Expression patterns of SRB1 and other stress-related genes in Candida albicans under oxidative, hyperosmotic and thermal stress

Med Mycol. 2019 Jan 1;57(1):114-121. doi: 10.1093/mmy/myy002.

Abstract

Candida albicans, a human fungal pathogen, is able to tolerate certain levels of environmental stresses. Its cell wall plays an important role in cellular homeostasis, responding to environmental stimuli. SRB1 gene encodes a GDP-mannose pyrophosphorylase that catalyzes the formation of the major cell wall component, mannan. The exact relationship between SRB1 and various stresses is not yet fully understood. In current study, C. albicans SC5314 cells were exposed to oxidative, hyperosmotic, and thermal stresses. The expression of SRB1 and related stress response genes, HOG1, CAP1, MKC1, and HSP90, was systematically evaluated in cells exposed to various levels of stress. In addition, the apoptosis and ultrastructural changes of the cells were examined. We found that the expression of SRB1 and related stress response genes significantly increased under oxidative, hyperosmotic, and thermal stresses, and the increased gene expression was correlated with higher percentages of apoptosis and ultrastructural changes in C. albicans cells. We propose that protein glycosylation is associated with stress response that involves SRB1 in C. albicans. Further in-depth studies of SRB1 function should aid our understanding of C. albicans pathogenesis, and provide important clues about the development of novel antifungal compounds for drug resistant C. albicans.

MeSH terms

  • Apoptosis
  • Candida albicans / genetics*
  • Candida albicans / physiology
  • Candida albicans / ultrastructure
  • Cell Membrane / ultrastructure
  • Cell Wall / ultrastructure
  • Fungal Proteins / genetics*
  • Gene Expression Regulation, Fungal / physiology*
  • Heat-Shock Response / genetics
  • Nucleotidyltransferases / genetics*
  • Osmoregulation / genetics
  • Oxidative Stress / genetics
  • Stress, Physiological / genetics*

Substances

  • Fungal Proteins
  • Nucleotidyltransferases
  • mannose 1-phosphate guanylyltransferase