Host antimicrobial peptide S100A12 disrupts the fungal membrane by direct binding and inhibits growth and biofilm formation of Fusarium species.

Fungal keratitis is the foremost cause of corneal infections worldwide, of which Fusarium spp. is the common etiological agent that causes loss of vision and warrants surgical intervention. An increase in resistance to the available drugs along with severe side effects of the existing antifungals demands for new effective antimycotics. Here, we demonstrate that antimicrobial peptide S100A12 directly binds to the phospholipids of the fungal membrane, disrupts the structural integrity, and induces generation of reactive oxygen species in fungus. In addition, it inhibits biofilm formation by Fusarium spp. and exhibits antifungal property against Fusarium spp. both in vitro and in vivo. Taken together, our results delve into specific effect of S100A12 against Fusarium spp. with an aim to investigate new antifungal compounds to combat fungal keratitis. [ABSTRACT FROM AUTHOR]