Bioinorganic Explorations of Zn(II) Sequestration by Human S100 Host-Defense Proteins

The human innate immune system launches a metal-withholding response to starve invading microbial pathogens of essential metal nutrients. Zn(II)-sequestering proteins of the human S100 family contribute to this process and include calprotectin (CP, S100A8/S100A9 oligomer, calgranulin A/B oligomer),...

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Bibliographic Details
Main Authors: Cunden, Lisa Stephanie (Author), Nolan, Elizabeth Marie (Author)
Other Authors: Massachusetts Institute of Technology. Department of Chemistry (Contributor)
Format: Article
Language:English
Published: American Chemical Society (ACS), 2020-01-23T20:25:02Z.
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Summary:The human innate immune system launches a metal-withholding response to starve invading microbial pathogens of essential metal nutrients. Zn(II)-sequestering proteins of the human S100 family contribute to this process and include calprotectin (CP, S100A8/S100A9 oligomer, calgranulin A/B oligomer), S100A12 (calgranulin C), and S100A7 (psoriasin). This Perspective highlights recent advances in the Zn(II) coordination chemistry of these three proteins, as well as select studies that evaluate Zn(II) sequestration as an antimicrobial mechanism. Keywords: immunology; peptides and proteins; metals; monomersIons
National Science Foundation (U.S.) (CHE-1352132)
National Institutes of Health (U.S.) (R01GM118695)