Glucosylceramides are required for mycelial growth and full virulence in Penicillium digitatum

Biochem Biophys Res Commun. 2014 Dec 12;455(3-4):165-71. doi: 10.1016/j.bbrc.2014.10.142. Epub 2014 Nov 4.

Abstract

Glucosylceramides (GlcCers) are important lipid components of the membrane systems of eukaryotes. Recent studies have suggested the roles for GlcCers in regulating fungal growth and pathogenesis. In this study, we report the identification and functional characterization of PdGcs1, a gene encoding GlcCer synthase (GCS) essential for the biosynthesis of GlcCers, in Penicilliumdigitatum genome. We demonstrated that the deletion of PdGcs1 in P. digitatum resulted in the complete loss of production of GlcCer (d18:1/18:0 h) and GlcCer (d18:2/18:0 h), a decrease in vegetation growth and sporulation, and a delay in spore germination. The virulence of the PdGcs1 deletion mutant on citrus fruits was also impaired, as evidenced by the delayed occurrence of water soaking lesion and the formation of smaller size of lesion. These results suggest that PdGcs1 is a bona fide GCS that plays an important role in regulating cell growth, differentiation, and virulence of P. digitatum by controlling the biosynthesis of GlcCers.

Keywords: GlcCers; GlcCers synthase; Penicillium digitatum; Virulence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Proliferation
  • Chromatography, High Pressure Liquid
  • Citrus / microbiology*
  • DNA Primers
  • Fungal Proteins / genetics
  • Fungal Proteins / physiology*
  • Gene Deletion*
  • Gene Expression Regulation, Fungal*
  • Genetic Complementation Test
  • Glucosylceramides / physiology*
  • Glucosyltransferases / genetics
  • Glucosyltransferases / physiology*
  • Membrane Microdomains / chemistry
  • Mutation
  • Penicillium / metabolism*
  • Penicillium / pathogenicity
  • Plant Diseases / microbiology
  • Tandem Mass Spectrometry
  • Virulence

Substances

  • DNA Primers
  • Fungal Proteins
  • Glucosylceramides
  • Glucosyltransferases
  • ceramide glucosyltransferase