Different isoforms of secreted aspartyl proteinases (Sap) are expressed by Candida albicans during oral and cutaneous candidosis in vivo

J Med Microbiol. 2001 Aug;50(8):743-747. doi: 10.1099/0022-1317-50-8-743.

Abstract

Distinct isoforms of secreted aspartyl proteinases (Sap) of Candida albicans are important virulence factors for different types of candidosis. Predominant expression of Sap1-3 has been shown to be crucial for superficial infections in experimental mucosal and cutaneous candidosis, whereas Sap4-6 might be important for systemic disease. This in-vivo study investigated Sap expression in two samples from patients with oral candidosis and from cutaneous infection. Two different polyclonal antibodies directed against Sap1-3 and Sap4-6 were used for ultrastructural characterisation of protein localisation and expression. Post-embedding immuno-electron microscopy revealed Sap1-3 and Sap4-6 immunoreactivity in all samples. All C. albicans cells expressed predominantly the proteinases Sap1-3 which were evenly distributed within the cell wall and cytoplasmic membrane. In contrast, Sap4-6 labelling was only evident in a few fungal cells. In particular it was localised at the tips of hyphal cells during invasion. These data suggest a different pathogenetic role for Sap1-3 and Sap4-6 during host-fungal interaction.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Antibodies, Fungal / immunology
  • Aspartic Acid Endopeptidases / immunology
  • Aspartic Acid Endopeptidases / metabolism*
  • Candida albicans / enzymology*
  • Candida albicans / immunology
  • Candida albicans / pathogenicity
  • Candida albicans / ultrastructure
  • Candidiasis, Cutaneous / enzymology*
  • Candidiasis, Oral / enzymology*
  • Female
  • Humans
  • Immunohistochemistry
  • Isoenzymes / immunology
  • Isoenzymes / metabolism
  • Male
  • Microscopy, Immunoelectron
  • Middle Aged
  • Virulence

Substances

  • Antibodies, Fungal
  • Isoenzymes
  • Aspartic Acid Endopeptidases