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Trichophyton rubrum secreted and membrane-associated carboxypeptidases

Christophe Zaugg1, Olivier Jousson, Barbara Léchenne

  • 1Service de Dermatologie et Vénéréologie, Laboratoire de Mycologie, BT422, Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland.

International Journal of Medical Microbiology : IJMM
|January 29, 2008
PubMed

Insights

Trichophyton rubrum secretes carboxypeptidases that degrade keratin, aiding fungal infections. These enzymes, both secreted and membrane-bound, work with others to break down tough tissues for nutrient absorption.

Area of Science:

  • Mycology
  • Biochemistry
  • Molecular Biology

Background:

  • Dermatophytes cause superficial mycoses by infecting keratinized tissues.
  • Proteolytic activity is a key virulence factor for these fungi.
  • Trichophyton rubrum is a common dermatophyte responsible for human fungal infections.

Purpose of the Study:

  • To investigate the carboxypeptidases secreted and associated with Trichophyton rubrum.
  • To understand the role of these enzymes in fungal virulence and keratin degradation.
  • To characterize the TruMcpA metallocarboxypeptidase and the TruScpA/B serine carboxypeptidases.

Main Methods:

  • Enzyme activity assays in protein-rich media.
  • Gene identification and characterization.
  • Analysis of enzyme localization (secreted vs. membrane-associated).
  • Homology comparisons with known carboxypeptidases.

Main Results:

  • Trichophyton rubrum secretes a metallocarboxypeptidase (TruMcpA) and two membrane-associated serine carboxypeptidases (TruScpA, TruScpB).
  • TruMcpA is processed by secreted subtilisins.
  • TruScpA and TruScpB are anchored to the membrane via GPI anchors, unlike homologs in other fungi.
  • These carboxypeptidases likely cooperate with other proteases to break down keratin.

Conclusions:

  • Secreted and membrane-bound carboxypeptidases of T. rubrum are crucial for virulence.
  • These enzymes contribute to the degradation of keratinized tissues, facilitating nutrient acquisition.
  • The dual localization of carboxypeptidases highlights a complex strategy for fungal invasion.

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