Aquaporin in Candida: characterization of a functional water channel protein
Copyright policy )Aquaporin in Candida: characterization of a functional water channel protein
AbstractThe Candida albicans genome database contains one ORF with homology to aquaporins, AQY1. Xenopus oocytes injected with cRNA encoding C. albicans Aqy1p displayed a coefficient of water permeability (Pf) that was equivalent to the Pf for oocytes injected with the cRNA of S. cerevisiae Aqy1p. In addition, as seen in Saccharomyces for Aqy1p and Aqy2p, deletion of AQY1 in C. albicans resulted in cells that were less sensitive than wild‐type to osmotic shock. In Saccharomyces, aquaporin null cells also have a cell surface that is more hydrophobic. However, unlike Saccharomyces, there was no effect on the cell surface hydrophobicity, flocculation or cell aggregation in aqy1 null C. albicans cells. Perhaps as a result, there was no difference between the virulence of C. albicans wild‐type and aqy1 null strains in a murine model for systemic candidiasis. Copyright © 2001 John Wiley & Sons, Ltd.
- Johns Hopkins Medicine United States
- Johns Hopkins University School of Medicine United States
Male, Mice, Inbred BALB C, Aquaporin 1, Sequence Homology, Amino Acid, Virulence, Surface Properties, Molecular Sequence Data, Candidiasis, Aquaporins, Disease Models, Animal, Mice, Osmotic Pressure, Candida albicans, Animals, Biological Assay, Female, Amino Acid Sequence, Sequence Alignment
Male, Mice, Inbred BALB C, Aquaporin 1, Sequence Homology, Amino Acid, Virulence, Surface Properties, Molecular Sequence Data, Candidiasis, Aquaporins, Disease Models, Animal, Mice, Osmotic Pressure, Candida albicans, Animals, Biological Assay, Female, Amino Acid Sequence, Sequence Alignment
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