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Aspartyl protease MfSAP2 is a key virulence factor in mycelial form of skin fungi Malassezia furfur

Summary

Malassezia furfur is a common skin fungus that can change from round yeast cells to thread-like filaments. When it becomes thread-like, it produces a special enzyme called MfSAP2 that damages the proteins holding together the dead skin cells that form our skin’s protective barrier. This damage may be responsible for the patches and discoloration seen in pityriasis versicolor, a common skin condition.

Background

Malassezia furfur is a dimorphic fungus that exists primarily as yeast but can transition to mycelial forms in certain conditions. The mycelial form is enriched in pityriasis versicolor (PV) lesions, a skin condition characterized by hyper- or hypopigmented scales. The molecular mechanisms by which M. furfur hyphae contribute to PV disease pathology remain poorly understood.

Objective

This study aimed to identify and characterize virulence factors expressed during the yeast-to-hyphal transition of M. furfur that may contribute to pityriasis versicolor pathogenesis. The researchers investigated changes in extracellular proteolytic activity and protease expression during mycelial induction.

Results

MfSAP2 expression was dramatically upregulated (10-300-fold) during mycelial formation compared to yeast. Aspartyl proteases dominated the secreted protease activity profile in hyphal cultures. Recombinant MfSAP2 efficiently degraded corneodesmosome proteins, particularly corneodesmosin (CDSN), both in vitro and in 3D human skin models.

Conclusion

MfSAP2 is identified as a key virulence factor specifically expressed in the mycelial form of M. furfur that degrades skin barrier proteins, particularly those maintaining corneocyte adhesion. This protease may play a crucial role in pityriasis versicolor pathogenesis and represents a potential therapeutic target for disease management.
  • Published in:Biochemical Journal,
  • Study Type:Experimental Research,
  • Source: 10.1042/BCJ20253109, PMID: 41332240
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