Transition Metal Sequestration by the Host-Defense Protein Calprotectin
Name
nihms977692.pdf
Description
Accepted version
Size
1.01 MB
Format
Adobe PDF
Checksum (MD5)
39e7299db8d0397332121ba96822581b
Author(s)
Zygiel, Emily Mikayla
Nolan, Elizabeth Marie
Date Issued
June 2018
Journal
Annual review of biochemistry
Publisher
Annual Reviews
Citation
Zygiel, Emily M. and Elizabeth M. Nolan. “Transition Metal Sequestration by the Host-Defense Protein Calprotectin.” Annual review of biochemistry 87 (2018): 621-643 © 2018 The Author(s)
Version
Author's final manuscript
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1146/ANNUREV-BIOCHEM-062917-012312
