Phospholipases play multiple cellular roles including growth, stress tolerance, sexual development, and virulence in fungi

Barman, Ananya; Gohain, Dibakar; Bora, Utpal; Tamuli, Ranjan

doi:10.1016/j.micres.2017.12.012

Cited by 61 publications

(31 citation statements)

References 199 publications

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“…Glycerophospholipid is the main lipid of the membrane bilayer and plays an important role in response to environmental stress (44,45). For example, cells lacking PLB1, which is critical for the remodeling of membrane phospholipids, showed sensitivity to osmotic stress (46). Moreover, overexpression of OLE1, encoding delta-9 desaturase to generate unsaturated fatty acids in Saccharomyces cerevisiae, activated the MAPK HOG pathway, thereby enhancing the tolerance to osmotic stress (8).…”

Section: Discussionmentioning

confidence: 99%

Cg Hog1-Mediated Cg Rds2 Phosphorylation Alters Glycerophospholipid Composition To Coordinate Osmotic Stress in Candida glabrata

Zhang

Zhu

et al. 2019

Appl Environ Microbiol

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Under stress conditions, Hog1 is required for cell survival through transiently phosphorylating downstream targets and reprogramming gene expression. Here, we report that Candida glabrata Hog1 (CgHog1) interacts with and phosphorylates CgRds2, a zinc cluster transcription factor, in response to osmotic stress. Additionally, we found that deletion of CgRDS2 led to decreases in cell growth and cell survival by 23.4% and 39.6%, respectively, at 1.5 M NaCl, compared with levels of the wild-type strain. This is attributed to significant downregulation of the expression levels of glycerophospholipid metabolism genes. As a result, the content of total glycerophospholipid decreased by 30.3%. Membrane integrity also decreased 47.6% in the Cgrds2Δ strain at 1.5 M NaCl. In contrast, overexpression of CgRDS2 increased the cell growth and cell survival by 10.2% and 6.3%, respectively, owing to a significant increase in the total glycerophospholipid content and increased membrane integrity by 27.2% and 12.1%, respectively, at 1.5 M NaCl, compared with levels for the wild-type strain. However, a strain in which the CgRDS2 gene encodes the replacement of Ser64 and Thr97 residues with alanines (Cgrds22A), harboring a CgRds2 protein that was not phosphorylated by CgHog1, failed to promote glycerophospholipid metabolism and membrane integrity at 1.5 M NaCl. Thus, the above results demonstrate that CgHog1-mediated CgRds2 phosphorylation enhanced glycerophospholipid composition and membrane integrity to resist osmotic stress in C. glabrata. IMPORTANCE This study explored the role of CgHog1-mediated CgRds2 phosphorylation in response to osmotic stress in Candida glabrata. CgHog1 interacts with and phosphorylates CgRds2, a zinc cluster transcription factor, under osmotic stress. Phosphorylated CgRds2 plays an important role in increasing glycerophospholipid composition and membrane integrity, thereby enhancing cell growth and survival.

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Section: Discussionmentioning

confidence: 99%

Cg Hog1-Mediated Cg Rds2 Phosphorylation Alters Glycerophospholipid Composition To Coordinate Osmotic Stress in Candida glabrata

Zhang

Zhu

et al. 2019

Appl Environ Microbiol

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“…During the infection of mammalian hosts, phospholipase enzymes released by fungi can play important roles in tissue invasion and nutrient acquisition [49,50]. In A. fumigatus , two phospholipase B ( plb ) genes ( Afplb1 and Afplb2 ) encode two secreted PLB and are upregulated in the presence of the major component of lung surfactant (DPPC) [44,50], substrate analyzed as substrate in the present work.…”

