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

László Galgóczy, Máté Virágh, Laura Kovács, Beáta Tóth, Tamás Papp, Csaba Vágvölgyi
Author Information
  1. László Galgóczy: Department of Microbiology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary. galgoczi@gmail.com

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.

MeSH Term

Amino Acid Motifs
Amino Acid Sequence
Antifungal Agents
Bacillus subtilis
Escherichia coli
Fungal Proteins
Fungi
Fusarium
Microbial Sensitivity Tests
Micrococcus luteus
Molecular Sequence Data
Penicillium chrysogenum
Phylogeny
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Serratia marcescens

Chemicals

Antifungal Agents
Fungal Proteins

Word Cloud

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