Cell extracts of Candida albicans block adherence of the organisms to endothelial cells.
Cell extracts of Candida albicans were fractionated by concanavalin A affinity chromatography. Eluted mannosylated proteins (fraction II) and nonbinding, nonmannosylated proteins (fraction I) were collected and assayed directly for inhibition of adherence of C. albicans to endothelium. Fraction II blocked blastospore adherence to endothelial cells. Fraction I blocked both blastospore and germ tube adherence to endothelial cells. Monoclonal antibody OKM-1 (anti-CR3) and an anti-C. albicans monoclonal antibody, CA-A (anti-CR2), reacted in Western blots with proteins from fraction I, suggesting the presence of the CR2- and CR3-like proteins that have been previously identified on C. albicans germ tubes.
Edwards
J E
JE
Department of Medicine, Harbor/UCLA Medical Center, Torrance 90509.
Mayer
C L
CL
Filler
S G
SG
Wadsworth
E
E
Calderone
R A
RA
D000268:Adhesiveness; D000944:Antigens, Differentiation, B-Lymphocyte / Q000502:physiology; D015153:Blotting, Western; D002176:Candida albicans / Q000737:chemistry*; D002473:Cell Wall / Q000502:physiology; D004730:Endothelium, Vascular / Q000382:microbiology*; D006801:Humans; D016177:Macrophage-1 Antigen / Q000502:physiology; D011951:Receptors, Complement / Q000502:physiology; D017464:Receptors, Complement 3d
D000944:Antigens, Differentiation, B-Lymphocyte; D016177:Macrophage-1 Antigen; D011951:Receptors, Complement; D017464:Receptors, Complement 3d