Related Experiment Video
Updated: Jun 26, 2025

A Soluble Tetrazolium-Based Reduction Assay to Evaluate the Effect of Antibodies on Candida tropicalis Biofilms
Published on: September 16, 2022
Secreted Aspartic Proteinases: Key Factors in Candida Infections and Host-Pathogen Interactions
Grazyna Bras1, Dorota Satala1, Magdalena Juszczak1,2
1Department of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland.
Abstract:
Extracellular proteases are key factors contributing to the virulence of pathogenic fungi from the genus Candida. Their proteolytic activities are crucial for extracting nutrients from the external environment, degrading host defenses, and destabilizing the internal balance of the human organism. Currently, the enzymes most frequently described in this context are secreted aspartic proteases (Saps). This review comprehensively explores the multifaceted roles of Saps, highlighting their importance in biofilm formation, tissue invasion through the degradation of extracellular matrix proteins and components of the coagulation cascade, modulation of host immune responses via impairment of neutrophil and monocyte/macrophage functions, and their contribution to antifungal resistance. Additionally, the diagnostic challenges associated with Candida infections and the potential of Saps as biomarkers were discussed. Furthermore, we examined the prospects of developing vaccines based on Saps and the use of protease inhibitors as adjunctive therapies for candidiasis. Given the complex biology of Saps and their central role in Candida pathogenicity, a multidisciplinary approach may pave the way for innovative diagnostic strategies and open new opportunities for innovative clinical interventions against candidiasis.
Insights
Secreted aspartic proteases (Saps) are vital for Candida virulence, aiding nutrient acquisition, host defense evasion, and antifungal resistance. Targeting Saps offers new strategies for diagnosing and treating candidiasis.
Area of Science:
- Microbiology
- Biochemistry
- Immunology
Background:
- Extracellular proteases are critical virulence factors in pathogenic *Candida* species.
- Secreted aspartic proteases (Saps) are extensively studied for their roles in fungal pathogenesis.
- These enzymes facilitate nutrient acquisition and host tissue damage.
Purpose of the Study:
- To comprehensively review the diverse roles of secreted aspartic proteases (Saps) in *Candida* infections.
- To discuss the implications of Saps in biofilm formation, tissue invasion, and immune modulation.
- To explore diagnostic and therapeutic strategies targeting Saps.
Main Methods:
- Literature review focusing on secreted aspartic proteases in *Candida*.
- Analysis of studies detailing Sap functions in virulence and host interactions.
- Examination of research on Saps as diagnostic biomarkers and therapeutic targets.
Main Results:
- Saps are crucial for biofilm development and invasion by degrading host matrix proteins and coagulation factors.
- These proteases impair neutrophil and macrophage functions, modulating host immune responses.
- Saps contribute to antifungal drug resistance and present diagnostic challenges.
Conclusions:
- Secreted aspartic proteases play a central role in *Candida* pathogenicity, impacting multiple host systems.
- Saps represent promising targets for novel diagnostic biomarkers and adjunctive therapies for candidiasis.
- A multidisciplinary approach is essential for developing innovative interventions against *Candida* infections.
Related Concept Videos
Caspases
Overview of Secretory Vesicles
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Pathophysiology of Peptic Ulcer Disease: Injurious Factors
In the antrum region, G cells secrete the gastrin hormone that binds to gastrin-cholecystokinin-B (CCK2) receptors on parietal and enterochromaffin-like (ECL) cells in the fundic glands. Simultaneously, the vagus nerve releases acetylcholine, which binds...

