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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aspartic Acid Endopeptidases / metabolism*
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Candida albicans / enzymology
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Candida albicans / pathogenicity*
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Cell Adhesion
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E-Selectin / biosynthesis
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Endothelium, Vascular / microbiology*
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Endothelium, Vascular / pathology
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Fungal Proteins / metabolism*
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Humans
Substances
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E-Selectin
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Fungal Proteins
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Aspartic Acid Endopeptidases
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SAP1 protein, Candida albicans
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SAP2 protein, Candida
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SAP3 protein, Candida albicans