Cell progression of biofilm formation in Candida albicans and estimation of aspartic proteinase activity

Elshazly, Rowida Ghareb; Selmi Sobieh, Shaimaa; Sobhy Zaki, Sanaa; Abdel Fattah Abdel Tawab, Sahar

doi:10.21608/jsrs.2022.275792

Cell progression of biofilm formation in Candida albicans and estimation of aspartic proteinase activity

Document Type : Original Article

Authors

¹ Botany department, Faculty of women for Arts, Science and Education, Ain Shams University, Cairo, Egypt

² Botany Department, Faculty of Women for Arts, Science and Education, Ain Shams University, Cairo, Egypt

³ Botany Department, Faculty of Women for Arts, Science and Education, Ain Shams University, Cairo, Egypt.

10.21608/jsrs.2022.275792

Abstract

Yeast cells are commonly used as powerful model system to study morphological phenotype and their processes. The study of morphogenesis of different modes of growth in yeast during biofilm development is an important issue. Cell progression is important tool to understand morphological transition and virulence in C. albicans. Biofilm formation and aspartic proteinase activity are two major important virulence factors associated with the pathogenicity of C. albicans. This study aimed to highlight the formation of biofilm, monitor the development of biofilm progression and estimate the activity of aspartic proteinase. Biofilm formation was assessed by Eliza plate and monitored at different pH values, different incubation time and different media. Biofilm development was visualized microscopically. Cell division and mitotic phases in yeast cells were studied and photographed. The production of aspartic proteinase was assessed by bovine serum albumin agar plates and evaluated at different pH values and different incubation time intervals. Results revealed that C. albicans was positive for biofilm formation and aspartic proteinase production. pH and different media had marked significant effect on biofilm formation. Additionally, the transition from simple yeast budding form to a complex filament structure was time dependent. Moreover, pH showed significant effect on aspartic proteinase activity.

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