Adherence of Candida albicans to immobilized extracellular matrix proteins is mediated by calcium-dependent surface glycoproteins.

The adherence of Candida albicans to the extracellular matrix proteins type I collagen and fibronectin (Fn) is dependent upon the presence of extracellular calcium. In the absence of calcium, 14 +/- 3% of yeast cells added to type I collagen adhered, whereas 62 +/- 3% of yeast cells adhered in the presence of 2 mM calcium. EDTA and EGTA reduced C. albicans adherence in a dose-dependent manner. Calcium, and to a lesser extent, cesium and magnesium, enhanced yeast cell adherence. The fluorescent probe, terbium (Tb+3), bound to the surface of yeast cells in a dose-dependent manner demonstrating the presence of cationic metal-binding sites on the yeast cell surface. When extracts of C. albicans yeast cells were applied to columns of Fn or gelatin coupled to agarose, two surface proteins of C. albicans were specifically eluted with 10 mM EDTA, 2% alpha-methylmannopyranoside or an Arg-Gly-Asp-containing peptide. The fungal proteins had relative molecular masses of 60,000 and 105,000 in the unreduced state. The proteins were present in the cell membrane as well as the cell wall and were demonstrated to be glycoproteins by their ability to bind concanavalin A. Immunoblot analysis of yeast extracts demonstrated that anti-integrin antibodies to the human fibronectin, vitronectin and complement receptor cross-reacted with the Candida 60 kDa glycoprotein. Thus, calcium-dependent fungal cell wall glycoproteins likely related to integrins may be receptors responsible for yeast cell adherence to host tissue such as the extracellular matrix.