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Effect of the echinocandin caspofungin on expression of Candida albicans secretory aspartyl proteinases and phospholipase in vitro.
- Source :
-
Antimicrobial agents and chemotherapy [Antimicrob Agents Chemother] 2002 Sep; Vol. 46 (9), pp. 3096-100. - Publication Year :
- 2002
-
Abstract
- Although the echinocandin caspofungin primarily inhibits the synthesis of cell wall 1,3-beta-D-glucan, its fungicidal activity could also potentially perturb the expression of virulence factors involved in the ability of Candida albicans to cause infection. Expression of the C. albicans secretory aspartyl proteinase (SAP) and phospholipase B (PLB) virulence genes was determined by reverse transcription-PCR after the addition of caspofungin to cells grown for 15 h in Sabouraud dextrose broth. In cells that remained viable, expression of SAP1 to SAP3, SAP7 to SAP9, and PLB1 was unaltered after exposure to fungicidal concentrations (4 to 16 micro g/ml) of caspofungin over a period of 7 h. However, expression of SAP5 increased steadily beginning 1 h after exposure to caspofungin. These results indicate that caspofungin is rapidly fungicidal against C. albicans, before any suppression of SAP or PLB1 gene expression can occur.
- Subjects :
- Aspartic Acid Endopeptidases genetics
Candida albicans drug effects
Candida albicans genetics
Caspofungin
Echinocandins
Genes, Fungal genetics
Lipopeptides
Microbial Sensitivity Tests
Phospholipases genetics
RNA, Fungal biosynthesis
RNA, Fungal genetics
RNA, Messenger biosynthesis
RNA, Messenger genetics
Reverse Transcriptase Polymerase Chain Reaction
Time Factors
Anti-Bacterial Agents pharmacology
Antifungal Agents pharmacology
Aspartic Acid Endopeptidases biosynthesis
Candida albicans enzymology
Gene Expression Regulation, Enzymologic drug effects
Peptides
Peptides, Cyclic
Phospholipases biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 0066-4804
- Volume :
- 46
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Antimicrobial agents and chemotherapy
- Publication Type :
- Academic Journal
- Accession number :
- 12183282
- Full Text :
- https://doi.org/10.1128/AAC.46.9.3096-3100.2002