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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Purification, Characterization, and Crystal Structure of Parvalbumins, the Major Allergens in Mustelus griseus
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Purification, Characterization, and Crystal Structure of Parvalbumins, the Major Allergens in Mustelus griseus

机译：Parvalbumins的纯化，表征和晶体结构，Mustelus Griseus的主要过敏原

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摘要

Fish play important roles in human nutrition and health, but also trigger allergic reactions in some population. Parvalbumin (PV) represents the major allergen of fish. While IgE cross-reactivity to PV in various bony fish species has been well characterized, little information is available about allergens in cartilaginous fish. In this study, two shark PV isoforms (named as SPV-I and SPV-II) from Mustelus griseus were purified. Their identities were further confirmed by mass spectroscopic analysis. IgE immunoblot analysis showed that sera from fish-allergic patients reacted to both SPV-I and SPV-II, but the majority of sera reacted more intensely to SPV-I than SPV-II. Thermal denaturation monitored by CD spectrum showed that both of the SPV allergens are highly thermostable. SPV-I maintained its IgE-binding capability after heat denaturation, while the IgE-binding capability of SPV-II was reduced. The results of crystal structure showed that SPV-I and SPV-II were similar in their overall tertiary structure, but their amino acid sequences shared lower similarities, indicating that the differences in the IgE-binding capabilities of SPV-I and SPV-II might be due to differential antigen epitopes in these two isoforms.
机译：鱼在人类营养和健康中发挥重要作用，但也引发了某些人口中的过敏反应。 Parvalbumin（PV）代表鱼的主要过敏原。虽然在各种骨鱼类种类中对PV的IgE交叉反应性具有很好的表征，但在软骨鱼中的过敏原少的信息很少。在这项研究中，纯化了来自法霉素Griseus的两种鲨鱼PV同种型（命名为SPV-I和SPV-II）。通过质谱分析进一步证实了它们的身份。 IgE免疫斑分析表明，来自鱼类过敏患者的血清对SPV-I和SPV-II反应，但大多数血清比SPV-I II更强烈地反应。 CD谱监测的热变性表明，两种SPV过敏原是高温稳定的。 SPV-I在热变性后保持其IgE结合能力，而SPV-II的IgE结合能力降低。晶体结构的结果表明，SPV-1和SPV-II在其总三结构中类似，但它们的氨基酸序列共同相似性，表明SPV-I和SPV-II的IgE结合能力的差异可能由于这两种同种型中的差异抗原表位。

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