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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Format: | Article |
Language: | English |
Published: |
American Chemical Society (ACS),
2020-01-23T20:25:02Z.
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Online Access: | Get fulltext |
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) |
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