The First Whole-Cell Proteome- and Lysine-Acetylome-Based Comparison between Trichophyton rubrum Conidial and Mycelial Stages

J Proteome Res. 2018 Apr 6;17(4):1436-1451. doi: 10.1021/acs.jproteome.7b00793. Epub 2018 Mar 28.

Abstract

Trichophyton rubrum is the most common fungal pathogen in the world, which has been studied as an important dermatophyte model organism. Despite the prevalence of T. rubrum, the available antifungal therapies are not sufficiently efficient. In this study, we performed the first comparison between the two major growth stages of T. rubrum: conidial and mycelial stages, based on their whole-cell proteomes and lysine acetylomes. In total, 4343 proteins were identified in both stages, and 1879 proteins were identified as differentially expressed between the two stages. The results showed that secretory proteases were more abundant in conidia, while aerobic metabolism and protein synthesis were significantly activated in the mycelial stage. In addition, 386 acetylated sites on 285 proteins and 5414 acetylated sites on 2335 proteins were identified in conidia and mycelia, respectively. The acetylation modifications were highly involved in metabolism and protein synthesis in both stages but differentially involved in Kyoto Encyclopedia of Genes and Genomes pathways and in epigenetic regulation between the two stages. Furthermore, inhibition of acetyltransferases or deacetylases significantly inhibited fungal growth and induced apoptosis. These results will enhance our understanding of the biological and physiological characteristics of T. rubrum and facilitate the development of improved therapies targeting these medically important pathogenic fungi.

Keywords: Dermatophytes; Trichophyton rubrum (T. rubrum); label-free quantification; lysine acetylation; proteome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Fungal Proteins / analysis*
  • Gene Expression Regulation, Fungal
  • Lysine
  • Metabolism / genetics
  • Mycelium / chemistry*
  • Peptide Hydrolases / genetics
  • Protein Biosynthesis / genetics
  • Proteome / analysis
  • Spores, Fungal / chemistry*
  • Trichophyton / chemistry*

Substances

  • Fungal Proteins
  • Proteome
  • Peptide Hydrolases
  • Lysine