Secreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells.
The endothelial cell interactions of homozygous null mutants of Candida albicans that were deficient in secreted aspartyl proteinase 1 (Sap1), Sap2, or Sap3 were investigated. Only Sap2 was found to contribute to the ability of C. albicans to damage endothelial cells and stimulate them to express E-selectin. None of the Saps studied appears to play a role in C. albicans adherence to endothelial cells.
Ibrahim
A S
AS
Division of Infectious Diseases, St. John's Cardiovascular Research Center, Department of Medicine, Harbor-UCLA Research and Education Institute, Torrance, California 90509, USA. Ibrahim@AFP76.HUMC.EDU
Filler
S G
SG
Sanglard
D
D
Edwards
J E
JE
Hube
B
B
D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D002176:Candida albicans / Q000201:enzymology / Q000472:pathogenicity*; D002448:Cell Adhesion; D019040:E-Selectin / Q000096:biosynthesis; D004730:Endothelium, Vascular / Q000382:microbiology* / Q000473:pathology; D005656:Fungal Proteins / Q000378:metabolism*; D006801:Humans
D019040:E-Selectin; D005656:Fungal Proteins; D016282:Aspartic Acid Endopeptidases; C086390:SAP1 protein, Candida albicans; C090753:SAP2 protein, Candida; C090754:SAP3 protein, Candida albicans