Related Experiment Video
Updated: Dec 23, 2025
Infecting Mice with Malassezia spp. to Study the Fungus-Host Interaction
Published on: November 6, 2019
Identification of Malassezia furfur Secreted Aspartyl Protease 1 (MfSAP1) and Its Role in Extracellular Matrix
Si En Poh1, Joleen P Z Goh2, Chen Fan2
1Molecular Engineering Lab, Institute of Bioengineering and Nanotechnology, Agency for Science Technology and Research, Singapore, Singapore.
Abstract:
Malassezia is the most abundant eukaryotic microbial genus on human skin. Similar to many human-residing fungi, Malassezia has high metabolic potential and secretes a plethora of hydrolytic enzymes that can potentially modify and structure the external skin environment. Here we show that the dominant secreted Malassezia protease isolated from cultured Malassezia furfur is an aspartyl protease that is secreted and active at all phases of culture growth. We observed that this protease, herein named as MfSAP1 (M. furfur secreted aspartyl protease 1) has a broader substrate cleavage profile and higher catalytic efficiency than the previously reported protease homolog in Malassezia globosa. We demonstrate that MfSAP1 is capable of degrading a wide range of human skin associated extracellular matrix (ECM) proteins and ECM isolated directly from keratinocytes and fibroblasts. Using a 3-D wound model with primary keratinocytes grown on human de-epidermized dermis, we show that MfSAP1 protease can potentially interfere with wound re-epithelization in an acute wound model. Taken together, our work demonstrates that Malassezia proteases have host-associated substrates and play important roles in cutaneous wound healing.
Insights
Malassezia furfur secretes a potent aspartyl protease, MfSAP1, that degrades skin extracellular matrix proteins. This enzyme impacts wound healing by potentially disrupting re-epithelialization.
Area of Science:
- Microbiology
- Dermatology
- Biochemistry
Background:
- Malassezia, a dominant skin fungus, possesses metabolic enzymes that can alter the skin environment.
- Secreted fungal enzymes play roles in host-microbe interactions and skin physiology.
Purpose of the Study:
- To identify and characterize the primary secreted protease from Malassezia furfur.
- To investigate the substrate specificity and enzymatic activity of this protease.
- To evaluate the protease's role in skin extracellular matrix degradation and wound healing.
Main Methods:
- Isolation and characterization of a secreted aspartyl protease (MfSAP1) from Malassezia furfur.
- Enzyme activity assays using various substrates, including human skin extracellular matrix proteins.
- Assessment of MfSAP1's effect on keratinocyte function in a 3-D wound healing model.
Main Results:
- Identified MfSAP1 as the dominant secreted aspartyl protease from Malassezia furfur, active throughout culture growth.
- MfSAP1 exhibits broader substrate specificity and higher catalytic efficiency compared to related fungal proteases.
- MfSAP1 degrades key human skin extracellular matrix proteins and interferes with wound re-epithelialization in vitro.
Conclusions:
- Malassezia proteases, exemplified by MfSAP1, target host-associated substrates.
- These fungal enzymes play a significant role in the processes of cutaneous wound healing.
More Related Videos
Related Concept Videos
01:23Role of Matrix Metalloproteases in Degradation of ECM
01:42The Extracellular Matrix
01:29The Extracellular Matrix
In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
Composition of the Extracellular Matrix
The extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse...
01:33Overview of Secretory Vesicles
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
01:24Caspases