Since there is a symbiotic and competitive relationship between microorganisms in the same ecological niche, fungal
defensins have been found to be important resources for
antimicrobial peptides. Here, a fungal
defensin, triintsin, was characterized in a clinical isolate of Trichophyton interdigitale from a patient with
onychomycosis. The comparison of its genomic and
mRNA sequences showed the gene organization and structure of three coding exons separated by two introns. The precursor
peptide of triintsin contained 85
amino acid residues, which were composed of three parts including an N-terminal signal domain of 21 residues, a pro-
peptide of 47 residues that ended at
lysine-
arginine and a mature
peptide of 38 residues at the C-terminus. The 3D-structure established by homology modeling revealed that triintsin presented a representative typical
cysteine-stabilized α-helical and β-sheet fold. The reductive linear
peptide of triintsin was obtained by chemical synthesis. After cyclization to form three pairs of
disulfide bonds, the oxidative-type
peptide displayed broad-spectrum antimicrobial activity against both gram-positive and gram-negative bacteria but also showed anti-fungal activity. Moreover, triintsin can effectively inhibit the growth of clinical strains. Altogether, the
peptide is a human pathogenic fungus-derived
defensin with broad-spectrum antimicrobial activity.