Phospholipase D activity is required for dimorphic transition in Candida albicans

McLain, Nealoo; Dolan, Joseph W.

doi:10.1099/00221287-143-11-3521

Cited by 42 publications

(42 citation statements)

References 45 publications

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“…Since C. albicans has not been shown to sporulate, we reasoned that a homologous phospholipase D1 in this fungus may have a different function. Earlier experiments from McLain & Dolan (1997) showed that at least one calcium-independent, phosphatidylinositol 4,5-bisphosphate-stimulated, oleatesensitive form of PLD1 exists in C. albicans. These studies also demonstrated that this enzyme was important to the process of dimorphic transition.…”

Section: Discussionmentioning

confidence: 99%

“…In fact, a PC-specific PLD activity providing PA, DAG and\or LPA, was shown to be involved in the yeast to hyphal transition (McLain & Dolan, 1997). The transition was stimulated by the addition of exogenous PLD.…”

Section: Introductionmentioning

confidence: 99%

“…Since PLD1 activity was stimulated by inducers of the dimorphic transition (McLain & Dolan, 1997), we questioned whether PLD1 is regulated during morphogenesis. Hyphal formation of C. albicans was induced by pH\temperature shift in Lee's medium (Buffo et al, 1984 were used as internal controls (Hube et al, 1994 ;Schaller et al, 1998).…”

Section: Pld1 In Vitro Expression Studiesmentioning

confidence: 99%

“…PLD1 activity has also been shown to increase during morphogenesis (McLain & Dolan, 1997). To investigate the relevance of PLD1 during growth and dimorphism, we produced mutants that lack functional copies of PLD1 (Fig.…”

Section: Pld1 Encodes a Phospholipase Dmentioning

confidence: 99%

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The role and relevance of phospholipase D1 during growth and dimorphism of Candida albicans

et al. 2001

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The phosphatidylcholine-specific phospholipase D1 (PLD1) in Saccharomyces cerevisiae is involved in vesicle transport and is essential for sporulation. The gene encoding the homologous phospholipase D1 from Candida albicans (PLD1) was used to study the role of PLD1 in this pathogenic fungus. In vitro and in vivo expression studies using Northern blots and reverse transcriptase-PCR showed low PLD1 mRNA levels in defined media supporting yeast growth and during experimental infection, while enhanced levels of PLD1 transcripts were detected during the yeast to hyphal transition. To study the relevance of PLD1 during yeast and hyphal growth, an essential part of the gene was deleted in both alleles of two isogenic strains. In vitro PLD1 activity assays showed that pld1 mutants produced no detectable levels of phosphatidic acid, the hydrolytic product of PLD1 activity, and strongly reduced levels of diacylglycerol, the product of lipid phosphate phosphohydrolase, suggesting no or a negligible background PLD1 activity in the pld1 mutants. The pld1 mutants showed no growth differences compared to the parental wild-type in liquid complex and minimal media, independent of the growth temperature. In addition, growth rates of pld1 mutants in media with protein as the sole source of nitrogen were similar to growth rates of the wild-type, indicating that secretion of proteinases was not reduced. Chlamydospore formation was normal in pld1 mutants. When germ tube formation was induced in liquid media, pld1 mutants showed similar rates of yeast to hyphal transition compared to the wild-type. However, no hyphae formation was observed on solid Spider medium, and cell growth on cornmeal/Tween 80 medium indicated aberrant morphogenesis. In addition, pld1 mutants growing on solid media had an attenuated ability to invade the agar. In a model of oral candidosis, pld1 mutants showed no attenuation of virulence. In contrast, the mutant was less virulent in two different mouse models. These data suggest that PLD1 is not essential for growth and oral infections. However, they also suggest that a prominent part of the phosphatidic acid and diacylglycerol pools is produced by PLD1 and that the level of these components is important for morphological transitions under certain conditions in C. albicans.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Pld1 In Vitro Expression Studiesmentioning

confidence: 99%

Section: Pld1 Encodes a Phospholipase Dmentioning

confidence: 99%

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The role and relevance of phospholipase D1 during growth and dimorphism of Candida albicans

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“…In addition, PIP # regulates the actin cytoskeleton by binding and regulating various actin-binding proteins (Janmey, 1994) such as profilin (DiNubile & Huang, 1997a, b), gelsolin and α-actinin (Fukami et al, 1992) in vertebrates. The modulation of the activity of other proteins is another function of PIP # : phospholipase D1 (PLD1) activity is stimulated by PIP # in mammalian (Liscovitch et al, 1994), Saccharomyces cerevisiae (Rose et al, 1995 ;Waksman et al, 1996) and Candida albicans cells (McLain & Dolan, 1997). Roles for proteins that contain a pleckstrin homology domain have also been described in PIP # signalling.…”

Section: Introductionmentioning

confidence: 99%

Phosphatidylinositol-4-phosphate 5-kinase activity is stimulated during temperature-induced morphogenesis in Candida albicans

2002

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(PA), which has been shown to activate PI4P5Ks in mammalian and Saccharomyces cerevisiae cells. In the present study, PI4P5K activity in the opportunistic pathogen Candida albicans was identified. A gene with significant sequence homology to the S. cerevisiae PI4P5K was cloned and designated MSS4. This gene was demonstrated to encode a functional PI4P5K by expression in S. cerevisiae. This enzyme was found to be membraneassociated and was stimulated by PA. Within the first 20 min after induction of polarized hyphal growth induced by a shift to elevated temperature, PI4P5K activity increased 25-fold. This stimulation was not observed when hyphae were induced by a combination of elevated temperature and serum. A lack of PLD1 activity resulted in the loss of induction of PI4P5K activity during the morphogenetic switch. Furthermore, the addition of propranolol attenuated the stimulation of PI4P5K activity during morphogenesis. These results suggest that PA derived from PLD1 activity stimulates C. albicans PI4P5K during the switch to the hyphal form under some conditions.

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Candida albicans: Clinical Relevance, Pathogenesis, and Host Immunity

Correia

Sampaio

Vilanova

et al. 2015

Human Emerging and Re‐emerging Infections

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Phospholipase D activity is required for dimorphic transition in Candida albicans

Cited by 42 publications

References 45 publications

The role and relevance of phospholipase D1 during growth and dimorphism of Candida albicans

The role and relevance of phospholipase D1 during growth and dimorphism of Candida albicans

Phosphatidylinositol-4-phosphate 5-kinase activity is stimulated during temperature-induced morphogenesis in Candida albicans

Candida albicans: Clinical Relevance, Pathogenesis, and Host Immunity

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