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Secretome analysis of Candida glabrata aspartyl protease-deficient strains

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

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

SUBMITTER: Rupinder Kaur

LAB HEAD: Rupinder Kaur

PROVIDER: PXD015132 | Pride | 2019-10-24

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

Project description: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.

2019-10-25 | PXD015131 | 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

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

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

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

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

Candida glabrata transcription profile when grown under Niacin starvation or in human urine

Project description:The transcription profile of Candida glabrata grown under two different Niacin limitation conditions were determined. Condition 1 is comparing log phase C. glabrata cells (O.D. 0.5-0.6) grown in synthetic medium containing 0.016 uM versus 3.25 uM nicotinic acid (NA), a common form of Niacin. The NA concentration of 3.25 uM is the standard concentration in synthetic complete (SC) medium. Condition 2 is comparing log phase C. glabrata cells (O.D. 0.4-0.6) grown in 3 individual human urine samples (supplemented with 2% glucose) versus in SC medium. Keywords: transcriptional profiling by microarray GSM151863, GSM151869 are dye-swap experiment #1 and GSM151880, GSM151881 are dye-swap experiment #2 for Niacin limitation condition 1. GSM151934, GSM152116 are dye-swap experiment #1, GSM152118, GSM152119 are dye-swap experiment #2 and GSM152130, GSM152131 are dye-swap experiment #3 for Niacin limitation condition 2.

2010-06-05 | E-GEOD-6582 | biostudies-arrayexpress

Proteomic profiling of Biomphalaria glabrata plasma proteins

Project description:Proteomic profiling of Biomphalaria glabrata plasma proteins with binding affinity to those expressed by early developing larval Schistosoma mansoni

2017-01-05 | PXD004942 | 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

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