The histidine-rich salivary peptides of the histatin family are known to bind copper (Cu) and other metal ions in vitro, but the details of these interactions are poorly understood and their implications on in vivo antifungal activity have not been established. Here, we show that the availability of Cu during exposure of <i>Candida albicans</i> to Histatin-5 modulates its antifungal activity, and provide evidence suggesting that this modulation is due to a direct interaction between Cu and the peptide. Together, our results establish new structure-function relationships linking specific histidine residues with Cu-binding affinity and antifungal activity, and provide further evidence for the involvement of metals in modulating the biological activity of these antifungal peptides.

Coping with intruders: Exploitation of metals by histatin antimicrobial peptides

254th National Meeting (2017)

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