Trichophyton rubrum secreted and membrane-associated carboxypeptidases

Details

Serval ID
serval:BIB_F45B34C93D65
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Trichophyton rubrum secreted and membrane-associated carboxypeptidases
Journal
International Journal of Medical Microbiology
Author(s)
Zaugg C., Jousson O., Léchenne B., Staib P., Monod M.
ISSN
1618-0607
Publication state
Published
Issued date
2008
Peer-reviewed
Oui
Volume
298
Number
7-8
Pages
669-682
Language
english
Abstract
Dermatophytes are the most common agents of superficial mycoses, and exclusively infect stratum corneum, nails or hair. Therefore, secreted proteolytic activity is considered a virulence trait of these fungi. In a medium containing protein as a sole nitrogen and carbon source Trichophyton rubrum secretes a metallocarboxypeptidase (TruMcpA) of the M14 family according to the MEROPS proteolytic enzyme database. TruMcpA is homologous to human pancreatic carboxypeptidase A, and is synthesized as a precursor in a preproprotein form. The propeptide is removed to generate the mature active enzyme alternatively by either one of two subtilisins which are concomitantly secreted by the fungus. In addition, T. rubrum was shown to possess two genes (TruSCPA and TruSCPB) encoding serine carboxypeptidases of the S10 family which are homologues of the previously characterized Aspergillus and Penicillium secreted acid carboxypeptidases. However, in contrast to the Aspergillus and Penicillium homologues, TruScpA and TruScpB enzymes are not secreted into the environment, but are membrane-associated with a glycosylphosphatidylinositol (GPI) anchor. During infection, T. rubrum secreted and GPI-anchored carboxypeptidases may contribute to fungal virulence by cooperating with previously characterized endoproteases and aminopeptidases in the degradation of compact keratinized tissues into assimilable amino acids and short peptides.
Keywords
Amino Acid Sequence, Blotting, Western, Carboxypeptidases, Culture Media, DNA, Fungal, Humans, Molecular Sequence Data, Proteins, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Trichophyton, Virulence Factors
Pubmed
Web of science
Create date
22/01/2009 12:29
Last modification date
20/08/2019 16:21
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