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Secretome analysis of Candida glabrata wild-type and aspartyl protease-deficient strains

ABSTRACT: The project is aimed at characterizing the secretome of a human opportunistic fungal pathogen Candida glabrata. Additionally, the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the Candida glabrata secretome is studied.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Candida Glabrata (yeast) (torulopsis Glabrata)

SUBMITTER: Rupinder Kaur

LAB HEAD: Rupinder Kaur

PROVIDER: PXD015131 | Pride | 2019-10-25

REPOSITORIES: Pride

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Publications

Global Secretome Characterization of the Pathogenic Yeast <i>Candida glabrata</i>.

Rasheed Mubashshir M Kumar Naveen N Kaur Rupinder R

Journal of proteome research 20191101 1

Secretory proteins are key modulators of host-pathogen interaction. The human opportunistic fungal pathogen <i>Candida glabrata</i> lacks secreted proteolytic activity but possesses 11 glycosylphosphatidylinositol-anchored aspartyl proteases, also referred to as Yapsins (CgYps1-11), that are essential for its virulence. To delineate the role of CgYapsins in interaction with host cells, we have profiled, through liquid chromatography-tandem mass spectrometry (LC-MS/MS) approach, the total secreto ...[more]

PMID: 31621333

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Total membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.

Project description:The project is aimed at characterizing the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the global membrane proteome of Candida glabrata.

2022-04-04 | PXD029614 | Pride

Label-free quantitative total membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.

Project description:The project is aimed at characterizing the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the abundance of proteins in the total membrane factions of Candida glabrata.

2022-04-04 | PXD029629 | Pride

Quantitative secretome profiling of Candida glabrata wild-type and aspartyl protease-deficient strains

Project description:The project is aimed at deciphering the proteins, which are differentially abundant in the secretome of Candida glabrata wild-type and a mutant strain deleted for eleven cell surface-associated aspartyl-proteases (CgYapsins).

2019-10-24 | PXD015147 | Pride

Secretome analysis of Candida glabrata aspartyl protease-deficient strains

Project description:The project is aimed at characterizing the effect of deletion of surface associated aspartyl protease(s) on the secretome of of the human opportunistic fungal pathogen Candida glabrata.

2019-10-24 | PXD015132 | Pride

Response of Candida glabrata to low pH

Project description:To examine the role of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata, transcriptional profiling analysis was carried out on wild-type and Cgyps1∆ cells grown in YNB medium (pH 5.5) and in YNB medium adjusted to pH 2.0. Genes involved in carbohydrate and amino acid metabolism, protein folding and stress response pathways were found to be differentially regulated in response to acidic environment in both the strains. To examine the role of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata, transcriptional profiling analysis was carried out on wild-type and Cgyps1∆ delta cells grown in YNB medium (pH 5.5) and in YNB medium adjusted to pH2.0. Genes involved in carbohydrate and amino acid metabolism, protein folding and stress response pathways were found to be differentially regulated in response to acidic environment in both the strains Agilent one-color experiment,Organism: Yeast ,Agilent-026378 Genotypic designed Custom Candida glabrata 8x15k , Labeling kit: Agilent Quick-Amp labeling

2011-01-10 | E-GEOD-24267 | biostudies-arrayexpress

Interactome identification of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the pathogenic yeast Candida glabrata

Project description:The major goal of this project is to identify proteins that interact with CgYps1 aspartyl protease in logarithmic-phase Candida glabrata cells.

2021-02-08 | PXD022766 | Pride

Candida glabrata GPI-anchored cell surface associated aspartyl protease CgYps1 and CgYps7 interactome analysis in the total cell extracts of A-498 human renal epithelial cell line

Project description:The project is aimed at identifying host epithelial proteins that interact with two different cell-surface associated aspartyl proteases (CgYps1 and CgYps7) in Candida glabrata cells.

2024-08-22 | PXD053938 | Pride

Long-term exposure of Candida glabrata to human monocyte-derived macrophages, with long-term medium growth controls

Project description:Candida glabrata were kept within human moncoyte-derived macrophages (MDM) for up to seven days to investigate the transcriptome of long-term residence within phagosomes. Samples were taken after 6h and 1, 2, 4, and 7 days. To control for general starvation, long-term exposure data for the growth media YPD, SD, and RPMI (with serum) were included. Experiments were performed as a common reference design, with log-phase YPD growth as Cy3-labeled reference for all arrays.

2023-05-31 | E-MTAB-11801 | biostudies-arrayexpress

Phosphatidylinositol 3-phosphate (PI3P) interactome analysis under varied iron conditions in Candida glabrata.

Project description:The project is aimed at identifying proteins that interact with PI3P in low-iron, regular-iron and high-iron grown Candida glabrata cells.

2024-02-19 | PXD042058 | Pride

Expression analysis of Candida glabrata CBS138 delta-cnb1, delta-crz1, delta-slt2, and delta-ire1 mutants in response to tunicamycin exposure (Transcriptional response of Candida glabrata to tunicamycin exposure)

Project description:Investigation of whole genome gene expression level changes in response to tunicamycin, an inhibitor of protein N-glycosylation, in Candida glabrata CBS138 delta-cnb1, delta-crz1, delta-slt2, and delta-ire1 mutants, compared to the wild-type strain. The mutations engineered into these strains render them hypersusceptible to tunicamycin. The mutants analyzed in this study are further described in Miyazaki, T. et al. (2010) Antimicrob Agents Chemother. 54(4):1639-1643 (PMID: 20100876) and Miyazaki, T. et al. (2010) FEMS Yeast Res 10(3):343-352, 2010 (PMID: 20214686). A fifteen chip study using total RNA isolated from Candida glabrata wild-type control and four mutant strains, in which the entire ORFs of CNB1 (XP_448800), CRZ1 (XP_449644), SLT2 (XP_447735), or IRE1 (XP_446111) are deleted. Each chip measures the expression level of 5,217 genes from Candida glabrata CBS138 with six 60-mer-probe pairs per gene, with two-fold technical redundancy.

2013-05-31 | E-GEOD-29855 | biostudies-arrayexpress

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