An extracellular antifungal protein of 28 kDa (exAFP-C28) was identified from an endophytic fungus Colletotrichum
sp. DM-06. After purification, the MIC value of exAFP-C28 against Candida albicans, a well-known human
pathogenic fungus was found to be 32 μg/mL that unaffected the human red blood cells. The antifungal activity associated
with exAFP-C28 was manifested by the increased membrane permeability of C. albicans cells followed by disruption.
Proteomics and bioinformatics analyses revealed that several peptide fragments of exAFP-C28 have identity with the bacterial
50S ribosomal protein L10, and a stretch of 55 amino acids of two peptide fragments corresponding to the Nterminus
of L10 protein is capable of forming amphipathic helix required for membrane penetration. Taken together, our
results suggest that the exAFP-C28 protein from Colletotrichum sp. DM-06 is a promising therapeutic agent in controlling
candidiasis disease in animals including humans.
Keywords: Antifungal protein, Candida albicans, Colletotrichum sp. DM-06, endophytic fungus, extracellular protein, pathogenic
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