Antifungal peptides homologous to the Penicillium chrysogenum antifungal protein (PAF) are widespread among Fusaria

Peptides. 2013 Jan:39:131-7. doi: 10.1016/j.peptides.2012.10.016. Epub 2012 Nov 19.

Abstract

Putative antifungal peptide encoding genes containing Penicillium chrysogenum antifungal protein (PAF) characteristic amino acid motifs were identified in 15 Fusarium isolates, representing 10 species. Based on the predicted sequences of mature peptides, discrepancy in one, two or three amino acids was observed between them. Phylogenetic investigations revealed that they show high amino acid sequence similarity to PAF and they belong to the group of fungal derived antifungal peptides with PAF-cluster. Ten from the 15 partially purified <10 kDa peptide fraction of Fusarium ferment broths showed antifungal activity. The presence of approximately 6.3 kDa molecular weight peptides was detected in all of the antifungally active ferment broths, and this peptide was isolated and purified from Fusarium polyphilaidicum. The minimal inhibitiory concentrations of F. polyphilaidicum antifungal protein (FPAP) were determined against different filamentous fungi, yeasts and bacteria. Filamentous fungal species were the most susceptible to FPAF, but some yeasts were also slightly sensitive.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Antifungal Agents / isolation & purification
  • Antifungal Agents / pharmacology*
  • Bacillus subtilis / drug effects
  • Escherichia coli / drug effects
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification
  • Fungal Proteins / pharmacology*
  • Fungi / drug effects
  • Fusarium / genetics*
  • Microbial Sensitivity Tests
  • Micrococcus luteus / drug effects
  • Molecular Sequence Data
  • Penicillium chrysogenum / genetics
  • Phylogeny
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Serratia marcescens / drug effects

Substances

  • Antifungal Agents
  • Fungal Proteins