Glycosaminoglycans inhibit Candida albicans adherence to extracellular matrix proteins.
The ability of Candida albicans to adhere to subendothelial extracellular matrix (ECM) may be important in the pathogenesis of disseminated candidiasis. ECM proteins, such as fibronectin, laminin, and types I and IV collagen bind C. albicans avidly. These proteins all possess heparin-binding domains. The influence of the glycosaminoglycans (GAGS) including heparin, heparan sulfate and dextran sulfate on C. albicans adherence to subendothelial ECM and ECM proteins was studied. It was demonstrated that the GAGS inhibited C. albicans adherence to ECM and ECM proteins. This possibly occurred by the GAGS binding to the ECM proteins and, in so doing, masking a preferred ligand for C. albicans adherence.
Klotz
S A
SA
Department of Medicine, Veterans Administration Hospital, Kansas City, Missouri 64128.
Smith
R L
RL
D001665:Binding Sites; D002176:Candida albicans / Q000187:drug effects* / Q000378:metabolism*; D016264:Dextran Sulfate / Q000494:pharmacology; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006493:Heparin / Q000494:pharmacology; D006497:Heparan Sulfate / Q000494:pharmacology
D016264:Dextran Sulfate; D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans; D006493:Heparin; D006497:Heparan Sulfate