Calprotectin S100A9 calcium-binding loops I and II are essential for keratinocyte resistance to bacterial invasion.

The Journal of Biological Chemistry
Chantrakorn ChampaiboonM C Herzberg

Abstract

Epithelial cells expressing calprotectin, a heterodimer of S100A8 and S100A9 proteins, are more resistant to bacterial invasion. To determine structural motifs that affect resistance to bacterial invasion, mutations were constructed in S100A9 targeting the calcium-binding loops I and II (E36Q, E78Q, E36Q,E78Q) and the C terminus (S100A9(1-99) and S100A9(1-112)), which contains putative antimicrobial zinc-binding and phosphorylation sites. The S100A8 and mutated S100A9 encoding plasmids were transfected into calprotectin-negative KB carcinoma cells. All transfected cells (except KB-sham) expressed 27E10-reactive heterodimers. In bacterial invasion assays with Listeria monocytogenes and Salmonella enterica serovar Typhimurium (Salmonella typhimurium), cell lines expressing S100A8 in complex with S100A9E36Q, S100A9E78Q, S100A9(1-99), or S100A9(1-112) mutants or the S100A9(1-114) (full-length) calprotectin resisted bacterial invasion better than KB-sham. When compared with KB-S100A8/A9(1-114), cells expressing truncated S100A9(1-99) or S100A9(1-112) with S100A8 also showed increased resistance to bacterial invasion. In contrast, glutamic acid residues 36 and 78 in calcium-binding loops I and II promote resistance in epithelial cell...Continue Reading

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