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自抗体结合和独特的酶基质中间形状的人类转谷氨酶3的自身抗体结合和独特的酶基质

Julie Elisabeth Heggelund^1,2, Saykat Das^3,4, Jorunn Stamnaes^3,4

¹KG Jebsen Coeliac Disease Research Centre, Institute of Clinical Medicine, University of Oslo, Oslo, Norway. j.e.heggelund@medisin.uio.no.

Nature communications

|October 5, 2023

概括

转胺酶3 (TG3) 是皮肤炎形性皮肤炎的自身抗原,在基质结合时改变了形状,揭示了患者抗体识别的独特结构. 这一发现支持了皮肤炎形性皮肤炎中自身免疫反应的模型.

科学领域:

生物化学生物化学
免疫学免疫学免疫学
结构生物学结构生物学

背景情况:

转谷氨酸酶3 (TG3) 是与皮肤炎形 (DH) 相关的自身抗原.
TG3是一种依赖的酶,需要蛋白质分解裂变才能产生催化活性.
肝炎是一种自身免疫性水泡皮肤疾病,与质敏感性有关.

研究的目的:

阐明TG3激活的结构基础及其由DH自身抗体的识别.
为了研究TG3在基质结合时所经历的形状变化.
了解TG3结构在DH的自身免疫病原发生中的作用.

主要方法:

人类TG3的X射线晶体学复合与来自DH患者的TG3特异性Fab片段.
对不活跃和活跃的TG3形状的分析.
与TG3的结构比较,有和没有它的C端β-桶 (C1C2).

主要成果:

四个X射线晶体结构揭示了与DH患者抗体碎片结合的不活跃和活跃的TG3形状.
分裂的TG3在与基质模仿抑制剂结合时经历了显著的构造变化,涉及催化核心域重组和C1C2脱离.
独特的TG3酶-基质构造,缺乏C1C2,由DH自身抗体特别识别.

结论:

该研究揭示了TG3激活的结构机制及其与DH自身抗体的相互作用.
这些发现支持B细胞内部化TG3-质复合体的模型,促进抗原呈现和DH的自身抗体产生.
没有C1C2的独特的TG3形状是皮肤炎形性皮肤炎的自身免疫识别的关键目标.

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