The heterodimeric complex of the two Ca2+-binding S100 proteins S100A8 and A9, also known as calgranulin A and B or calprotectin, exhibits selective biostatic activity at high concentrations against C. albicans (Murthy et al. 1993). Zinc chelation was proposed as a potentially important host defense function of calprotectin (Clohessy and Golden 1995) and it was shown that intact calprotectin, consisting of both subunits, is necessary to form a zinc-binding site capable of inhibiting microbial growth (Sohnle et al. 2000).
Calgranulin C (S100 A12), representing a minor calgranulin in neutrophils, demonstrated filariacidal and filariastatic activity (Gottsch et al. 1999) and a short C-terminal peptide fragment of calgranulin c, named "calcitermin", exhibited bactericidal activity against Gram-negative bacteria, which interestingly was potentiated by adding Zn2+ (Cole et al. 2001).
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