A gene encoding phosphatidyl inositol-specific phospholipase C from Cryphonectria parasitica modulates the lac1 expression

Chung, Hea-Jong; Kim, Myoung-Ju; Lim, Jin-Young; Park, Seung-Moon; Cha, Byeongjin; Kim, Young‐Ho; Yang, Moon-Sik; Kim, Dae-Hyuk

doi:10.1016/j.fgb.2005.12.009

Cited by 25 publications

(18 citation statements)

References 45 publications

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“…Our previous findings established that, similar to other fungal species, C. neoformans calcineurin is activated by the addition of exogenous calcium to the growth medium (12). Furthermore, in filamentous fungi, addition of calcium restored some of the defects observed in the ⌬plc1 mutant, such as growth rate in Cryphonectria parasitica, and formation of infection structures (appressoria) in Magnaporthe oryzae (26,27). In S. cerevisiae, addition of calcium to the medium allowed the ⌬plc1 mutant to grow at 38°C (28).…”

Section: Figsupporting

confidence: 65%

Phospholipase C of Cryptococcus neoformans Regulates Homeostasis and Virulence by Providing Inositol Trisphosphate as a Substrate for Arg1 Kinase

Lev

Desmarini

et al. 2013

Infect Immun

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dPhospholipase C (PLC) of Cryptococcus neoformans (CnPlc1) is crucial for virulence of this fungal pathogen. To investigate the mechanism of CnPlc1-mediated signaling, we established that phosphatidylinositol 4,5-bisphosphate (PIP 2 ) is a major CnPlc1 substrate, which is hydrolyzed to produce inositol trisphosphate (IP 3 ). In Saccharomyces cerevisiae, Plc1-derived IP 3 is a substrate for the inositol polyphosphate kinase Arg82, which converts IP 3 to more complex inositol polyphosphates. In this study, we show that in C. neoformans, the enzyme encoded by ARG1 is the major IP 3 kinase, and we further demonstrate that catalytic activity of Arg1 is essential for cellular homeostasis and virulence in the Galleria mellonella infection model. IP 3 content was reduced in the Cn⌬plc1 mutant and markedly increased in the Cn⌬arg1 mutant, while PIP 2 was increased in both mutants. The Cn⌬plc1 and Cn⌬arg1 mutants shared significant phenotypic similarity, including impaired thermotolerance, compromised cell walls, reduced capsule production and melanization, defective cell separation, and the inability to form mating filaments. In contrast to the S. cerevisiae ARG82 deletion mutant (Sc⌬arg82) strain, the Cn⌬arg1 mutant exhibited dramatically enlarged vacuoles indicative of excessive vacuolar fusion. In mammalian cells, PLC-derived IP 3 causes Ca 2؉ release and calcineurin activation. Our data show that, unlike mammalian PLCs, CnPlc1 does not contribute significantly to calcineurin activation. Collectively, our findings provide the first evidence that the inositol polyphosphate anabolic pathway is essential for virulence of C. neoformans and further show that production of IP 3 as a precursor for synthesis of more complex inositol polyphosphates is the key biochemical function of CnPlc1.

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Section: Figsupporting

confidence: 65%

Phospholipase C of Cryptococcus neoformans Regulates Homeostasis and Virulence by Providing Inositol Trisphosphate as a Substrate for Arg1 Kinase

Lev

Desmarini

et al. 2013

Infect Immun

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“…1c). Calcium signaling has also been shown to be modulated by hypovirus infection (Allen et al, 2003;Allen and Nuss, 2004;Chung et al, 2006;Larson et al, 1992).…”

Section: Genes Involved In Key Signaling Pathways In C Parasiticamentioning

confidence: 99%

Large-scale expressed sequence tag analysis for the chestnut blight fungus Cryphonectria parasitica

Shang

Lan

et al. 2008

Fungal Genetics and Biology

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“…Notably, the mouse PLC-d1 gene is able to suppress MoPLC1 deletion-mediated defects, supporting the importance of PLC-mediated signaling in fungal development. From the MoPLC1 study, we noticed that the two characterized fungal PLCs from Neurospora crassa (Gavric et al, 2007) and Cryphonectria parasitica (Chung et al, 2006) lack the PH domain present in MoPLC1, which suggests that M. oryzae may have multiple forms of PLC. These structural differences in the characterized PLCs prompted us to search for additional copies in the genome database (http://www.broad.mit.edu/annotation/ fungi/magnaporthe).…”

Section: Introductionmentioning

confidence: 99%

Differential roles of the phospholipase C genes in fungal development and pathogenicity of Magnaporthe oryzae

Choi

Kim

Rho

et al. 2011

Fungal Genetics and Biology

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A gene encoding phosphatidyl inositol-specific phospholipase C from Cryphonectria parasitica modulates the lac1 expression

Cited by 25 publications

References 45 publications

Phospholipase C of Cryptococcus neoformans Regulates Homeostasis and Virulence by Providing Inositol Trisphosphate as a Substrate for Arg1 Kinase

Phospholipase C of Cryptococcus neoformans Regulates Homeostasis and Virulence by Providing Inositol Trisphosphate as a Substrate for Arg1 Kinase

Large-scale expressed sequence tag analysis for the chestnut blight fungus Cryphonectria parasitica

Differential roles of the phospholipase C genes in fungal development and pathogenicity of Magnaporthe oryzae

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