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Secreted proteases from dermatophytes.

Michel Monod1

  • 1Service de Dermatologie et Vénéréologie, Laboratoire de Mycologie, BT422, Centre Hospitalier Universitaire Vaudois, 1011 Lausanne, Switzerland. Michel.Monod@chuv.ch

Mycopathologia
|May 15, 2008
PubMed
Summary

Dermatophyte fungi use unique proteases and sulphite to break down keratin. This sulphitolysis process is essential for digesting tough skin, nail, and hair tissues, aiding fungal infection.

Area of Science:

  • Mycology
  • Biochemistry
  • Dermatology

Background:

  • Dermatophytes are specialized fungi causing infections of keratinized tissues.
  • Proteolytic enzymes are crucial for dermatophyte virulence.
  • Dermatophyte proteases share similarities with Aspergillus spp. proteases.

Purpose of the Study:

  • To investigate the unique proteolytic mechanisms of dermatophytes.
  • To understand the role of sulphite in keratin degradation by dermatophytes.

Main Methods:

  • Analysis of secreted endo- and exoproteases.
  • Investigation of sulphite excretion and its effect on keratin structure.

Main Results:

  • Dermatophytes secrete multiple endoproteases belonging to subtilisin and fungalysin families.

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  • Dermatophytes excrete sulphite, a reducing agent.
  • Sulphite directly cleaves disulfide bonds in keratin, facilitating protease access.
  • Conclusions:

    • Sulphitolysis, involving sulphite action on keratin disulfide bonds, is a key step preceding protease digestion.
    • This mechanism is essential for dermatophytes to degrade compact keratinized tissues.
    • The dual action of sulphite and proteases enhances dermatophyte virulence.