ArticleJournal of the American Chemical Society2013
Contributions of the S100A9 C-terminal tail to high-affinity Mn(II) chelation by the host-defense protein human calprotectin.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 73 citations in OpenAlex.
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- The Abundance Paradox of S100A8/A9 in Neutrophils: Functional Logic of Calprotectin Dominance in the Cytosolic Proteome.International journal of molecular sciences · 2026Review
- Metal-independent effects of calprotectin on cocultures ofbioRxiv : the preprint server for biology · 2026Article
- Calprotectin-mediated survival ofmBio · 2025Article
- Metals at the Host-Fungal Pathogen Battleground.Annual review of microbiology · 2024Review
- Manganese uptake by MtsABC contributes to the pathogenesis of human pathogen group A streptococcus by resisting host nutritional immune defenses.Infection and immunity · 2024Article
- Nutritional Immunity and Fungal Pathogens: a New Role for Manganese.Current clinical microbiology reports · 2024Article
- Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins.ACS chemical neuroscience · 2024Article
- Iron Sequestration by Murine Calprotectin Induces Starvation Responses inACS infectious diseases · 2024Article
- 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
- Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- S100A12 promotes Mn(II) binding to pneumococcal PsaA and staphylococcal MntC by Zn(II) sequestration.Journal of inorganic biochemistry · 2022Article
- 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 Sensor Histidine Kinase ArlS Is Necessary for Staphylococcus aureus To Activate ArlR in Response to Nutrient Availability.Journal of bacteriology · 2021Article
- Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin.Journal of the American Chemical Society · 2021Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human calprotectin (CP) is an antimicrobial protein that coordinates Mn(II) with high affinity in a Ca(II)-dependent manner at an unusual histidine-rich site (site 2) formed at the S100A8/S100A9 dimer interface. We present a 16-member CP mutant family where mutations in the S100A9 C-terminal tail (residues 96-114) are employed to evaluate the contributions of this region, which houses three histidines and four acidic residues, to Mn(II) coordination at site 2. The results from analytical size-exclusion chromatography, Mn(II) competition titrations, and electron paramagnetic resonance spectroscopy establish that the C-terminal tail is essential for high-affinity Mn(II) coordination by CP in solution. The studies indicate that His103 and His105 (HXH motif) of the tail complete the Mn(II) coordination sphere in solution, affording an unprecedented biological His6 site. These solution studies are in agreement with a Mn(II)-CP crystal structure reported recently (Damo, S. M.; et al. Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 3841). Remarkably high-affinity Mn(II) binding is retained when either H103 or H105 are mutated to Ala, when the HXH motif is shifted from positions 103-105 to 104-106, and when the human tail is substituted by the C-terminal tail of murine S100A9. Nevertheless, antibacterial activity assays employing human CP mutants reveal that the native disposition of His residues is important for conferring growth inhibition against Escherichia coli and Staphylococcus aureus. Within the S100 family, the S100A8/S100A9 heterooligomer is essential for providing high-affinity Mn(II) binding; the S100A7, S100A9(C3S), S100A12, and S100B homodimers do not exhibit such Mn(II)-binding capacity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.