Open AccessA Candida albicans metallopeptidase degrades constitutive proteins of extracellular matrix
Author(s) -
Rodier MarieHélène,
El Moudni Brahim,
KauffmannLacroix Catherine,
Daniault Gyslaine,
Jacquemin JeanLouis
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13733.x
Subject(s) - fibronectin , extracellular matrix , laminin , candida albicans , extracellular , enzyme , biology , biochemistry , proteolytic enzymes , yeast , virulence , corpus albicans , microbiology and biotechnology , gene
Among potential virulence factors of Candida albicans , enzymes seem to play an important role. Many studies concern the secreted aspartic proteinases (saps), and the degradation of some components of the subendothelial extracellular matrix by the isoenzyme sap2 has been proved. Nevertheless, other proteolytic enzymes could be involved in the pathogenicity of the yeast. We studied the degradation of four constitutive proteins of the extracellular matrix: type I and IV collagens, laminin and fibronectin, by a 95‐kDa metallopeptidase, localised in the cell wall of C. albicans . Each of these constituents was incubated with the purified enzyme and its degradation products analysed by an electrophoretic method. We observed that type I collagen and fibronectin were totally degraded by the enzyme whereas type IV collagen and laminin were only partially degraded. The C. albicans metallopeptidase may play a role in the degradation of the subendothelial extracellular matrix components. This enzyme could facilitate the migration of the yeast in the tissues after crossing the endothelial layer, allowing the fungal invasion of target organs.