ACandida albicansmetallopeptidase degrades constitutive proteins of extracellular matrix

Abstract

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.

Unmatched Level of Molecular Convergence among Deeply Divergent Complex Multicellular Fungi

“…In non-CM fungi and vegetative mycelia of CM species, the shared developmentally regulated gene families function in processes ranging from plant–fungal interactions ( Maillet et al. 2011 ), host protein degradation ( Rodier et al. 1999 ) or appressorium development in pathogenic fungi ( Geoghegan et al.…”

The genome of newly classified Ochroconis mirabilis: Insights into fungal adaptation to different living conditions

“…Among the four M10A peptidases, three (UM578_7033, UM578_12210 and UM578_12211) are similar to myroilysin that was reported to have elastinolytic activity and synergistic effect in collagen degradation [ 32 ]. The matrix metallopeptidase from Candida albicans was reported to degrade fibronectin and type I collagen completely as well as partially degrade laminin and type IV collagen [ 33 , 34 ]. Astacin family peptidases (family M12A) have diverse functions ranging from digestion of food to the processing of extracellular matrix components [ 35 ].…”

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