Identification of proteins highly expressed in the hyphae of Candida albicans by two-dimensional electrophoresis

Yeast. 2003 Sep;20(12):1053-60. doi: 10.1002/yea.1022.

Abstract

The increase in Candida albicans infections is caused by the increase in therapies resulting in immunocompromised patients. One factor required for C. albicans pathogenicity is the morphological transition from yeast to hypha. The protein profiles of whole extracts from yeasts and hyphae were examined using two-dimensional electrophoresis to identify the proteins related to the morphological transition. Over 900 protein spots were visualized by silver staining and 11 spots were increased more than three-fold reproducibly during hyphal differentiation. Six of the 11 spots were identified by peptide mass fingerprints, of which three represented PRA1, two PHR1 and the last TSA1. Vertical streak patterns of Pra1p and Phr1p indicated that post-translational modifications seem to be caused by variable glycosylation. Comparative proteome analysis between the wild-type and the deletion mutants, CAMB43 (deltapra1) and CAS10 (deltaphr1), further confirmed the identity of PRA1 and PHR1. Interestingly, Pra1p was downregulated in phr1-deleted mutants. Only PHR1 transcription was increased, indicating that PRA1 and TSA1 are controlled at the post-translational level.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoenzymes / biosynthesis
  • Apoenzymes / genetics
  • Blotting, Northern
  • Candida albicans / cytology
  • Candida albicans / genetics
  • Candida albicans / metabolism*
  • Deoxyribodipyrimidine Photo-Lyase / biosynthesis
  • Deoxyribodipyrimidine Photo-Lyase / genetics
  • Electrophoresis, Gel, Two-Dimensional
  • Fungal Proteins / biosynthesis*
  • Fungal Proteins / genetics
  • Gene Expression
  • Hyphae / cytology
  • Hyphae / genetics
  • Hyphae / metabolism*
  • Membrane Glycoproteins*
  • Neoplasm Proteins*
  • Peptide Mapping
  • Peroxidases / biosynthesis
  • Peroxidases / genetics
  • Peroxiredoxins
  • Proteomics / methods
  • RNA, Fungal / genetics
  • RNA, Fungal / metabolism
  • Receptors, Cell Surface / biosynthesis
  • Receptors, Cell Surface / genetics
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Apoenzymes
  • Fungal Proteins
  • Membrane Glycoproteins
  • Neoplasm Proteins
  • PHR1 protein, Candida albicans
  • PRA1 protein, Candida albicans
  • RNA, Fungal
  • Receptors, Cell Surface
  • Peroxidases
  • Peroxiredoxins
  • Deoxyribodipyrimidine Photo-Lyase