Transition Metal Sequestration by the Host-Defense Protein Calprotectin
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 o...
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| Format: | Article |
| Language: | English |
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Annual Reviews
2020
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| Online Access: | https://hdl.handle.net/1721.1/125572 |
| _version_ | 1811091658029137920 |
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| author | Zygiel, Emily Mikayla Nolan, Elizabeth Marie |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Zygiel, Emily Mikayla Nolan, Elizabeth Marie |
| author_sort | Zygiel, Emily Mikayla |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T15:05:52Z |
| format | Article |
| id | mit-1721.1/125572 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T15:05:52Z |
| publishDate | 2020 |
| publisher | Annual Reviews |
| record_format | dspace |
| spelling | mit-1721.1/1255722022-10-02T00:35:21Z Transition Metal Sequestration by the Host-Defense Protein Calprotectin Zygiel, Emily Mikayla Nolan, Elizabeth Marie Massachusetts Institute of Technology. Department of Chemistry 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. National Institutes of Health (U.S.) (Grant R01 GM118695) National Institutes of Health (U.S.) (Grant R01 GM126376) National Science Foundation (U.S.) (Grant CHE-1352132) 2020-05-29T14:28:18Z 2020-05-29T14:28:18Z 2018-06 2020-01-02T17:33:18Z Article http://purl.org/eprint/type/JournalArticle 0066-4154 https://hdl.handle.net/1721.1/125572 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) en https://dx.doi.org/10.1146/ANNUREV-BIOCHEM-062917-012312 Annual review of biochemistry Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ application/pdf Annual Reviews PMC |
| spellingShingle | Zygiel, Emily Mikayla Nolan, Elizabeth Marie Transition Metal Sequestration by the Host-Defense Protein Calprotectin |
| title | Transition Metal Sequestration by the Host-Defense Protein Calprotectin |
| title_full | Transition Metal Sequestration by the Host-Defense Protein Calprotectin |
| title_fullStr | Transition Metal Sequestration by the Host-Defense Protein Calprotectin |
| title_full_unstemmed | Transition Metal Sequestration by the Host-Defense Protein Calprotectin |
| title_short | Transition Metal Sequestration by the Host-Defense Protein Calprotectin |
| title_sort | transition metal sequestration by the host defense protein calprotectin |
| url | https://hdl.handle.net/1721.1/125572 |
| work_keys_str_mv | AT zygielemilymikayla transitionmetalsequestrationbythehostdefenseproteincalprotectin AT nolanelizabethmarie transitionmetalsequestrationbythehostdefenseproteincalprotectin |