Comparison of phospholipase and proteinase activity in Candida albicans and C. dubliniensis.
Although the production of virulence enzymes by Candida albicans has been extensively explored, little attention has been given to the virulence factors of C. dubliniensis. In the present study, an attempt was made to investigate phospholipase activity (Pz value) and secretory aspartyl proteinase production of C. dubliniensis and compare it with C. albicans. None of the 87 C. dubliniensis isolates tested, produced phosholipases whereas, in contrast all the 52 (100%) C. albicans isolates tested demonstrated varying degree of phospholipase activity (Pz value: 0.37-0.74), with 35 (67.3%) of them eliciting a higher phospholipase activity (Pz values between 0.37 and 0.50). Only 32% of the C. dubliniensis isolates exhibited moderate activity (score of 1+) of secretory aspartyl proteinase whereas a vast majority (68%) of them were non-proteolytic. On the contrary, a strong proteinase activity (score of 2+) was observed for 79% of C. albicans while the remaining 21% isolates showed moderate proteinase activity (score of 1+). As phospholipases and aspartyl proteinases of C. albicans are considered important virulence factors, the absence or lowered expression of these enzymes in C. dubliniensis may indicate the less virulent nature of this novel yeast species when compared with C. albicans.
Fotedar
R
R
Department of Pathology, The Medical Mycology Unit, College of Medicine, King Khalid University Hospital, Riyadh, Saudi Arabia. rfotedar@hotmail.com
Al-Hedaithy
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SS
D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D002175:Candida / Q000201:enzymology* / Q000472:pathogenicity; D002176:Candida albicans / Q000201:enzymology* / Q000472:pathogenicity; D002177:Candidiasis / Q000382:microbiology; D005260:Female; D006761:Hospitals; D006801:Humans; D008297:Male; D010740:Phospholipases / Q000378:metabolism*; D012529:Saudi Arabia; D014774:Virulence
D010740:Phospholipases; D016282:Aspartic Acid Endopeptidases