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. 1998 Jun;66(6):3003-5.
doi: 10.1128/IAI.66.6.3003-3005.1998.

Secreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells

A S Ibrahim  1 , S G Filler, D Sanglard, J E Edwards Jr, B Hube
Affiliations

Secreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells

A S Ibrahim et al. Infect Immun. 1998 Jun.

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.

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Figures

FIG. 1
FIG. 1
Endothelial cell injury caused by C. albicans SC5314, a sap2 null mutant (Sap2), and the SAP2 revertant (M41). Results are the mean ± standard deviation of nine determinations. ∗, P < 0.01. The data were analyzed by analysis of variance and corrected for multiple comparisons with the Bonferroni correction.
FIG. 2
FIG. 2
Adherence of C. albicans SC5314, a sap2 null mutant (Sap2), and the SAP2 revertant (M41) to endothelial cells. Results are the mean ± standard deviation of nine determinations. ∗, P < 0.0001. The data were analyzed by analysis of variance and corrected for multiple comparisons with the Bonferroni correction.
FIG. 3
FIG. 3
Endothelial cell E-selectin expression (optical density at 490 nm [OD490]) in response to medium alone (−), C. albicans SC5314, or the proteinase mutants. Results are the mean ± standard deviation of at least nine determinations. ∗, P = 0.01. The data were analyzed by analysis of variance and corrected for multiple comparisons with the Bonferroni correction.
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