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MYCOLOGY |
Department of Dermatology and Allergology, Ludwig-Maximilians-University Munich, Munich, Germany
Corresponding author: Dr M. Schaller (e-mail: Martin.Schaller{at}lrz.uni-muenchen.de).
Received 29 Sept. 2000; revised version accepted 20 Feb. 2001.
Abstract
Distinct isoforms of secreted aspartyl proteinases (Sap) of Candida albicans are important virulence factors for different types of candidosis. Predominant expression of Sap13 has been shown to be crucial for superficial infections in experimental mucosal and cutaneous candidosis, whereas Sap46 might be important for systemic disease. This in-vivo study investigated Sap expression in two samples from patients with oral candidosis and from cutaneous infection. Two different polyclonal antibodies directed against Sap13 and Sap46 were used for ultrastructural characterisation of protein localisation and expression. Post-embedding immuno-electron microscopy revealed Sap13 and Sap46 immunoreactivity in all samples. All C. albicans cells expressed predominantly the proteinases Sap13 which were evenly distributed within the cell wall and cytoplasmic membrane. In contrast, Sap46 labelling was only evident in a few fungal cells. In particular it was localised at the tips of hyphal cells during invasion. These data suggest a different pathogenetic role for Sap13 and Sap46 during hostfungal interaction.
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