Timpel, Claudia and Strahl-Bolsinger, Sabine and Ziegelbauer, Karl and Ernst, Joachim F. (1998) Multiple functions of Pmt1p-mediated protein O-mannosylation in the fungal pathogen Candida albicans. JOURNAL OF BIOLOGICAL CHEMISTRY, 273 (33). pp. 20837-20846. ISSN 0021-9258, 1083-351X
Full text not available from this repository. (Request a copy)Abstract
Protein mannosylation by Pmt proteins initiates O-glycosylation in fungi, We have identified the PMT1 gene and analyzed the function of Pmt1p in the fungal human pathogen Candida albicans. Mutants defective in PMT1 alleles lacked Pmt in vitro enzymatic activity, showed reduced growth rates, and tended to for-m cellular aggregates. In addition, multiple specific deficiencies not known in Saccharomyces cerevisiae (including defective hyphal morphogenesis; supersensitivity to the antifungal agents hygromycin B, G418, clotrimazole, and calcofluor white; and reduced adherence to Caco-2 epithelial cells) were observed in pmt1 mutants. PMT1 deficiency also led to faster electrophoretic mobility of the Als1p cell wall protein and to elevated extracellular activities of chitinase. Homozygous pmt1 mutants were avirulent in a mouse model of systemic infection, while heterozygous PMT1/pmt1 strains showed reduced virulence. The results indicate that protein O-mannosylation by Pmt proteins occurs in different fungal species, where PMT1 deficiency can lead to defects in multiple cellular functions.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | YEAST SACCHAROMYCES-CEREVISIAE; ENDOTHELIAL-CELLS; HYPHAL FORMATION; GENE FAMILY; GLYCOSYLATION; MUTANTS; MANNOSYLTRANSFERASE; VIRULENCE; GROWTH; OLIGOSACCHARIDES |
| Subjects: | 500 Science > 570 Life sciences 500 Science > 580 Botanical sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 16 Feb 2023 10:48 |
| Last Modified: | 16 Feb 2023 10:48 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49597 |
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