66.84±1.65%）导致β-折叠增加和 HC 变应原性降低。通过比较八种甲壳类动物的氨基酸序列，发现 HC 高度保守。通过小鼠致敏模型鉴定和验证了 HC 的 5 个表位，其中 2 个（P3 和 P10）与 6 种生物信息学预测的完全一致。结合小鼠致敏模型的多种生物信息学分析似乎是鉴定变应原表位的有效方法。
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