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首页> 外文期刊>Biochemistry >Initial Biochemical and Functional Evaluation of Murine Calprotectin Reveals Ca(II)-Dependence and Its Ability to Chelate Multiple Nutrient Transition Metal Ions
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Initial Biochemical and Functional Evaluation of Murine Calprotectin Reveals Ca(II)-Dependence and Its Ability to Chelate Multiple Nutrient Transition Metal Ions

机译：小鼠CalProtectin的初始生化和功能评估显示Ca（ii） - 依赖性及其螯合多种营养过渡金属离子的能力

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摘要

Calprotectin (CP) is an abundant host-defense protein that contributes to the metal-withholding innate immune response by sequestering nutrient metal ions from microbial pathogens in the extracellular space. Over the past decade, murine models of infectious disease have advanced understanding of the physiological functions of CP and its ability to compete with microbes for essential metal nutrients. Despite this extensive work, murine CP (mCP) has not been biochemically evaluated, and structural and biophysical understanding of CP is currently limited to the human orthologue. We present the reconstitution, purification, and characterization of mCP as well as the cysteine-null variant mCP-Ser. Apo mCP is a mS100A8/mS100A9 heterodimer, and Ca(II) binding causes two heterodimers to self-associate and form a heterotetramer. Initial metal-depletion studies demonstrate that mCP depletes multiple first-row transition metal ions, including Mn, Fe, Ni, Cu, and Zn, from complex microbial growth medium, indicating that mCP binds multiple nutrient metals with high affinity. Moreover, antibacterial activity assays show that mCP inhibits the growth of a variety of bacterial species. The metal-depletion and antibacterial activity studies also provide evidence that Ca(II) ions enhance these functional properties of mCP. This contribution provides the groundwork for understanding the similarities and differences between the human and murine orthologues of CP and for further elucidation of its biological coordination chemistry.
机译：CalProtectin（CP）是一种丰富的宿主防御蛋白，通过在细胞外空间中的微生物病原体中螯合营养金属离子来促成金属预扣纯度免疫应答。在过去十年中，传染病的小鼠模型对CP的生理功能进行了先进的理解及其与基本金属营养素的微生物竞争的能力。尽管有这种广泛的工作，鼠CP（MCP）尚未生物化学评估，并且对CP的结构和生物物理学理解目前仅限于人体原语。我们提出了MCP的重构，纯化和表征，以及半胱氨酸 - 空变量MCP-Ser。 APO MCP是MS100A8 / MS100A9异二聚体，Ca（II）结合使两个异二聚体与自相缔合，形成异质四聚体。初始金属耗尽研究表明，MCP从复杂的微生物生长培养基中耗尽包括Mn，Fe，Ni，Cu，Cu和Zn的多个第一行过渡金属离子，表明MCP与高亲和力结合多种营养金属。此外，抗菌活性测定表明MCP抑制各种细菌种类的生长。金属耗尽和抗菌活性研究还提供了Ca（II）离子增强MCP的这些功能性质的证据。这一贡献为了解CP人和鼠突显的相似性和差异提供了基础，进一步阐明了其生物协调化学。

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  • 来源
    《Biochemistry》 |2018年第19期|共11页
  • 作者

    Rose C. Hadley; Yu Gu; Elizabeth M. Nolan;

  • 作者单位

    Department of Chemistry Massachusetts Institute of Technology Cambridge Massachusetts 02139 United States;

    Department of Chemistry Massachusetts Institute of Technology Cambridge Massachusetts 02139 United States;

    Department of Chemistry Massachusetts Institute of Technology Cambridge Massachusetts 02139 United States;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
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