phospholipases

Candida species are a leading cause of fungal infections worldwide. Candidiasis, the disease caused by Candida , represents a significant public health concern globally. Candida albicans is the most common causative agent, responsible for 50 - 90% of invasive candidiasis cases. Candida albicans employs various virulence factors to adhere to, invade host tissues, and cause disease.

This study aimed to detect and compare the virulence factors of C. albicans , including hydrophobicity, biofilm formation, ergosterol content, and secretory enzymes, in clinical and environmental samples.

A total of 105 clinical and 165 environmental samples suspected of containing C. albicans were collected from Imam Khomeini Hospital in Ahvaz, Iran. The isolates were evaluated for five potential virulence factors: Ergosterol content, cell surface hydrophobicity (CSH), biofilm formation, protease activity, and phospholipase activity.

Sixty C. albicans isolates were identified, consisting of 30 clinical and 30 environmental isolates. Biofilm production was observed in 100% of clinical isolates and 80% of environmental isolates (P < 0.001). Protease activity was detected in 66.6% of clinical isolates and 76.7% of environmental isolates (P = 0.008). Phospholipase activity was present in 60% of clinical isolates and 76.7% of environmental isolates (P = 0.262). Clinical isolates exhibited higher CSH (66.4 ± 9.8) compared to environmental isolates (47.7 ± 17.0) (P < 0.001). The ergosterol content was 1.2 ± 0.5 in clinical isolates and 1.1 ± 0.3 in environmental isolates.

Biofilm formation was a consistent characteristic of clinical isolates, while phospholipase and protease activity were more prevalent in environmental C. albicans isolates. The results suggest possible cross-contamination between patients and the environment, as the virulence factors of clinical and environmental isolates were similar.

  Candida glabrata is an opportunistic yeast that has emerged as a cause of human fungal disease, and is a complex of three closely related species. Until now, there is not enough information about its virulence attributes. Moreover, its resistance to echinocandins has been documented, which is a cause of clinical concern. The objective of this study was to evaluate the in vitro production of aspartyl proteinase, phospholipase, esterase, hemolysin, DNase, and coagulase in a subset of 107 Mexican clinical isolates of C. glabrata sensu stricto, as well as to determinate its echinocandin susceptibility. The enzymatic determinations were carried out in plate assays using specific substrates, excepting coagulase, which was determined by the classic tube test. Antifungal susceptibility testing was determined in accordance with the CLSI broth microdilution
method. Aspartyl proteinase, hemolysin, and phospholipase were detected in 100%, 95%, and 79% of isolates, respectively. Blood isolates were associated with a very strong activity of aspartyl proteinase and hemolysin, and those recovered from vaginal swabs were associated with very strong production of aspartyl proteinase, phospholipase, and hemolysin. All isolates were susceptible to
echinocandins, except one bloodstream isolate, which was resistant to echinocandins. A very strong activity of aspartyl proteinase and hemolysin was particularly associated with both, bloodstream, and vaginal swab isolates. Echinocandin resistance was rare