Related Experiment Video
Updated: Sep 28, 2026

Assessing the Putative Anticryptococcal Properties of Crude and Clarified Extracts from Mollusks
Published on: December 2, 2022
Secreted proteases from pathogenic fungi
Michel Monod1, Sabrina Capoccia, Barbara Léchenne
1Service de Dermatologie (DHURDV), Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland. Michel.Monod@chuv.hospvd.ch
Abstract:
Many species of human pathogenic fungi secrete proteases in vitro or during the infection process. Secreted endoproteases belong to the aspartic proteases of the pepsin family, serine proteases of the subtilisin family, and metalloproteases of two different families. To these proteases has to be added the non-pepsin-type aspartic protease from Aspergillus niger and a unique chymotrypsin-like protease from Coccidioides immitis. Pathogenic fungi also secrete aminopeptidases, carboxypeptidases and dipeptidyl-peptidases. The function of fungal secreted proteases and their importance in infections vary. It is evident that secreted proteases are important for the virulence of dermatophytes since these fungi grow exclusively in the stratum corneum, nails or hair, which constitutes their sole nitrogen and carbon sources. The aspartic proteases secreted by Candida albicans are involved in the adherence process and penetration of tissues, and in interactions with the immune system of the infected host. For Aspergillus fumigatus, the role of proteolytic activity has not yet been proved. Although the secreted proteases have been intensively investigated as potential virulence factors, knowledge on protease substrate specificities is rather poor and few studies have focused on the research of inhibitors. Knowledge of substrate specificities will increase our understanding about the action of each protease secreted by pathogenic fungi and will help to determine their contribution to virulence.
Insights
Pathogenic fungi secrete various proteases crucial for virulence, aiding in nutrient acquisition and host tissue invasion. Understanding these fungal proteases and their specific targets is key to developing effective antifungal therapies.
Area of Science:
- Mycology
- Biochemistry
- Infectious Diseases
Background:
- Human pathogenic fungi secrete diverse proteases, including aspartic, serine, and metalloproteases.
- These secreted enzymes play roles in fungal nutrition, tissue adherence, invasion, and immune system modulation.
- While investigated as virulence factors, specific functions and substrate specificities of many fungal proteases remain poorly understood.
Purpose of the Study:
- To review the types and known functions of proteases secreted by pathogenic fungi.
- To highlight the importance of understanding protease substrate specificities for elucidating their role in fungal infections.
- To emphasize the need for research into protease inhibitors for potential therapeutic applications.
Main Methods:
- Literature review of studies on fungal secreted proteases.
- Analysis of protease families (aspartic, serine, metalloproteases) and their known roles.
- Discussion of specific examples like Candida albicans and Coccidioides immitis.
Main Results:
- Pathogenic fungi secrete a range of proteases, including endoproteases and exopeptidases.
- Secreted proteases are vital for dermatophytes' nutrient acquisition from keratinous substrates.
- Candida albicans aspartic proteases contribute to adherence, tissue penetration, and immune evasion.
Conclusions:
- Secreted fungal proteases are significant virulence factors with diverse roles in pathogenesis.
- Further research into protease substrate specificities is essential for understanding fungal virulence mechanisms.
- Targeting fungal proteases or their inhibitors presents a promising avenue for antifungal drug development.
Related Concept Videos
Determinants of Bacterial Pathogenicity and Virulence
Role of Matrix Metalloproteases in Degradation of ECM
A...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
Antifungal Agents
Lysosomal Hydrolases