Section: Discussionmentioning

confidence: 99%

Non-Mammalian Prdx6 Enzymes (Proteins with 1-Cys Prdx Mechanism) Display PLA2 Activity Similar to the Human Orthologue

et al. 2019

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Mammalian peroxiredoxin class 6 (Prdx6) are bifunctional enzymes. Non-mammalian Prdx6 enzymes display Cys-based peroxidase activity, but to date their putative phospholipase A2 (PLA2 activities) has not been experimentally investigated. Initially, we observed that five non-mammalian Prdx6 enzymes (enzymes from Arabidopsis thaliana (AtPER1), Triticum aestivum (TaPER1), Pseudomonas aeruginosa (PaLsfA) and Aspergillus fumigatus (AfPrx1 and AfPrxC)) present features compatible with PLA2 activities in mammalian Prdx6 by amino acid sequences alignment and tertiary structure modeling. Employing unilamellar liposomes with tracer amounts of [3H]-1,2-Dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and thin layer chromatography, all the tested non-mammalian Prdx6 enzymes displayed PLA2 activities, with values ranging from 3.4 to 6.1 nmol/min/mg protein. It was previously shown that Thr177 phosphorylation of human Prdx6 increases its PLA2 activity, especially at neutral pH. Therefore, we investigated if human Erk2 kinase could also phosphorylate homologous Thr residues in non-mammalian Prdx6 proteins. We observed phosphorylation of the conserved Thr in three out of the five non-mammalian Prdx enzymes by mass spectrometry. In the case of the mitochondrial Prdx6 from A. fumigatus (AfPrxC), we also observed phosphorylation by western blot, and as a consequence, the PLA2 activity was increased in acidic and neutral conditions by the human Erk2 kinase treatment. The possible physiological meanings of these PLA2 activities described open new fields for future research.

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“…The main function of PLC is to generate IP 3 which activates Ca 2+ channels (Lew et al, 2015;Singh et al, 2015). In many fungi, PLC mediates various aspects of fungal development, including conidium and appressorium formation, hyphal extension and branching, and fungal pathogenicity (Oh et al, 2012;Zhu et al, 2015;Barman et al, 2018). A wide range of pharmacological agents have been used to disrupt Ca 2+ influxes or to interfere with Ca 2+ -binding proteins.…”

Section: Introductionmentioning

confidence: 99%

Phospholipase C From Alternaria alternata Is Induced by Physiochemical Cues on the Pear Fruit Surface That Dictate Infection Structure Differentiation and Pathogenicity

Huang

et al. 2020

Front. Microbiol.

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To investigate the mechanisms of phospholipase C (PLC)-mediated calcium (Ca 2+) signaling in Alternaria alternata, the regulatory roles of PLC were elucidated using neomycin, a specific inhibitor of PLC activity. Three isotypes of PLC designated AaPLC1, AaPLC2, and AaPLC3 were identified in A. alternata through genome sequencing. qRT-PCR analysis showed that fruit wax extracts significantly upregulated the expression of all three PLC genes in vitro. Pharmacological experiments showed that neomycin treatment led to a dose-dependent reduction in spore germination and appressorium formation in A. alternata. Appressorium formation was stimulated on hydrophobic and pear wax-coated surfaces but was significantly inhibited by neomycin treatment. The appressorium formation rates of neomycin treated A. alternata on hydrophobic and wax-coated surfaces decreased by 86.6 and 47.4%, respectively. After 4 h of treatment, exogenous CaCl 2 could partially reverse the effects of neomycin treatment. Neomycin also affected mycotoxin production in alternariol (AOH), alternariol monomethyl ether (AME), altenuene (ALT), and tentoxin (TEN), with exogenous Ca 2+ partially reversing these effects. These results suggest that PLC is required for the growth, infection structure differentiation, and secondary metabolism of A. alternata in response to physiochemical signals on the pear fruit surface.

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Phospholipases play multiple cellular roles including growth, stress tolerance, sexual development, and virulence in fungi

Cited by 61 publications

References 199 publications

Cg Hog1-Mediated Cg Rds2 Phosphorylation Alters Glycerophospholipid Composition To Coordinate Osmotic Stress in Candida glabrata

Cg Hog1-Mediated Cg Rds2 Phosphorylation Alters Glycerophospholipid Composition To Coordinate Osmotic Stress in Candida glabrata

Non-Mammalian Prdx6 Enzymes (Proteins with 1-Cys Prdx Mechanism) Display PLA2 Activity Similar to the Human Orthologue

Phospholipase C From Alternaria alternata Is Induced by Physiochemical Cues on the Pear Fruit Surface That Dictate Infection Structure Differentiation and Pathogenicity

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