title: Candida albicans growth studies: a hypothesis for the pathogenesis of Candida infections in burns.
abstract: The proteolytic environment in which Candida albicans exists strongly affects its virulence. To determine whether virulence might be related to C. albicans growth in different proteolytic environments, we measured renal fungal load in burned mice and found significantly greater Candida census in kidneys from mice that were challenged with a high proteinase-generating parent C. albicans (MY 1044) versus those that were challenged with its low proteinase-generating mutant (MY 1049). In vitro, MY 1044 cells grew faster than MY 1049 cells in media that contained sera from burned mice as the only nitrogen source. Augmentation of media with proteinase or a mixture of amino acids increased growth of MY 1049 cells, whereas augmentation with proteinase inhibitor decreased MY 1044 growth. In conclusion, in vitro growth of both the mutant and its parent strain was affected by the proteolytic environment in which they existed; thus, virulence differences for MY 1044 and MY 1049 could be due in part to growth differences between these two strains in different proteolytic environments. These results were combined with existing observations, and we proposed a theory for the pathogenesis of C. albicans in burns.
authors.affiliation: Department of Physiology and Biophysics, University of Cincinnati College of Medicine, OH.
authors.forename: A N
authors.initials: AN
authors.lastname: Neely
authors.forename: M M
authors.initials: MM
authors.lastname: Orloff
authors.forename: I A
authors.initials: IA
authors.lastname: Holder
mesh_terms: D000596:Amino Acids / Q000494:pharmacology; D000818:Animals; D002056:Burns / Q000150:complications*; D002176:Candida albicans / Q000254:growth & development* / Q000472:pathogenicity; D002177:Candidiasis / Q000209:etiology*; D002478:Cells, Cultured; D003470:Culture Media; D010450:Endopeptidases / Q000502:physiology*; D005260:Female; D051379:Mice; D011480:Protease Inhibitors / Q000494:pharmacology; D012694:Serine / Q000494:pharmacology; D013820:Thermolysin / Q000494:pharmacology; D014774:Virulence; D014946:Wound Infection / Q000382:microbiology*; D000511:alpha-Macroglobulins / Q000494:pharmacology
chemical_list: D000596:Amino Acids; D003470:Culture Media; D011480:Protease Inhibitors; D000511:alpha-Macroglobulins; D012694:Serine; D010450:Endopeptidases; D013820:Thermolysin