Adherence of Candida albicans to components of the subendothelial extracellular matrix.
Candida albicans yeasts adhered avidly to extracellular matrix (ECM) proteins, type IV collagen, laminin, and fibronectin immobilized on plastic. Type IV collagen showed an increase of adherence of 400% above control values; laminin, 300%; and fibronectin, 150%. In addition, all three (in quantities of 0.02-200 micrograms/well of a culture tray) bound yeasts in a dose-response fashion. Adherence was inhibited when the proteins were preincubated with specific antibody, except with type IV collagen. Soluble laminin or fibronectin inhibited yeast adherence to the same proteins by 36 and 94%, respectively. Soluble fibronectin bound to the yeast surface and in so doing inhibited subsequent yeast adherence to fibronectin by 66%. By comparison, Candida albicans yeasts adhered in smaller numbers to glycosaminoglycans (GAGs). Keratan sulfate, hyaluronic acid, chondroitin sulfate, Type B, and heparin actually decreased yeast adherence compared to control from 10% to 25%.
Klotz
S A
SA
Department of Medicine, Veterans Administration, Shreveport, LA 71101-4295.
D000818:Animals; D000906:Antibodies; D002176:Candida albicans / Q000378:metabolism*; D002448:Cell Adhesion; D003094:Collagen / Q000276:immunology / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism*; D005353:Fibronectins / Q000276:immunology / Q000378:metabolism; D007797:Laminin / Q000276:immunology / Q000378:metabolism; D012995:Solubility
D000906:Antibodies; D005353:Fibronectins; D007797:Laminin; D003094:Collagen