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Transition Metal Sequestration by the Host-Defense Protein Calprotectin
Annual Review of Biochemistry ( IF 12.1 ) Pub Date : 2018-06-20 00:00:00 , DOI: 10.1146/annurev-biochem-062917-012312
Emily M. Zygiel 1 , Elizabeth M. Nolan 1
Affiliation  

In response to microbial infection, the human host deploys metal-sequestering host-defense proteins, which reduce nutrient availability and thereby inhibit microbial growth and virulence. Calprotectin (CP) is an abundant antimicrobial protein released from neutrophils and epithelial cells at sites of infection. CP sequesters divalent first-row transition metal ions to limit the availability of essential metal nutrients in the extracellular space. While functional and clinical studies of CP have been pursued for decades, advances in our understanding of its biological coordination chemistry, which is central to its role in the host–microbe interaction, have been made in more recent years. In this review, we focus on the coordination chemistry of CP and highlight studies of its metal-binding properties and contributions to the metal-withholding innate immune response. Taken together, these recent studies inform our current model of how CP participates in metal homeostasis and immunity, and they provide a foundation for further investigations of a remarkable metal-chelating protein at the host–microbe interface and beyond.

中文翻译:


宿主防御蛋白钙卫蛋白的过渡金属螯合

响应微生物感染,人类宿主部署了金属螯合的宿主防御蛋白,其降低了养分的利用率,从而抑制了微生物的生长和毒力。钙卫蛋白(CP)是一种中性粒细胞和上皮细胞在感染部位释放的丰富抗菌蛋白。CP螯合二价的第一行过渡金属离子,以限制细胞外空间中必需金属养分的利用。尽管CP的功能和临床研究已经进行了数十年,但近几年来,我们对它的生物配位化学的理解有了新的进展,这对于它在宿主与微生物相互作用中的作用至关重要。在这篇评论中,我们专注于CP的配位化学,重点研究其金属结合特性及其对扣留先天免疫反应的贡献。综上所述,这些最新研究为我们目前的CP如何参与金属稳态和免疫提供了模型,它们为进一步研究宿主-微生物界面及其他部位的非凡的金属螯合蛋白奠定了基础。

更新日期:2018-06-20
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