Abstract
The vacuole of Candida albicans plays a significant role in many processes including homeostasis control, cellular trafficking, dimorphic switching, and stress tolerance. Thus, understanding the factors affecting vacuole function is important for the identification of new drug targets needed in response to the world’s increasing levels of invasive infections and the growing issue of fungal drug resistance. Past studies have shown that vacuolar proton-translocating ATPases (V-ATPases) play a central role in pH homeostasis and filamentation. Vacuolar protein sorting components (VPS) regulate V-ATPases assembly and at the same time affect hyphal development. As well, vacuolar calcium exchange systems like Yvc1 and Pmc1 maintain cytosolic calcium levels while being affected by V-ATPases function. All these proteins play a role in the virulence and pathogenesis of C. albicans. This review highlights the relationships among V-ATPases, VPS, and vacuolar calcium exchange proteins while summarizing their importance in C. albicans infections.
Highlights
Candida albicans is an opportunistic fungal pathogen generating a high rate of mortality in systemic infections (Jenks et al, 2020)
Vacuolar function changes can have profound effects on the virulence of C. albicans, and targeting the vacuolar function of C. albicans may provide a new strategy for the development of antifungal drugs (Olsen, 2014)
VPH2 encodes the homologue of Vma12, which is one of the V-ATPases assembly factors, TABLE 1 | Genes encoding the subunits of V-ATPases and their null mutant phenotypes in C. albicans
Summary
Candida albicans is an opportunistic fungal pathogen generating a high rate of mortality in systemic infections (Jenks et al, 2020). The deletion of Tfp1, the putative C. albicans homologue of S. cerevisiae Vma1, can cause a defect in vacuolar acidification and strongly reduces virulence (Jia et al, 2014). VPH2 encodes the homologue of Vma12, which is one of the V-ATPases assembly factors, TABLE 1 | Genes encoding the subunits of V-ATPases and their null mutant phenotypes in C. albicans.
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