The vesicle transport protein Vac1p is required for virulence of Candida albicans

被引:24
|
作者
Franke, Kathrin
Nguyen, Monika
Haertl, Albert
Dahse, Hans-Martin
Vogl, Georgia
Wuerzner, Reinhard
Zipfel, Peter F.
Kuenkel, Waldemar
Eck, Raimund
机构
[1] Univ Appl Sci, Dept Med Engn, D-07745 Jena, Germany
[2] Hans Knoell Inst, Leibniz Inst Nat Prod Res & Infect Biol, Dept Infect Biol, D-07745 Jena, Germany
[3] Dept Hyg Microbiol & Social Med, A-6020 Innsbruck, Austria
来源
MICROBIOLOGY-SGM | 2006年 / 152卷
关键词
D O I
10.1099/mic.0.29115-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The putative vesicle transport protein Vac1p of the human pathogenic yeast Candida albicans plays an important role in virulence. To determine the cellular functions of Vac1p, a null mutant was generated by sequential disruption of both alleles. The vac1 null mutant strain showed defective endosomal vesicle transport, demonstrating a role of Vac1p in protein transport to the vacuole. Vac1p also contributes to resistance to metal ions, as the null mutant strain was hypersensitive to Cu2+, Zn2+ and Ni2+. In addition, the loss of Vac1p affected several virulence factors of C. albicans. In particular, the vac1 null mutant strain showed defective hyphal growth, even when hyphal formation was induced via different pathways. Furthermore, Vac1p affects chlamydospore formation, adherence to human vaginal epithelial cells, and the secretion of aspartyl proteinases (Saps). Avirulence in a mouse model of systemic infection of the vac1 null mutant strongly suggests that Vac1p of C. albicans is essential for pathogenicity. In summary, the Vac1p protein is required for several cellular pathways, in particular those that control virulence and pathogenicity. Consequently, Vac1p is a novel and interesting target for antifungal drugs.
引用
收藏
页码:3111 / 3121
页数:11
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