title: Secreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells.
abstract: 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.
authors.affiliation: 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
authors.forename: A S
authors.initials: AS
authors.lastname: Ibrahim
authors.forename: S G
authors.initials: SG
authors.lastname: Filler
authors.forename: D
authors.initials: D
authors.lastname: Sanglard
authors.forename: J E
authors.initials: JE
authors.lastname: Edwards
authors.forename: B
authors.initials: B
authors.lastname: Hube
mesh_terms: 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
chemical_list: D019040:E-Selectin; D005656:Fungal Proteins; D016282:Aspartic Acid Endopeptidases; C086390:SAP1 protein, Candida albicans; C090753:SAP2 protein, Candida; C090754:SAP3 protein, Candida albicans