The secreted aspartate proteinase of Candida albicans: physiology of secretion and virulence of a proteinase-deficient mutant

J Gen Microbiol. 1990 Apr;136(4):687-94. doi: 10.1099/00221287-136-4-687.


It was established that Candida albicans grew rapidly in a simple medium containing yeast extract (0.2%, w/v) plus glucose (2%, w/v). These cultures were in or near to a state of nitrogen limitation and the concentration of secreted aspartate proteinase increased rapidly (within 3-4 h) on addition of BSA. Synthesis and secretion were apparently controlled both positively (induction by albumin or, more probably, the peptides produced from it) and negatively (repression by NH4Cl). A small intracellular pool of the enzyme was detected during production of the enzyme and this pool decreased with the cessation of synthesis and secretion. A stable mutant, IR24, was isolated which secreted less than 0.3% of the amount of the proteinase exported by the parent strain ATCC 10261. The LD50 values for mutant IR24 and the parent strain administered intravenously to mice were greater than 1.0 x 10(9) and 1.6 x 10(6) c.f.u. kg-1 respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspartic Acid Endopeptidases
  • Candida albicans / genetics
  • Candida albicans / pathogenicity
  • Candida albicans / physiology*
  • Candidiasis / metabolism
  • Candidiasis / pathology
  • Endopeptidases / genetics
  • Endopeptidases / metabolism*
  • Female
  • Gene Expression
  • Lethal Dose 50
  • Mice
  • Mice, Inbred Strains
  • Mutation
  • Virulence


  • Endopeptidases
  • Aspartic Acid Endopeptidases