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Lookup NU author(s): Professor John Common
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2025 The Author(s). Malassezia is the dominant genus of fungi residing on human skin and is associated with both healthy skin and many dermatological conditions. Among these skin diseases, pityriasis versicolor (PV) has strong etiological connections with Malassezia. In the hyper- or hypo-pigmented scales of PV patients, Malassezia is enriched in its mycelial form, which is rarely present on healthy skin. How these Malassezia hyphae contribute to disease pathology in PV is unknown. In this study, we observed a distinct shift in the extracellular proteolytic activity when Malassezia furfur transitions from yeast to hyphae. We identified that the expression of the aspartyl protease MfSAP2 is dramatically up-regulated at both the mRNA and protein level when M. furfur is in the mycelial form. We determined the protease substrate specificity and observed that MfSAP2 can degrade corneodesmosome proteins, which are intercellular adhesive proteins between corneocytes in the stratum corneum. In a 3D human skin model with MfSAP2 treatment, we observed clear degradation of corneodesmosin, a component of the corneodesmosome. Taken together, our study demonstrates that a secreted protease is a key virulence factor associated with M. furfur mycelium and is potentially involved in the disease pathogenesis of PV.
Author(s): Chua W, Hei Y, Koh LF, Yap BLH, Saw HL, Maciel Fernandes TH, da Silva EB, Goh S, Dawson TL, O'Donoghue AJ, Common JE, Li H
Publication type: Article
Publication status: Published
Journal: Biochemical Journal
Year: 2026
Volume: 483
Issue: 1
Pages: 23-36
Print publication date: 01/01/2026
Online publication date: 24/12/2025
Acceptance date: 27/11/2025
Date deposited: 23/01/2026
ISSN (print): 0264-6021
ISSN (electronic): 1470-8728
Publisher: Portland Press
URL: https://doi.org/10.1042/BCJ20253109
DOI: 10.1042/BCJ20253109
Data Access Statement: All data and reagents are available from the authors upon request.
PubMed id: 41332240
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