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由宿主防御蛋白的人类calprotectin封存

Toshiki G Nakashige¹, Emily M Zygiel¹, Catherine L Drennan¹

¹Department of Chemistry, ‡Department of Biology, and §Howard Hughes Medical Institute, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.

Journal of the American Chemical Society

|June 3, 2017

概括

人类calprotectin (CP) 结合并封存 (Ni(II),是病原体如金黄色葡萄球菌和肺炎菌的重要营养物质. 这项研究显示,

科学领域:

生物化学
金属蛋白化学
天生的免疫力

背景情况:

人类的calprotectin (CP) 是一种已知的先天性免疫蛋白质,可化必需的过渡金属,如Mn,Fe和Zn,使其不受微生物的影响.
CP在 (Ni(II)) 稳态中的作用及其与该金属的协调化学是以前未知的.

研究的目的:

为了阐明人类蛋白 (CP) 的Ni (II) 协调化学.
调查CP的离病原细菌和抑制依赖酶的能力.

主要方法:

在2.6Å分辨率下进行X射线晶体检测,以确定与Ni (II) 和Ca (II) 结合的CP.
在CP的金属结合部位进行生物化学测试以评估Ni (II) 和Zn (II) 的结合偏好.
与CP进行的细菌共化研究,以评估Ni (II) 封存和尿素酶抑制.

主要成果:

晶体结构显示在CP的His3Asp (位点1) 和His6 (位点2) 基因上存在Ni(II) 结合.
热力学研究显示,在六基胺结合部位上,Ni (II) 优先于Zn (II).
CP有效地从金色葡萄球菌和Klebsiella肺炎中隔离Ni (II),抑制其依赖Ni (II) 的尿酶活性.

结论:

人类calprotectin表现出独特的Ni (II) 协调化学反应,在已知过渡金属位点结合金属.
CP 能够隔离 Ni ((II) 和抑制细菌尿酶,这表明它在对抗 Ni ((II) 依存性病原体的宿主防御中起作用.
这些发现扩大了对生物系统中的Ni (II) 协调和CP在宿主-微生物界面上的作用的理解.

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