Structural diversity and bioactivities of peptaibol compounds from the longibrachiatum clade of the filamentous fungal genus trichoderma

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Researchers

  • Tamás Marik
  • Chetna Tyagi
  • Dóra Balázs
  • Péter Urbán
  • Ágnes Szepesi
  • László Bakacsy
  • Gábor Endre
  • Dávid Rakk
  • András Szekeres
  • Aino Andersson

  • Heidi Salonen

  • Irina S. Druzhinina
  • Csaba Vágvölgyi
  • László Kredics

Research units

  • University of Szeged
  • University of Pecs
  • Vienna University of Technology
  • Nanjing Agricultural University

Abstract

This study examined the structural diversity and bioactivity of peptaibol compounds produced by species from the phylogenetically separated Longibrachiatum Clade of the filamentous fungal genus Trichoderma, which contains several biotechnologically, agriculturally and clinically important species. HPLC-ESI-MS investigations of crude extracts from 17 species of the Longibrachiatum Clade (T. aethiopicum, T. andinense, T. capillare, T. citrinoviride, T. effusum, T. flagellatum, T. ghanense, T. konilangbra, T. longibrachiatum, T. novae-zelandiae, T. pinnatum, T. parareesei, T. pseudokoningii, T. reesei, T. saturnisporum, T. sinensis, and T. orientale) revealed several new and recurrent 20-residue peptaibols related to trichobrachins, paracelsins, suzukacillins, saturnisporins, trichoaureocins, trichocellins, longibrachins, hyporientalins, trichokonins, trilongins, metanicins, trichosporins, gliodeliquescins, alamethicins and hypophellins, as well as eight 19-residue sequences from a new subfamily of peptaibols named brevicelsins. Non-ribosomal peptide synthetase genes were mined from the available genome sequences of the Longibrachiatum Clade. Their annotation and product prediction were performed in silico and revealed full agreement in 11 out of 20 positions regarding the amino acids predicted based on the signature sequences and the detected amino acids incorporated. Molecular dynamics simulations were performed for structural characterization of four selected peptaibol sequences: paracelsins B, H and their 19-residue counterparts brevicelsins I and IV. Loss of position R6 in brevicelsins resulted in smaller helical structures with higher atomic fluctuation for every residue than the structures formed by paracelsins. We observed the formation of highly bent, almost hairpin-like, helical structures throughout the trajectory, along with linear conformation. Bioactivity tests were performed on the purified peptaibol extract of T. reesei on clinically and phytopathologically important filamentous fungi, mammalian cells, and Arabidopsis thaliana seedlings. Porcine kidney cells and boar spermatozoa proved to be sensitive to the purified peptaibol extract. Peptaibol concentrations =0.3 mg ml-1 deterred the growth of A. thaliana. However, negative effects to plants were not detected at concentrations below 0.1 mg ml-1, which could still inhibit plant pathogenic filamentous fungi, suggesting that those peptaibols reported here may have applications for plant protection.

Details

Original languageEnglish
Article number1434
Number of pages38
JournalFrontiers in Microbiology
Volume10
Issue numberJUN
Publication statusPublished - 1 Jan 2019
MoE publication typeA1 Journal article-refereed

    Research areas

  • Antifungal activity, Arabidopsis, Brevicelsin, Longibrachiatum, Mammalian cells, Mass spectrometry, Peptaibol, Trichoderma

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