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The mode of action of hirsutellin A on eukaryotic cells

J C Liu1, D G Boucias, J C Pendland

  • 1Department of Entomology and Nematology, University of Florida, Gainesville 32611, USA.

Insights

Hirsutellin A (HtA), a novel protein toxin from Hirsutella thompsonii, inhibits invertebrate cell growth and protein synthesis by targeting ribosomes. This mycotoxin shows specificity towards invertebrate cells.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Mycology

Background:

  • Hirsutella thompsonii var thompsonii is an entomopathogenic fungus.
  • Protein toxins produced by entomopathogens can have significant biological activity.

Purpose of the Study:

  • To purify and characterize a novel protein toxin from Hirsutella thompsonii var thompsonii.
  • To investigate the biological activity and mechanism of action of this toxin on invertebrate cells and viral protein synthesis.

Main Methods:

  • Purification of a 16-kDa protein toxin, named hirsutellin A (HtA).
  • Assessment of cytopathic effects and cell growth inhibition on Spodoptera frugiperda (Sf-9) cells.
  • Electron microscopy to observe cellular damage.
  • In vitro inhibition assays using rabbit reticulocyte and wheat germ translation systems.
  • Analysis of ribosomal RNA from treated and untreated cells.

Main Results:

  • HtA induced cytopathic effects and completely inhibited Sf-9 cell growth at 0.5 and 5.0 microM concentrations.
  • Electron microscopy revealed cell hypotrophy and disruption of organelles and membranes in HtA-treated cells.
  • HtA inhibited Brome mosaic virus protein synthesis in vitro and altered ribosomal RNA structure in Sf-9 cells.

Conclusions:

  • HtA is the first identified mycotoxin from an invertebrate mycopathogen with ribosomal inhibiting activity.
  • HtA exhibits specificity towards invertebrate cells, suggesting potential applications in pest control or as a research tool.

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