The human innate immune system launches a metal-withholding response during microbial infection. Metal-sequestering host-defense proteins are deployed to sites of infection where they coordinate first-row transition metal ions (Mn, Fe, Zn) and lower the bioavailable levels of these nutrients such that the invading pathogen is confronted with metal limitation. Calprotectin (CP) is an abundant host protein that chelates nutrient metals in the extracellular space. It is a heterooligomer of the Ca(II)-binding polypeptides S100A8 and S100A9, and it exhibits remarkable coordination chemistry because each heterodimer unit contains six different metal-binding sites. We present results from our recent biochemical and biophysical investigations of metal sequestration by CP with focus on its capacity to capture Mn(II) and compete with microbes for this nutrient.

Bioinorganic explorations of the competition for nutrient metal ions at the host/microbe interface

255th National Meeting (2018)

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