ArticleJournal of the American Chemical Society2016
The Hexahistidine Motif of Host-Defense Protein Human Calprotectin Contributes to Zinc Withholding and Its Functional Versatility.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 56 citations in OpenAlex.
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- Alkaline Amino Acids for Salt Reduction in Surimi: A Review.Foods (Basel, Switzerland) · 2025Review
- Calprotectin elicits aberrant iron starvation responses inJournal of bacteriology · 2025Article
- Zebrafish do not have a calprotectin ortholog.PloS one · 2025Article
- Manganese uptake by MtsABC contributes to the pathogenesis of human pathogen group A streptococcus by resisting host nutritional immune defenses.Infection and immunity · 2024Article
- An opportunistic pathogen under stress: how Group B Streptococcus responds to cytotoxic reactive species and conditions of metal ion imbalance to survive.FEMS microbiology reviews · 2024Review
- Spectroscopic and computational investigations of Cobalt(II) binding to the innate immune protein human calprotectin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Post-translational modifications on the metal-sequestering protein calprotectin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- Steric Effects on the Chelation of MnChemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Current progress on innate immune evasion mediated by NFrontiers in immunology · 2023Review
- Metal retention and replacement in QueD2 protect queuosine-tRNA biosynthesis in metal-starvedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Metal sequestration by S100 proteins in chemically diverse environments.Trends in microbiology · 2022Review
- Adherence Enables Neisseria gonorrhoeae to Overcome Zinc Limitation Imposed by Nutritional Immunity Proteins.Infection and immunity · 2022Article
- Zinc sequestration by human calprotectin facilitates manganese binding to the bacterial solute-binding proteins PsaA and MntC.Metallomics : integrated biometal science · 2022Article
- Managing Manganese: The Role of Manganese Homeostasis in Streptococcal Pathogenesis.Frontiers in cell and developmental biology · 2022Review
- The Innate Immune Protein Calprotectin Interacts With and Encases Biofilm Communities ofFrontiers in cellular and infection microbiology · 2022Article
- Bacterial Responses to Iron Withholding by Calprotectin.Biochemistry · 2021Review
- Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin.Journal of the American Chemical Society · 2021Article
- Nutritional immunity: targeting fungal zinc homeostasis.Heliyon · 2021Review
- Zinc: Multidimensional Effects on Living Organisms.Biomedicines · 2021Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Human calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/MRP-14 oligomer) is an abundant host-defense protein that is involved in the metal-withholding innate immune response. CP coordinates a variety of divalent first-row transition metal ions, which is implicated in its antimicrobial function, and its ability to sequester nutrient Zn(II) ions from microbial pathogens has been recognized for over two decades. CP has two distinct transition-metal-binding sites formed at the S100A8/S100A9 dimer interface, including a histidine-rich site composed of S100A8 residues His17 and His27 and S100A9 residues His91 and His95. In this study, we report that CP binds Zn(II) at this site using a hexahistidine motif, completed by His103 and His105 of the S100A9 C-terminal tail and previously identified as the high-affinity Mn(II) and Fe(II) coordination site. Zn(II) binding at this unique site shields the S100A9 C-terminal tail from proteolytic degradation by proteinase K. X-ray absorption spectroscopy and Zn(II) competition titrations support the formation of a Zn(II)-His6 motif. Microbial growth studies indicate that the hexahistidine motif is important for preventing microbial Zn(II) acquisition from CP by the probiotic Lactobacillus plantarum and the opportunistic human pathogen Candida albicans. The Zn(II)-His6 site of CP expands the known biological coordination chemistry of Zn(II) and provides new insight into how the human innate immune system starves microbes of essential metal nutrients.
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