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

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